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Conserved domains on  [gi|90193624|ref|NP_001035027|]
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integrator complex subunit 6 isoform c [Homo sapiens]

Protein Classification

VWA domain-containing protein( domain architecture ID 10608872)

VWA (von Willebrand factor type A) domain-containing protein may be involved in one of a wide variety of important cellular functions, including basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and immune defenses

CATH:  3.40.50.410
PubMed:  10830113
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWA_2 pfam13519
von Willebrand factor type A domain;
4-103 8.32e-18

von Willebrand factor type A domain;


:

Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 72.32  E-value: 8.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193624     4 LLFLIDTSASMNQRShLGTTYLDTAKGAVETFMKLRardpasRGDRYMLVTFEEPPYaIKAGWKENHATFMNELKNLQAE 83
Cdd:pfam13519   1 LVFVLDTSGSMRNGD-YGPTRLEAAKDAVLALLKSL------PGDRVGLVTFGDGPE-VLIPLTKDRAKILRALRRLEPK 72

                          90       100
                  ....*....|....*....|.
gi 90193624    84 -GLTTLGQSLRTAFDLLNLNR 103
Cdd:pfam13519  73 gGGTNLAAALQLARAALKHRR 93
 
Name Accession Description Interval E-value
VWA_2 pfam13519
von Willebrand factor type A domain;
4-103 8.32e-18

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 72.32  E-value: 8.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193624     4 LLFLIDTSASMNQRShLGTTYLDTAKGAVETFMKLRardpasRGDRYMLVTFEEPPYaIKAGWKENHATFMNELKNLQAE 83
Cdd:pfam13519   1 LVFVLDTSGSMRNGD-YGPTRLEAAKDAVLALLKSL------PGDRVGLVTFGDGPE-VLIPLTKDRAKILRALRRLEPK 72

                          90       100
                  ....*....|....*....|.
gi 90193624    84 -GLTTLGQSLRTAFDLLNLNR 103
Cdd:pfam13519  73 gGGTNLAAALQLARAALKHRR 93
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 4-100 2.05e-11

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 57.19  E-value: 2.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193624   4 LLFLIDTSASMnqrshlGTTYLDTAKGAVETFmkLRARDPASRGDRYMLVTFEEPPY----AIKAGWKENHATFMNELKN 79
Cdd:cd00198   3 IVFLLDVSGSM------GGEKLDKAKEALKAL--VSSLSASPPGDRVGLVTFGSNARvvlpLTTDTDKADLLEAIDALKK 74

                        90       100
                ....*....|....*....|.
gi 90193624  80 lQAEGLTTLGQSLRTAFDLLN 100
Cdd:cd00198  75 -GLGGGTNIGAALRLALELLK 94
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 4-114 2.06e-09

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 53.02  E-value: 2.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193624   4 LLFLIDTSASMNQRSHlgttyLDTAKGAVETFMKLrardpASRGDRYMLVTFEEPPYaIKAGWKENHATFMNELKNLQAE 83
Cdd:COG1240  95 VVLVVDASGSMAAENR-----LEAAKGALLDFLDD-----YRPRDRVGLVAFGGEAE-VLLPLTRDREALKRALDELPPG 163

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 90193624  84 GLTTLGQSLRTAFDLLNLNR--------LVT-GIDNYGQV 114
Cdd:COG1240 164 GGTPLGDALALALELLKRADparrkvivLLTdGRDNAGRI 203
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 4-100 1.88e-07

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 47.06  E-value: 1.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193624      4 LLFLIDTSASMNQRshlgttYLDTAKGAVETFMKLRARDPasRGDRYMLVTF-EEPPYAIKAGWKENHATFMNELKNLQ- 81
Cdd:smart00327   2 VVFLLDGSGSMGGN------RFELAKEFVLKLVEQLDIGP--DGDRVGLVTFsDDARVLFPLNDSRSKDALLEALASLSy 73

                           90       100
                   ....*....|....*....|
gi 90193624     82 -AEGLTTLGQSLRTAFDLLN 100
Cdd:smart00327  74 kLGGGTNLGAALQYALENLF 93
 
Name Accession Description Interval E-value
VWA_2 pfam13519
von Willebrand factor type A domain;
4-103 8.32e-18

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 72.32  E-value: 8.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193624     4 LLFLIDTSASMNQRShLGTTYLDTAKGAVETFMKLRardpasRGDRYMLVTFEEPPYaIKAGWKENHATFMNELKNLQAE 83
Cdd:pfam13519   1 LVFVLDTSGSMRNGD-YGPTRLEAAKDAVLALLKSL------PGDRVGLVTFGDGPE-VLIPLTKDRAKILRALRRLEPK 72

                          90       100
                  ....*....|....*....|.
gi 90193624    84 -GLTTLGQSLRTAFDLLNLNR 103
Cdd:pfam13519  73 gGGTNLAAALQLARAALKHRR 93
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 4-100 2.05e-11

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 57.19  E-value: 2.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193624   4 LLFLIDTSASMnqrshlGTTYLDTAKGAVETFmkLRARDPASRGDRYMLVTFEEPPY----AIKAGWKENHATFMNELKN 79
Cdd:cd00198   3 IVFLLDVSGSM------GGEKLDKAKEALKAL--VSSLSASPPGDRVGLVTFGSNARvvlpLTTDTDKADLLEAIDALKK 74

                        90       100
                ....*....|....*....|.
gi 90193624  80 lQAEGLTTLGQSLRTAFDLLN 100
Cdd:cd00198  75 -GLGGGTNIGAALRLALELLK 94
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 4-114 2.06e-09

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 53.02  E-value: 2.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193624   4 LLFLIDTSASMNQRSHlgttyLDTAKGAVETFMKLrardpASRGDRYMLVTFEEPPYaIKAGWKENHATFMNELKNLQAE 83
Cdd:COG1240  95 VVLVVDASGSMAAENR-----LEAAKGALLDFLDD-----YRPRDRVGLVAFGGEAE-VLLPLTRDREALKRALDELPPG 163

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 90193624  84 GLTTLGQSLRTAFDLLNLNR--------LVT-GIDNYGQV 114
Cdd:COG1240 164 GGTPLGDALALALELLKRADparrkvivLLTdGRDNAGRI 203
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 4-100 1.88e-07

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 47.06  E-value: 1.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193624      4 LLFLIDTSASMNQRshlgttYLDTAKGAVETFMKLRARDPasRGDRYMLVTF-EEPPYAIKAGWKENHATFMNELKNLQ- 81
Cdd:smart00327   2 VVFLLDGSGSMGGN------RFELAKEFVLKLVEQLDIGP--DGDRVGLVTFsDDARVLFPLNDSRSKDALLEALASLSy 73

                           90       100
                   ....*....|....*....|
gi 90193624     82 -AEGLTTLGQSLRTAFDLLN 100
Cdd:smart00327  74 kLGGGTNLGAALQYALENLF 93
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 4-105 1.60e-05

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 42.01  E-value: 1.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193624   4 LLFLIDTSASMNQRShlgttyLDTAKGAVETFM-KLRArdpasrGDRYMLVTFEE------PPYAIkagwkENHATFMNE 76
Cdd:COG2304  94 LVFVIDVSGSMSGDK------LELAKEAAKLLVdQLRP------GDRVSIVTFAGdarvllPPTPA-----TDRAKILAA 156

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 90193624  77 LKNLQAEGLTTLGQSLRTAFDLLN-------LNRLV 105
Cdd:COG2304 157 IDRLQAGGGTALGAGLELAYELARkhfipgrVNRVI 192
YeaD2 COG1721
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];
4-99 4.30e-04

Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];


Pssm-ID: 441327 [Multi-domain]  Cd Length: 287  Bit Score: 37.88  E-value: 4.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193624   4 LLFLIDTSASMNQRSHlGTTYLDTAKGAVETFMKLRARdpasRGDRYMLVTF-EEPPYAIKAGWKENHAT-FMNELKNLQ 81
Cdd:COG1721 150 VVLLLDTSASMRFGSG-GPSKLDLAVEAAASLAYLALR----QGDRVGLLTFgDRVRRYLPPRRGRRHLLrLLEALARLE 224

                        90
                ....*....|....*...
gi 90193624  82 AEGLTTLGQSLRTAFDLL 99
Cdd:COG1721 225 PAGETDLAAALRRLARRL 242
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 4-100 4.54e-03

vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix.


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 34.88  E-value: 4.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193624   4 LLFLIDTSASMNQRShlgttyLDTAKGAVETFMK-LRArdpasrGDRYMLVTF-----EEPPYAIKAGwKENHATFMNEL 77
Cdd:cd01461   5 VVFVIDTSGSMSGTK------IEQTKEALLTALKdLPP------GDYFNIIGFsdtveEFSPSSVSAT-AENVAAAIEYV 71

                        90       100
                ....*....|....*....|...
gi 90193624  78 KNLQAEGLTTLGQSLRTAFDLLN 100
Cdd:cd01461  72 NRLQALGGTNMNDALEAALELLN 94
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 4-99 4.60e-03

VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 34.56  E-value: 4.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193624   4 LLFLIDTSASMNQRShlgttyLDTAKGAVETFM-KLRARDPASrgdrymLVTFE-EPPYAIKAGWKENHATFMNELKNLQ 81
Cdd:cd01465   3 LVFVIDRSGSMDGPK------LPLVKSALKLLVdQLRPDDRLA------IVTYDgAAETVLPATPVRDKAAILAAIDRLT 70

                        90
                ....*....|....*...
gi 90193624  82 AEGLTTLGQSLRTAFDLL 99
Cdd:cd01465  71 AGGSTAGGAGIQLGYQEA 88
vWA_BABAM1 cd21502
Von-Willebrand factor A (vWA) domain found in BRISC and BRCA1-A complex member 1; BRISC and ...
 4-98 7.15e-03

Von-Willebrand factor A (vWA) domain found in BRISC and BRCA1-A complex member 1; BRISC and BRCA1 A complex member 1 (BABAM1) is also known as Mediator of RAP80 interactions and targeting subunit of 40 kDa (MERIT40), New component of the BRCA1-A complex (NBA1), HSPC142, or C19orf620. It is a core component of the BRCA1-A and BRISC complexes that function in DNA double-strand break repair and immune signaling, and contain the lysine-63 linkage-specific BRCC36 subunit that is functionalized by scaffold subunits Abraxas and ABRO1, respectively. BABAM1 interacts with Rap80, BRCC36, BRCC45, and Abraxas to form the BRCA1-A complex, a lysine-63-Ub specific deubiquitinating enzyme (DUB) which specifically recognizes lysine-63-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). BRISC is a DUB complex containing three other subunits, BRCC36, ABRO1 and BRCC45. It specifically hydrolyzes lysine-63 polyubiquitin chains, and is involved in multiple biological processes, including IFN-mediated antiviral immune regulation and inflammatory reaction. BABAM1 likely serves as a scaffold protein by integrating other components to form a functional complex. Furthermore, BABAM1 has been shown to play a critical role in BRISC-mediated regulation of Tankyrase1 (TNKS1) function during spindle assembly; it directly binds to the ankyrin repeat cluster V (ARC-V) domain of TNKS1 via its RXXPEG motif. BABAM1 contains a Von-Willebrand factor A (vWA) domain that is distantly related to classical vWA domains.


Pssm-ID: 411071  Cd Length: 216  Bit Score: 34.53  E-value: 7.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193624   4 LLFLIDTSASMNQ---RSHLGTTY--LDTAKGAVETFMKLRARdpASRGDRYMLVTFEEppyaiKAGWkenHATFMNELK 78
Cdd:cd21502   5 IIFCIDLSEEMNTtpfESTNGSKYtrLDMLKRALELFVHTKSR--INPRHEFALVVLNE-----SASW---LQDFTSDPK 74

                        90       100
                ....*....|....*....|..
gi 90193624  79 NLQA--EGLTTlgQSLRTAFDL 98
Cdd:cd21502  75 DILSalDDLEP--SGSYDSFDL 94
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 4-99 8.89e-03

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 34.27  E-value: 8.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193624   4 LLFLIDTSASMnqrshlGTTYLDTAKGAVETFMKLRArdpasRGDRYMLVTFEEPPYA-IKAGWKENHATFMNELKNLQA 82
Cdd:COG2425 121 VVLCVDTSGSM------AGSKEAAAKAAALALLRALR-----PNRRFGVILFDTEVVEdLPLTADDGLEDAIEFLSGLFA 189

                        90
                ....*....|....*..
gi 90193624  83 EGLTTLGQSLRTAFDLL 99
Cdd:COG2425 190 GGGTDIAPALRAALELL 206
 
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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