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Conserved domains on  [gi|578813655|ref|XP_006715849|]
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cerebral cavernous malformations 2 protein isoform X4 [Homo sapiens]

Protein Classification

PH-like and HHD_CCM2 domain-containing protein( domain architecture ID 10987421)

PH-like and HHD_CCM2 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 64-212 5.49e-73

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13166:

Pssm-ID: 473070  Cd Length: 193  Bit Score: 225.46  E-value: 5.49e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813655  64 HTVVLSLPERVEPDRLLSDYIEKEVKYLGQLTSIPGYLNPSSRTEILHFIDNAKRAHQLPGHLTQEHDAVLSLSAYNVKL 143
Cdd:cd13166    1 SVPLYPPDYRVDPDVLLNDYIEKEVKYLGQLTSVPGSLDPSSRTELLQLLDTARRLGQLPLQLTPEQDAILSLSAYNVKL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578813655 144 AWRDGEDIILRVPIHDIAAVSYVRDDAAHLVVLKTDDSSTKVDIKETYEVEASTfcfPESVDVGGASPH 212
Cdd:cd13166   81 LWRDGEDLILRVPTHDIAAVSYVRDDSLHLVVLKTASEPGISPSQSLSAESSPT---SGSLSESGPVPV 146
CCM2_C pfam16545
Cerebral cavernous malformation protein, harmonin-homology; CCM2_HHD is a folded-helical ...
 217-311 7.60e-55

Cerebral cavernous malformation protein, harmonin-homology; CCM2_HHD is a folded-helical region of a family of vertebral proteins, mutations in which cause cerebral cavernous malformations (CCMs). These malformations are congenital vascular anomalies of the central nervous system that can result in haemorrhagic stroke, seizures, recurrent headaches, and focal neurologic deficits. This domain is structurally homologous to the N-terminal domain of harmonin, so it is named the CCM2 harmonin-homology domain or CCM2_HHD. This protein is often called Malcavernin.


:

Pssm-ID: 435415  Cd Length: 95  Bit Score: 175.33  E-value: 7.60e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813655  217 SESELSASATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHEFCINLRQLYGDSRKFLLLGLRPFIPEKDSQHFE 296
Cdd:pfam16545   1 SDSSNSSSAAELLQDYMVTLRSKLSPDEIQQFALLLREYRLGKSILEFCSELLQLYGDERKFLLLGMRPFIPEKDIGYFE 80

                          90
                  ....*....|....*
gi 578813655  297 NFLETIGVKDGRGII 311
Cdd:pfam16545  81 SFLESIGIREGNGIL 95
 
Name Accession Description Interval E-value
PTB_CCM2 cd13166
Cerebral cavernous malformation 2 FERM domain C-lobe; CCM2 (also called malcavernin; C7orf22 ...
 64-212 5.49e-73

Cerebral cavernous malformation 2 FERM domain C-lobe; CCM2 (also called malcavernin; C7orf22/chromosome 7 open reading frame 22; OSM) along with CCM1 and CCM3 constitutes a set of proteins which when mutated are responsible for cerebral cavernous malformations, an autosomal dominant neurovascular disease characterized by cerebral hemorrhages and vascular malformations in the central nervous system. CCM2 plays many functional roles. CCM2 functions as a scaffold involved in small GTPase Rac-dependent p38 mitogen-activated protein kinase (MAPK) activation when the cell is under hyperosmotic stress. It associates with CCM1 in the signalling cascades that regulate vascular integrity and participates in HEG1 (the transmembrane receptor heart of glass 1) mediated endothelial cell junctions. CCM proteins also inhibit the activation of small GTPase RhoA and its downstream effector Rho kinase (ROCK) to limit vascular permeability. CCM2 mediates TrkA-dependent cell death via its N-terminal PTB domain in pediatric neuroblastic tumours. CCM2 possesses an N-terminal PTB domain and a C-terminal Karet domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269987  Cd Length: 193  Bit Score: 225.46  E-value: 5.49e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813655  64 HTVVLSLPERVEPDRLLSDYIEKEVKYLGQLTSIPGYLNPSSRTEILHFIDNAKRAHQLPGHLTQEHDAVLSLSAYNVKL 143
Cdd:cd13166    1 SVPLYPPDYRVDPDVLLNDYIEKEVKYLGQLTSVPGSLDPSSRTELLQLLDTARRLGQLPLQLTPEQDAILSLSAYNVKL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578813655 144 AWRDGEDIILRVPIHDIAAVSYVRDDAAHLVVLKTDDSSTKVDIKETYEVEASTfcfPESVDVGGASPH 212
Cdd:cd13166   81 LWRDGEDLILRVPTHDIAAVSYVRDDSLHLVVLKTASEPGISPSQSLSAESSPT---SGSLSESGPVPV 146
CCM2_C pfam16545
Cerebral cavernous malformation protein, harmonin-homology; CCM2_HHD is a folded-helical ...
 217-311 7.60e-55

Cerebral cavernous malformation protein, harmonin-homology; CCM2_HHD is a folded-helical region of a family of vertebral proteins, mutations in which cause cerebral cavernous malformations (CCMs). These malformations are congenital vascular anomalies of the central nervous system that can result in haemorrhagic stroke, seizures, recurrent headaches, and focal neurologic deficits. This domain is structurally homologous to the N-terminal domain of harmonin, so it is named the CCM2 harmonin-homology domain or CCM2_HHD. This protein is often called Malcavernin.


Pssm-ID: 435415  Cd Length: 95  Bit Score: 175.33  E-value: 7.60e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813655  217 SESELSASATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHEFCINLRQLYGDSRKFLLLGLRPFIPEKDSQHFE 296
Cdd:pfam16545   1 SDSSNSSSAAELLQDYMVTLRSKLSPDEIQQFALLLREYRLGKSILEFCSELLQLYGDERKFLLLGMRPFIPEKDIGYFE 80

                          90
                  ....*....|....*
gi 578813655  297 NFLETIGVKDGRGII 311
Cdd:pfam16545  81 SFLESIGIREGNGIL 95
HHD_CCM2 cd13516
harmonin-homology domain (harmonin_N_like domain) of malcavernin (CCM2); CCM2 (also called ...
 212-307 1.10e-51

harmonin-homology domain (harmonin_N_like domain) of malcavernin (CCM2); CCM2 (also called malcavernin; C7orf22/chromosome 7 open reading frame 22; OSM) along with CCM1 and CCM3 constitutes a set of proteins which when mutated are responsible for cerebral cavernous malformations, an autosomal dominant neurovascular disease characterized by cerebral hemorrhages and vascular malformations in the central nervous system. CCM2 plays many functional roles. CCM2 functions as a scaffold involved in small GTPase Rac-dependent p38 mitogen-activated protein kinase (MAPK) activation when the cell is under hyperosmotic stress. It associates with CCM1 in the signaling cascades that regulate vascular integrity and participates in HEG1 (the transmembrane receptor heart of glass 1) mediated endothelial cell junctions. CCM proteins also inhibit the activation of small GTPase RhoA and its downstream effector Rho kinase (ROCK) to limit vascular permeability. CCM2 mediates TrkA-dependent cell death via its N-terminal PTB domain in pediatric neuroblastic tumours. CCM2 possesses an N-terminal PTB domain. The C-terminal domain of malcavernin, which is represented here, appears similar to the N-terminal domain of the scaffolding protein harmonin. It has also been referred to as the Karet domain.


Pssm-ID: 259825  Cd Length: 97  Bit Score: 167.44  E-value: 1.10e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813655 212 HSKTISESELS-ASATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHEFCINLRQLYGDSRKFLLLGLRPFIPEK 290
Cdd:cd13516    1 HSTSASRSDSSiVSADELLQDYMEVLRSKLTPDELQQFAALLREYRTGSPIEEFCQKLLELYGPERKFLLLGMRPFIPEK 80

                         90
                 ....*....|....*..
gi 578813655 291 DSQHFENFLETIGVKDG 307
Cdd:cd13516   81 DLPYFESFLEKIGIADG 97
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 87-184 7.75e-03

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 36.52  E-value: 7.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813655    87 EVKYLGqltSIPgyLNPSSRTEIlhfIDNA--KRAHQLPGHLTQEHDAVLSLSAYNVKLAWRDGEDIILRVPIHDIAAVS 164
Cdd:smart00462   7 RVKYLG---SVE--VPEARGLQV---VQEAirKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCA 78

                           90       100
                   ....*....|....*....|
gi 578813655   165 YVRDDAAHLVVLKTDDSSTK 184
Cdd:smart00462  79 VGPDDLDVFGYIARDPGSSR 98
 
Name Accession Description Interval E-value
PTB_CCM2 cd13166
Cerebral cavernous malformation 2 FERM domain C-lobe; CCM2 (also called malcavernin; C7orf22 ...
 64-212 5.49e-73

Cerebral cavernous malformation 2 FERM domain C-lobe; CCM2 (also called malcavernin; C7orf22/chromosome 7 open reading frame 22; OSM) along with CCM1 and CCM3 constitutes a set of proteins which when mutated are responsible for cerebral cavernous malformations, an autosomal dominant neurovascular disease characterized by cerebral hemorrhages and vascular malformations in the central nervous system. CCM2 plays many functional roles. CCM2 functions as a scaffold involved in small GTPase Rac-dependent p38 mitogen-activated protein kinase (MAPK) activation when the cell is under hyperosmotic stress. It associates with CCM1 in the signalling cascades that regulate vascular integrity and participates in HEG1 (the transmembrane receptor heart of glass 1) mediated endothelial cell junctions. CCM proteins also inhibit the activation of small GTPase RhoA and its downstream effector Rho kinase (ROCK) to limit vascular permeability. CCM2 mediates TrkA-dependent cell death via its N-terminal PTB domain in pediatric neuroblastic tumours. CCM2 possesses an N-terminal PTB domain and a C-terminal Karet domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269987  Cd Length: 193  Bit Score: 225.46  E-value: 5.49e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813655  64 HTVVLSLPERVEPDRLLSDYIEKEVKYLGQLTSIPGYLNPSSRTEILHFIDNAKRAHQLPGHLTQEHDAVLSLSAYNVKL 143
Cdd:cd13166    1 SVPLYPPDYRVDPDVLLNDYIEKEVKYLGQLTSVPGSLDPSSRTELLQLLDTARRLGQLPLQLTPEQDAILSLSAYNVKL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578813655 144 AWRDGEDIILRVPIHDIAAVSYVRDDAAHLVVLKTDDSSTKVDIKETYEVEASTfcfPESVDVGGASPH 212
Cdd:cd13166   81 LWRDGEDLILRVPTHDIAAVSYVRDDSLHLVVLKTASEPGISPSQSLSAESSPT---SGSLSESGPVPV 146
CCM2_C pfam16545
Cerebral cavernous malformation protein, harmonin-homology; CCM2_HHD is a folded-helical ...
 217-311 7.60e-55

Cerebral cavernous malformation protein, harmonin-homology; CCM2_HHD is a folded-helical region of a family of vertebral proteins, mutations in which cause cerebral cavernous malformations (CCMs). These malformations are congenital vascular anomalies of the central nervous system that can result in haemorrhagic stroke, seizures, recurrent headaches, and focal neurologic deficits. This domain is structurally homologous to the N-terminal domain of harmonin, so it is named the CCM2 harmonin-homology domain or CCM2_HHD. This protein is often called Malcavernin.


Pssm-ID: 435415  Cd Length: 95  Bit Score: 175.33  E-value: 7.60e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813655  217 SESELSASATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHEFCINLRQLYGDSRKFLLLGLRPFIPEKDSQHFE 296
Cdd:pfam16545   1 SDSSNSSSAAELLQDYMVTLRSKLSPDEIQQFALLLREYRLGKSILEFCSELLQLYGDERKFLLLGMRPFIPEKDIGYFE 80

                          90
                  ....*....|....*
gi 578813655  297 NFLETIGVKDGRGII 311
Cdd:pfam16545  81 SFLESIGIREGNGIL 95
HHD_CCM2 cd13516
harmonin-homology domain (harmonin_N_like domain) of malcavernin (CCM2); CCM2 (also called ...
 212-307 1.10e-51

harmonin-homology domain (harmonin_N_like domain) of malcavernin (CCM2); CCM2 (also called malcavernin; C7orf22/chromosome 7 open reading frame 22; OSM) along with CCM1 and CCM3 constitutes a set of proteins which when mutated are responsible for cerebral cavernous malformations, an autosomal dominant neurovascular disease characterized by cerebral hemorrhages and vascular malformations in the central nervous system. CCM2 plays many functional roles. CCM2 functions as a scaffold involved in small GTPase Rac-dependent p38 mitogen-activated protein kinase (MAPK) activation when the cell is under hyperosmotic stress. It associates with CCM1 in the signaling cascades that regulate vascular integrity and participates in HEG1 (the transmembrane receptor heart of glass 1) mediated endothelial cell junctions. CCM proteins also inhibit the activation of small GTPase RhoA and its downstream effector Rho kinase (ROCK) to limit vascular permeability. CCM2 mediates TrkA-dependent cell death via its N-terminal PTB domain in pediatric neuroblastic tumours. CCM2 possesses an N-terminal PTB domain. The C-terminal domain of malcavernin, which is represented here, appears similar to the N-terminal domain of the scaffolding protein harmonin. It has also been referred to as the Karet domain.


Pssm-ID: 259825  Cd Length: 97  Bit Score: 167.44  E-value: 1.10e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813655 212 HSKTISESELS-ASATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHEFCINLRQLYGDSRKFLLLGLRPFIPEK 290
Cdd:cd13516    1 HSTSASRSDSSiVSADELLQDYMEVLRSKLTPDELQQFAALLREYRTGSPIEEFCQKLLELYGPERKFLLLGMRPFIPEK 80

                         90
                 ....*....|....*..
gi 578813655 291 DSQHFENFLETIGVKDG 307
Cdd:cd13516   81 DLPYFESFLEKIGIADG 97
harmonin_N_like cd07347
N-terminal protein-binding module of harmonin and similar domains, also known as HHD (harmonin ...
 225-301 7.01e-20

N-terminal protein-binding module of harmonin and similar domains, also known as HHD (harmonin homology domain); This domain is found in harmonin, and similar proteins such as delphilin, and whirlin. These are postsynaptic density-95/discs-large/ZO-1 (PDZ) domain-containing scaffold proteins. Harmonin and whirlin are organizers of the Usher protein network of the inner ear and the retina, delphilin is found at the cerebellar parallel fiber-Purkinje cell synapses. This domain is also found in CCM2 (also called malcavernin; C7orf22/chromosome 7 open reading frame 22; OSM). CCM2 along with CCM1 and CCM3 constitutes a set of proteins which when mutated are responsible for cerebral cavernous malformations, an autosomal dominant neurovascular disease characterized by cerebral hemorrhages and vascular malformations in the central nervous system. CCM2 plays many functional roles. CCM2 functions as a scaffold involved in small GTPase Rac-dependent p38 mitogen-activated protein kinase (MAPK) activation when the cell is under hyperosmotic stress. It associates with CCM1 in the signaling cascades that regulate vascular integrity and participates in HEG1 (the transmembrane receptor heart of glass 1) mediated endothelial cell junctions. CCM proteins also inhibit the activation of small GTPase RhoA and its downstream effector Rho kinase (ROCK) to limit vascular permeability. CCM2 mediates TrkA-dependent cell death via its N-terminal PTB domain in pediatric neuroblastic tumours; the C-terminal domain of malcavernin represented here has also been refered to as the Karet domain. Harmonin contains a single copy of this domain at its N-terminus which binds specifically to a short internal peptide fragment of the cadherin 23 cytoplasmic domain (a component of the Usher protein network). Whirlin contains two copies of this domain; the first of these has been assayed for interaction with the cytoplasmic domain of cadherin 23 and no interaction could be detected.


Pssm-ID: 259818  Cd Length: 78  Bit Score: 83.02  E-value: 7.01e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578813655 225 ATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHEFCINLRQLYG-DSRKFLLLGLRPFIPEKDSQHFENFLET 301
Cdd:cd07347    1 RRELARLFSEQADQLLTDQERAYVTQALSEYRKGRSVEALVADLFPVLDtPAKLSLLQGLRSLIPPKDQQRFDELVAQ 78
HN_RTEL1 cd13932
harmonin_N_like domain of regulator of telomere elongation helicase 1 (also known as RTEL); ...
 217-302 6.00e-09

harmonin_N_like domain of regulator of telomere elongation helicase 1 (also known as RTEL); Mouse Rtel is an essential protein required for the maintenance of both telomeric and genomic stability. RTEL1 appears to maintain genome stability by suppressing homologous recombination (HR). In vitro, purified human and insect RTEL1 have been shown to promote the disassembly of D loop recombination intermediates, in a reaction dependent upon ATP hydrolysis. Human RTEL1 is implicated in the etiology of Dyskeratosis congenital (DC, is an inherited bone marrow failure and cancer predisposition syndrome). Point mutations in its helicase domains, and truncations which result in loss of its C-terminus have been discovered in DC families. RTEL1 is also a candidate gene influencing glioma susceptibility. The C-terminal domain of RTEL1, represented here, appears similar to the N-terminal domain of the scaffolding protein harmonin.


Pssm-ID: 259826 [Multi-domain]  Cd Length: 99  Bit Score: 53.05  E-value: 6.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813655 217 SESELSASATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHEFCINLRQLYGDSRK-FLLLGLRPFIPEKDSQHF 295
Cdd:cd13932    8 SSSSGAKPAPESASAFLREVKQKLSAAEYRQFSAALQAYKTGDDFEQLLAVLAELFAEPERhPLLRGFRRFVRPHHKKEF 87


                 ....*..
gi 578813655 296 ENFLETI 302
Cdd:cd13932   88 DERCKSL 94
PTB_ICAP1 cd13163
Integrin beta-1-binding protein 1 Phosphotyrosine-binding (PTB) PH-like fold; ICAP1 (also ...
 85-185 1.63e-05

Integrin beta-1-binding protein 1 Phosphotyrosine-binding (PTB) PH-like fold; ICAP1 (also called Integrin cytoplasmic domain-associated protein 1) binds specifically to the beta1 integrin subunit cytoplasmic domain and the cerebral cavernous malformation (CCM) protein CCM1. It regulates beta1 integrin-dependent cell migration by affecting the pattern of focal adhesion formation. ICAP1 recruits CCM1 to the cell membrane and activates CCM1 by changing its conformation. Since CCM1 plays role in cardiovascular development, it is hypothesized ICAP1 is involved in vascular differentiation. ICAP-1 has an N-terminal domain that rich in serine and threonine and a C-terminal PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269985  Cd Length: 129  Bit Score: 43.98  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813655  85 EKEVKYLGQLTSIPGYLNP-SSRTEILHFIDNAKRAHQLPgHLTQEHDAVLSLSAYNVKLAWRDGEDIILRVPIHDIA-A 162
Cdd:cd13163    2 EFRVKYVGVIENLEGLSHSlEGPLDLINAIDVAQQDGKLP-FVAIEEEVILGLSKYGIKVTELNQPVVLKRHPLYSIIrM 80

                         90       100
                 ....*....|....*....|....*.
gi 578813655 163 VSYvrDDA---AHLVVLKTDDSSTKV 185
Cdd:cd13163   81 VCY--DDGlggKSLLAVKTGDPGEEV 104
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 87-169 2.02e-04

Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269911  Cd Length: 120  Bit Score: 40.57  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813655  87 EVKYLGQLTSIPGYLNPSSRTEILHFIDNAKRAHQLPGhltqehDAVLSLSAYNVKLAWRDGEDIILRVPIHDIAAVSYV 166
Cdd:cd00934    4 QVKYLGSVEVGSSRGVDVVEEALKALAAALKSSKRKPG------PVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRD 77


                 ...
gi 578813655 167 RDD 169
Cdd:cd00934   78 PDN 80
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 87-184 7.75e-03

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 36.52  E-value: 7.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813655    87 EVKYLGqltSIPgyLNPSSRTEIlhfIDNA--KRAHQLPGHLTQEHDAVLSLSAYNVKLAWRDGEDIILRVPIHDIAAVS 164
Cdd:smart00462   7 RVKYLG---SVE--VPEARGLQV---VQEAirKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCA 78

                           90       100
                   ....*....|....*....|
gi 578813655   165 YVRDDAAHLVVLKTDDSSTK 184
Cdd:smart00462  79 VGPDDLDVFGYIARDPGSSR 98
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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