l2
SMART MODE:

NORMAL GENOMIC

SMART

Letunic et al. (2017) Nucleic Acids Res doi: 10.1093/nar/gkx922
Letunic et al. (2020) Nucleic Acids Res doi: 10.1093/nar/gkaa937

14_3_3

14-3-3 homologues
14_3_3
SMART accession number:SM00101
Description: 14-3-3 homologues mediates signal transduction by binding to phosphoserine-containing proteins. They are involved in growth factor signalling and also interact with MEK kinases.
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There are 6285 14_3_3 domains in 6269 proteins in SMART's nrdb database.

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4.1m

putative band 4.1 homologues' binding motif
4.1m
SMART accession number:SM00294
Description: -
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acidPPc

Acid phosphatase homologues
acidPPc
SMART accession number:SM00014
Description: -
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ADF

Actin depolymerisation factor/cofilin -like domains
ADF
SMART accession number:SM00102
Description: Severs actin filaments and binds to actin monomers.
GO function:actin binding (GO:0003779)
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ANK

ankyrin repeats
ANK
SMART accession number:SM00248
Description: Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
GO function:protein binding (GO:0005515)
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APCDDC

Adenomatosis polyposis coli down-regulated 1
APCDDC
SMART accession number:SM01352
Description: The domain is duplicated in most members of this family. APCDD is directly regulated by the beta-catenin/Tcf complex, and its elevated expression promotes proliferation of colonic epithelial cells in vitro and in vivo (PMID:12384519). APCDD1 has an N-terminal signal-peptide and a C-terminal transmembrane region. The domain is rich in cysteines, there being up to 12 such residues, a structural motif important for interaction between Wnt ligands and their receptors. APCDD1 is expressed in a broad repertoire of cell types, indicating that it may regulate a diverse range of biological processes controlled by Wnt signalling (PMID:20393562).
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ARF

ARF-like small GTPases; ARF, ADP-ribosylation factor
ARF
SMART accession number:SM00177
Description: Ras homologues involved in vesicular transport. Activator of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. ARFs are N-terminally myristoylated. Contains ATP/GTP-binding motif (P-loop).
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ArfGap

Putative GTP-ase activating proteins for the small GTPase, ARF
ArfGap
SMART accession number:SM00105
Description: Putative zinc fingers with GTPase activating proteins (GAPs) towards the small GTPase, Arf. The GAP of ARD1 stimulates GTPase hydrolysis for ARD1 but not ARFs.
GO function:GTPase activator activity (GO:0005096)
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ARM

Armadillo/beta-catenin-like repeats
ARM
SMART accession number:SM00185
Description: Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.
GO function:protein binding (GO:0005515)
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B41

Band 4.1 homologues
B41
SMART accession number:SM00295
Description: Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.
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B561

Cytochrome b-561 / ferric reductase transmembrane domain.
B561
SMART accession number:SM00665
Description: Cytochrome b-561 recycles ascorbate for the generation of norepinephrine by dopamine-beta-hydroxylase in the chromaffin vesicles of the adrenal gland. It is a transmembrane heme protein with the two heme groups being bound to conserved histidine residues. A cytochrome b-561 homologue, termed Dcytb, is an iron-regulated ferric reductase in the duodenal mucosa. Other homologues of these are also likely to be ferric reductases. SDR2 is proposed to be important in regulating the metabolism of iron in the onset of neurodegenerative disorders.
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B_lectin

Bulb-type mannose-specific lectin
B_lectin
SMART accession number:SM00108
Description: -
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BAG

BAG domains, present in regulator of Hsp70 proteins
BAG
SMART accession number:SM00264
Description: BAG domains, present in Bcl-2-associated athanogene 1 and silencer of death domains
GO function:chaperone binding (GO:0051087)
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BH4

BH4 Bcl-2 homology region 4
BH4
SMART accession number:SM00265
Description: -
GO process:regulation of apoptotic process (GO:0042981)
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BIR

Baculoviral inhibition of apoptosis protein repeat
BIR
SMART accession number:SM00238
Description: Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.
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BTK

Bruton's tyrosine kinase Cys-rich motif
BTK
SMART accession number:SM00107
Description: Zinc-binding motif containing conserved cysteines and a histidine. Always found C-terminal to PH domains (but not all PH domains are followed by BTK motifs). The crystal structure shows this motif packs against the PH domain. The PH+Btk module pair has been called the Tec homology (TH) region.
GO process:intracellular signal transduction (GO:0035556)
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C1

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains)
C1
SMART accession number:SM00109
Description: Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.
GO process:intracellular signal transduction (GO:0035556)
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C2

Protein kinase C conserved region 2 (CalB)
C2
SMART accession number:SM00239
Description: Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.
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Calx_beta

Domains in Na-Ca exchangers and integrin-beta4
Calx_beta
SMART accession number:SM00237
Description: Domain in Na-Ca exchangers and integrin subunit beta4 (and some cyanobacterial proteins)
GO process:cell communication (GO:0007154)
GO component:integral component of membrane (GO:0016021)
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CARD

Caspase recruitment domain
CARD
SMART accession number:SM00114
Description: Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain.
GO process:regulation of apoptotic process (GO:0042981)
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CASc

Caspase, interleukin-1 beta converting enzyme (ICE) homologues
CASc
SMART accession number:SM00115
Description: Cysteine aspartases that mediate programmed cell death (apoptosis). Caspases are synthesised as zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologues.
GO function:cysteine-type peptidase activity (GO:0008234)
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CH

Calponin homology domain
CH
SMART accession number:SM00033
Description: Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
GO function:protein binding (GO:0005515)
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CheW

Two component signalling adaptor domain
CheW
SMART accession number:SM00260
Description: -
GO process:signal transduction (GO:0007165), chemotaxis (GO:0006935)
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CNH

Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2
CNH
SMART accession number:SM00036
Description: Unpublished observations.
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cNMP

Cyclic nucleotide-monophosphate binding domain
cNMP
SMART accession number:SM00100
Description: Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.
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CULLIN

Cullin
CULLIN
SMART accession number:SM00182
Description: -
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CYCc

Adenylyl- / guanylyl cyclase, catalytic domain
CYCc
SMART accession number:SM00044
Description: Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.
GO process:cyclic nucleotide biosynthetic process (GO:0009190), intracellular signal transduction (GO:0035556)
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Cyclin_C

Cyclin_C
SMART accession number:SM01332
Description: Cyclins are a family of proteins that control the progression of cells through the cell cycle by activating cyclin-dependent kinase (Cdk) enzymes.
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Cyt-b5

Cytochrome b5-like Heme/Steroid binding domain
Cyt-b5
SMART accession number:SM01117
Description: This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors such as O00264 ((PUBMED:9705155),(PUBMED:8774719)). Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.
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DAGKa

Diacylglycerol kinase accessory domain (presumed)
DAGKa
SMART accession number:SM00045
Description: Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain might either be an accessory domain or else contribute to the catalytic domain. Bacterial homologues are known.
GO process:protein kinase C-activating G protein-coupled receptor signaling pathway (GO:0007205)
GO function:diacylglycerol kinase activity (GO:0004143)
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DAGKc

Diacylglycerol kinase catalytic domain (presumed)
DAGKc
SMART accession number:SM00046
Description: Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain is presumed to be the catalytic domain. Bacterial homologues areknown.
GO function:kinase activity (GO:0016301)
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DAX

Domain present in Dishevelled and axin
DAX
SMART accession number:SM00021
Description: Domain of unknown function.
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DEATH

DEATH domain, found in proteins involved in cell death (apoptosis).
DEATH
SMART accession number:SM00005
Description: Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.
GO process:signal transduction (GO:0007165)
GO function:protein binding (GO:0005515)
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DED

Death effector domain
DED
SMART accession number:SM00031
Description: -
GO process:regulation of apoptotic process (GO:0042981)
GO function:protein binding (GO:0005515)
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DEP

Domain found in Dishevelled, Egl-10, and Pleckstrin
DEP
SMART accession number:SM00049
Description: Domain of unknown function present in signalling proteins that contain PH, rasGEF, rhoGEF, rhoGAP, RGS, PDZ domains. DEP domain in Drosophila dishevelled is essential to rescue planar polarity defects and induce JNK signalling (Cell 94, 109-118).
GO process:intracellular signal transduction (GO:0035556)
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DSPc

Dual specificity phosphatase, catalytic domain
DSPc
SMART accession number:SM00195
Description: -
GO process:protein dephosphorylation (GO:0006470)
GO function:protein tyrosine/serine/threonine phosphatase activity (GO:0008138)
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DYNc

Dynamin, GTPase
DYNc
SMART accession number:SM00053
Description: Large GTPases that mediate vesicle trafficking. Dynamin participates in the endocytic uptake of receptors, associated ligands, and plasma membrane following an exocytic event.
GO function:GTPase activity (GO:0003924), GTP binding (GO:0005525)
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EAL

Putative diguanylate phosphodiesterase
EAL
SMART accession number:SM00052
Description: Putative diguanylate phosphodiesterase, present in a variety of bacteria.
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EFh

EF-hand, calcium binding motif
EFh
SMART accession number:SM00054
Description: EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.
GO function:calcium ion binding (GO:0005509)
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EH

Eps15 homology domain
EH
SMART accession number:SM00027
Description: Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.
GO function:protein binding (GO:0005515)
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ENTH

Epsin N-terminal homology (ENTH) domain
ENTH
SMART accession number:SM00273
Description: -
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FBOX

A Receptor for Ubiquitination Targets
FBOX
SMART accession number:SM00256
Description: -
GO function:protein binding (GO:0005515)
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FCH

Fes/CIP4 homology domain
FCH
SMART accession number:SM00055
Description: Alignment extended from original report. Highly alpha-helical. Also known as the RAEYL motif or the S. pombe Cdc15 N-terminal domain.
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FF

Contains two conserved F residues
FF
SMART accession number:SM00441
Description: A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.
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FH2

Formin Homology 2 Domain
FH2
SMART accession number:SM00498
Description: FH proteins control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarisation. Members of this family have been found to interact with Rho-GTPases, profilin and other actin-assoziated proteins. These interactions are mediated by the proline-rich FH1 domain, usually located in front of FH2 (but not listed in SMART). Despite this cytosolic function, vertebrate formins have been assigned functions within the nucleus. A set of Formin-Binding Proteins (FBPs) has been shown to bind FH1 with their WW domain.
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FHA

Forkhead associated domain
FHA
SMART accession number:SM00240
Description: Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
GO function:protein binding (GO:0005515)
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FIST

FIST N domain
FIST
SMART accession number:SM00897
Description: The FIST N domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids.
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Frizzled

Frizzled/Smoothened family membrane region
Frizzled
SMART accession number:SM01330
Description: Frizzled is a family of G protein-coupled receptor proteins (PMID: 14977528) that serves as receptors in the Wnt signaling pathway and other signaling pathways. When activated, Frizzled leads to activation of Dishevelled in the cytosol.
GO process:cell surface receptor signaling pathway (GO:0007166)
GO component:membrane (GO:0016020)
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FYVE

Protein present in Fab1, YOTB, Vac1, and EEA1
FYVE
SMART accession number:SM00064
Description: The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.
GO function:metal ion binding (GO:0046872)
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G_alpha

G protein alpha subunit
G_alpha
SMART accession number:SM00275
Description: Subunit of G proteins that contains the guanine nucleotide binding site
GO process:G protein-coupled receptor signaling pathway (GO:0007186)
GO function:GTPase activity (GO:0003924), guanyl nucleotide binding (GO:0019001), G-protein beta/gamma-subunit complex binding (GO:0031683)
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GAF

Domain present in phytochromes and cGMP-specific phosphodiesterases.
GAF
SMART accession number:SM00065
Description: Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.
GO function:protein binding (GO:0005515)
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GAS2

Growth-Arrest-Specific Protein 2 Domain
GAS2
SMART accession number:SM00243
Description: GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
GO function:microtubule binding (GO:0008017)
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GED

Dynamin GTPase effector domain
GED
SMART accession number:SM00302
Description: -
GO function:GTPase activity (GO:0003924), GTP binding (GO:0005525)
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GGDEF

diguanylate cyclase
GGDEF
SMART accession number:SM00267
Description: Diguanylate cyclase, present in a variety of bacteria.
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GGL

G protein gamma subunit-like motifs
GGL
SMART accession number:SM00224
Description: -
GO process:G protein-coupled receptor signaling pathway (GO:0007186)
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GoLoco

LGN motif, putative GEFs specific for G-alpha GTPases
GoLoco
SMART accession number:SM00390
Description: GEF specific for Galpha_i proteins
GO function:GTPase regulator activity (GO:0030695)
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GRAM

domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins
GRAM
SMART accession number:SM00568
Description: -
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GS

GS motif
GS
SMART accession number:SM00467
Description: Aa approx. 30 amino acid motif that precedes the kinase domain in types I and II TGF beta receptors. Mutation of two or more of the serines or threonines in the TTSGSGSG of TGF-beta type I receptor impairs phosphorylation and signaling activity.
GO process:protein phosphorylation (GO:0006468)
GO component:membrane (GO:0016020)
GO function:ATP binding (GO:0005524), transmembrane receptor protein serine/threonine kinase activity (GO:0004675)
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GuKc

Guanylate kinase homologues.
GuKc
SMART accession number:SM00072
Description: Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.
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HAMP

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain
HAMP
SMART accession number:SM00304
Description: -
GO process:signal transduction (GO:0007165)
GO component:integral component of membrane (GO:0016021)
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HATPase_c

Histidine kinase-like ATPases
HATPase_c
SMART accession number:SM00387
Description: Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
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HECTc

Domain Homologous to E6-AP Carboxyl Terminus with
HECTc
SMART accession number:SM00119
Description: E3 ubiquitin-protein ligases. Can bind to E2 enzymes.
GO function:ubiquitin-protein transferase activity (GO:0004842)
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HisKA

His Kinase A (phosphoacceptor) domain
HisKA
SMART accession number:SM00388
Description: Dimerisation and phosphoacceptor domain of histidine kinases.
GO process:signal transduction (GO:0007165)
GO function:phosphorelay sensor kinase activity (GO:0000155)
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HPT

Histidine Phosphotransfer domain
HPT
SMART accession number:SM00073
Description: Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.
GO process:phosphorelay signal transduction system (GO:0000160)
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Hr1

Rho effector or protein kinase C-related kinase homology region 1 homologues
Hr1
SMART accession number:SM00742
Description: Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain
GO process:signal transduction (GO:0007165)
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ILWEQ

I/LWEQ domain
ILWEQ
SMART accession number:SM00307
Description: Thought to possess an F-actin binding function.
GO function:actin binding (GO:0003779)
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IPPc

Inositol polyphosphate phosphatase, catalytic domain homologues
IPPc
SMART accession number:SM00128
Description: Mg(2+)-dependent/Li(+)-sensitive enzymes.
GO process:phosphatidylinositol dephosphorylation (GO:0046856)
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IQ

Short calmodulin-binding motif containing conserved Ile and Gln residues.
IQ
SMART accession number:SM00015
Description: Calmodulin-binding motif.
GO function:protein binding (GO:0005515)
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ITAM

Immunoreceptor tyrosine-based activation motif
ITAM
SMART accession number:SM00077
Description: Motif that may be dually phosphorylated on tyrosine that links antigen receptors to downstream signalling machinery.
GO process:cell surface receptor signaling pathway (GO:0007166)
GO component:membrane (GO:0016020)
GO function:transmembrane signaling receptor activity (GO:0004888)
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KISc

Kinesin motor, catalytic domain. ATPase.
KISc
SMART accession number:SM00129
Description: Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.
GO process:microtubule-based movement (GO:0007018)
GO function:ATP binding (GO:0005524), microtubule binding (GO:0008017), microtubule motor activity (GO:0003777)
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L27

domain in receptor targeting proteins Lin-2 and Lin-7
L27
SMART accession number:SM00569
Description: -
GO function:protein binding (GO:0005515)
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LIM

Zinc-binding domain present in Lin-11, Isl-1, Mec-3.
LIM
SMART accession number:SM00132
Description: Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.
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LMWPc

Low molecular weight phosphatase family
LMWPc
SMART accession number:SM00226
Description: -
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MA

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer).
MA
SMART accession number:SM00283
Description: Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
GO process:signal transduction (GO:0007165)
GO component:membrane (GO:0016020)
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MeTrc

Methyltransferase, chemotaxis proteins
MeTrc
SMART accession number:SM00138
Description: Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.
GO function:S-adenosylmethionine-dependent methyltransferase activity (GO:0008757)
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MIR

Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases
MIR
SMART accession number:SM00472
Description: -
GO component:membrane (GO:0016020)
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MYSc

Myosin. Large ATPases.
MYSc
SMART accession number:SM00242
Description: ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
GO component:myosin complex (GO:0016459)
GO function:motor activity (GO:0003774), ATP binding (GO:0005524)
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MyTH4

Domain in Myosin and Kinesin Tails
MyTH4
SMART accession number:SM00139
Description: Domain present twice in myosin-VIIa, and also present in 3 other myosins.
GO component:cytoskeleton (GO:0005856)
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PAC

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain)
PAC
SMART accession number:SM00086
Description: PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
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PAS

PAS domain
PAS
SMART accession number:SM00091
Description: PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels ([1]; Ponting & Aravind, in press).
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PASTA

PASTA
SMART accession number:SM00740
Description: -
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PBD

P21-Rho-binding domain
PBD
SMART accession number:SM00285
Description: Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).
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PDZ

Domain present in PSD-95, Dlg, and ZO-1/2.
PDZ
SMART accession number:SM00228
Description: Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.
GO function:protein binding (GO:0005515)
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PH

Pleckstrin homology domain.
PH
SMART accession number:SM00233
Description: Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.
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PI3K_C2

Phosphoinositide 3-kinase, region postulated to contain C2 domain
PI3K_C2
SMART accession number:SM00142
Description: Outlier of C2 family.
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PI3K_p85B

PI3-kinase family, p85-binding domain
PI3K_p85B
SMART accession number:SM00143
Description: Region of p110 PI3K that binds the p85 subunit.
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PI3K_rbd

PI3-kinase family, Ras-binding domain
PI3K_rbd
SMART accession number:SM00144
Description: Certain members of the PI3K family possess Ras-binding domains in their N-termini. These regions show some similarity (although not highly significant similarity) to Ras-binding RA domains (unpublished observation).
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PI3Ka

Phosphoinositide 3-kinase family, accessory domain (PIK domain)
PI3Ka
SMART accession number:SM00145
Description: PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation.
Family alignment:
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PI3Kc

Phosphoinositide 3-kinase, catalytic domain
PI3Kc
SMART accession number:SM00146
Description: Phosphoinositide 3-kinase isoforms participate in a variety of processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, and apoptosis. These homologues may be either lipid kinases and/or protein kinases: the former phosphorylate the 3-position in the inositol ring of inositol phospholipids. The ataxia telangiectesia-mutated gene produced, the targets of rapamycin (TOR) and the DNA-dependent kinase have not been found to possess lipid kinase activity. Some of this family possess PI-4 kinase activities.
Family alignment:
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PIPKc

Phosphatidylinositol phosphate kinases
PIPKc
SMART accession number:SM00330
Description: -
GO process:phosphatidylinositol metabolic process (GO:0046488)
GO function:phosphatidylinositol phosphate kinase activity (GO:0016307)
Family alignment:
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PLAc

Cytoplasmic phospholipase A2, catalytic subunit
PLAc
SMART accession number:SM00022
Description: Cytosolic phospholipases A2 hydrolyse arachidonyl phospholipids. Family includes phospholipases B isoforms.
GO process:phospholipid catabolic process (GO:0009395)
GO function:phospholipase activity (GO:0004620)
Family alignment:
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PLCXc

Phospholipase C, catalytic domain (part); domain X
PLCXc
SMART accession number:SM00148
Description: Phosphoinositide-specific phospholipases C. These enzymes contain 2 regions (X and Y) which together form a TIM barrel-like structure containing the active site residues. Phospholipase C enzymes (PI-PLC) act as signal transducers that generate two second messengers, inositol-1,4,5-trisphosphate and diacylglycerol. The bacterial enzyme [6] appears to be a homologue of the mammalian PLCs.
Family alignment:
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PLCYc

Phospholipase C, catalytic domain (part); domain Y
PLCYc
SMART accession number:SM00149
Description: Phosphoinositide-specific phospholipases C. These enzymes contain 2 regions (X and Y) which together form a TIM barrel-like structure containing the active site residues. Phospholipase C enzymes (PI-PLC) act as signal transducers that generate two second messengers, inositol-1,4,5-trisphosphate and diacylglycerol. The bacterial enzyme [6] appears to be a homologue of the mammalian PLCs.
GO process:lipid metabolic process (GO:0006629), signal transduction (GO:0007165), intracellular signal transduction (GO:0035556)
GO function:phosphatidylinositol phospholipase C activity (GO:0004435)
Family alignment:
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PLDc

Phospholipase D. Active site motifs.
PLDc
SMART accession number:SM00155
Description: Phosphatidylcholine-hydrolyzing phospholipase D (PLD) isoforms are activated by ADP-ribosylation factors (ARFs). PLD produces phosphatidic acid from phosphatidylcholine, which may be essential for the formation of certain types of transport vesicles or may be constitutive vesicular transport to signal transduction pathways. PC-hydrolysing PLD is a homologue of cardiolipin synthase, phosphatidylserine synthase, bacterial PLDs, and viral proteins. Each of these appears to possess a domain duplication which is apparent by the presence of two motifs containing well-conserved histidine, lysine, aspartic acid, and/or asparagine residues which may contribute to the active site. An E. coli endonuclease (nuc) and similar proteins appear to be PLD homologues but possess only one of these motifs. The profile contained here represents only the putative active site regions, since an accurate multiple alignment of the repeat units has not been achieved.
GO function:catalytic activity (GO:0003824)
Family alignment:
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PP2Ac

Protein phosphatase 2A homologues, catalytic domain.
PP2Ac
SMART accession number:SM00156
Description: Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.
GO function:hydrolase activity (GO:0016787)
Family alignment:
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PP2Cc

Serine/threonine phosphatases, family 2C, catalytic domain
PP2Cc
SMART accession number:SM00332
Description: The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.
Family alignment:
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PTB

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain
PTB
SMART accession number:SM00462
Description: PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.
GO function:protein binding (GO:0005515)
Family alignment:
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PTBI

Phosphotyrosine-binding domain (IRS1-like)
PTBI
SMART accession number:SM00310
Description: -
Family alignment:
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PTEN_C2

C2 domain of PTEN tumour-suppressor protein
PTEN_C2
SMART accession number:SM01326
Description: This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (Pfam PF00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane (PMID:10555148).
Family alignment:
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PTPc

Protein tyrosine phosphatase, catalytic domain
PTPc
SMART accession number:SM00194
Description: -
GO process:protein dephosphorylation (GO:0006470)
GO function:protein tyrosine phosphatase activity (GO:0004725)
Family alignment:
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