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Conserved domains on  [gi|1034673777|ref|XP_016884838|]
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integrator complex subunit 6-like isoform X16 [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|12579041|12388743
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 5.39e-17

von Willebrand factor type A domain;


:

Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 70.40  E-value: 5.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673777   4 LLFLIDTSASMNQRtDLGTSYLDIAKGAVELFLKLRardpasRGDRYMLVTYDEPPYcIKAGWKENHATFMSELKNLQA- 82
Cdd:pfam13519   1 LVFVLDTSGSMRNG-DYGPTRLEAAKDAVLALLKSL------PGDRVGLVTFGDGPE-VLIPLTKDRAKILRALRRLEPk 72

                          90       100
                  ....*....|....*....|.
gi 1034673777  83 SGLTTLGQALRSSFDLLNLNR 103
Cdd:pfam13519  73 GGGTNLAAALQLARAALKHRR 93
 
Name Accession Description Interval E-value
VWA_2 pfam13519
von Willebrand factor type A domain;
4-103 5.39e-17

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 70.40  E-value: 5.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673777   4 LLFLIDTSASMNQRtDLGTSYLDIAKGAVELFLKLRardpasRGDRYMLVTYDEPPYcIKAGWKENHATFMSELKNLQA- 82
Cdd:pfam13519   1 LVFVLDTSGSMRNG-DYGPTRLEAAKDAVLALLKSL------PGDRVGLVTFGDGPE-VLIPLTKDRAKILRALRRLEPk 72

                          90       100
                  ....*....|....*....|.
gi 1034673777  83 SGLTTLGQALRSSFDLLNLNR 103
Cdd:pfam13519  73 GGGTNLAAALQLARAALKHRR 93
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 4-100 3.33e-10

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: 54.11  E-value: 3.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673777   4 LLFLIDTSASMnqrtdlGTSYLDIAKGAVELFLKlrARDPASRGDRYMLVTYDEPPYCI----KAGWKENHATFMSELKN 79
Cdd:cd00198     3 IVFLLDVSGSM------GGEKLDKAKEALKALVS--SLSASPPGDRVGLVTFGSNARVVlpltTDTDKADLLEAIDALKK 74

                          90       100
                  ....*....|....*....|.
gi 1034673777  80 lQASGLTTLGQALRSSFDLLN 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 5.21e-10

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: 54.94  E-value: 5.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673777   4 LLFLIDTSASMnqrtdLGTSYLDIAKGAVELFLKLrardpASRGDRYMLVTYDEPPYcIKAGWKENHATFMSELKNLQAS 83
Cdd:COG1240    95 VVLVVDASGSM-----AAENRLEAAKGALLDFLDD-----YRPRDRVGLVAFGGEAE-VLLPLTRDREALKRALDELPPG 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034673777  84 GLTTLGQALRSSFDLLNLNR--------LIS-GIDNYGQV 114
Cdd:COG1240   164 GGTPLGDALALALELLKRADparrkvivLLTdGRDNAGRI 203
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 4-100 9.01e-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: 45.14  E-value: 9.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673777    4 LLFLIDTSASMNQrtdlgtSYLDIAKGAVELFLKLRARDPasRGDRYMLVTYDEPPYCIKA-GWKENHATFMSELKNLQ- 81
Cdd:smart00327   2 VVFLLDGSGSMGG------NRFELAKEFVLKLVEQLDIGP--DGDRVGLVTFSDDARVLFPlNDSRSKDALLEALASLSy 73

                           90       100
                   ....*....|....*....|
gi 1034673777   82 -ASGLTTLGQALRSSFDLLN 100
Cdd:smart00327  74 kLGGGTNLGAALQYALENLF 93
 
Name Accession Description Interval E-value
VWA_2 pfam13519
von Willebrand factor type A domain;
4-103 5.39e-17

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 70.40  E-value: 5.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673777   4 LLFLIDTSASMNQRtDLGTSYLDIAKGAVELFLKLRardpasRGDRYMLVTYDEPPYcIKAGWKENHATFMSELKNLQA- 82
Cdd:pfam13519   1 LVFVLDTSGSMRNG-DYGPTRLEAAKDAVLALLKSL------PGDRVGLVTFGDGPE-VLIPLTKDRAKILRALRRLEPk 72

                          90       100
                  ....*....|....*....|.
gi 1034673777  83 SGLTTLGQALRSSFDLLNLNR 103
Cdd:pfam13519  73 GGGTNLAAALQLARAALKHRR 93
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 4-100 3.33e-10

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: 54.11  E-value: 3.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673777   4 LLFLIDTSASMnqrtdlGTSYLDIAKGAVELFLKlrARDPASRGDRYMLVTYDEPPYCI----KAGWKENHATFMSELKN 79
Cdd:cd00198     3 IVFLLDVSGSM------GGEKLDKAKEALKALVS--SLSASPPGDRVGLVTFGSNARVVlpltTDTDKADLLEAIDALKK 74

                          90       100
                  ....*....|....*....|.
gi 1034673777  80 lQASGLTTLGQALRSSFDLLN 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 5.21e-10

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: 54.94  E-value: 5.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673777   4 LLFLIDTSASMnqrtdLGTSYLDIAKGAVELFLKLrardpASRGDRYMLVTYDEPPYcIKAGWKENHATFMSELKNLQAS 83
Cdd:COG1240    95 VVLVVDASGSM-----AAENRLEAAKGALLDFLDD-----YRPRDRVGLVAFGGEAE-VLLPLTRDREALKRALDELPPG 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034673777  84 GLTTLGQALRSSFDLLNLNR--------LIS-GIDNYGQV 114
Cdd:COG1240   164 GGTPLGDALALALELLKRADparrkvivLLTdGRDNAGRI 203
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 4-100 9.01e-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: 45.14  E-value: 9.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673777    4 LLFLIDTSASMNQrtdlgtSYLDIAKGAVELFLKLRARDPasRGDRYMLVTYDEPPYCIKA-GWKENHATFMSELKNLQ- 81
Cdd:smart00327   2 VVFLLDGSGSMGG------NRFELAKEFVLKLVEQLDIGP--DGDRVGLVTFSDDARVLFPlNDSRSKDALLEALASLSy 73

                           90       100
                   ....*....|....*....|
gi 1034673777   82 -ASGLTTLGQALRSSFDLLN 100
Cdd:smart00327  74 kLGGGTNLGAALQYALENLF 93
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 4-105 8.34e-06

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 43.17  E-value: 8.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673777   4 LLFLIDTSASMNqrtdlGTSyLDIAKGAVELFL-KLRArdpasrGDRYMLVTYDE------PPycIKAgwkENHATFMSE 76
Cdd:COG2304    94 LVFVIDVSGSMS-----GDK-LELAKEAAKLLVdQLRP------GDRVSIVTFAGdarvllPP--TPA---TDRAKILAA 156

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034673777  77 LKNLQASGLTTLGQALRSSFDLLN-------LNRLI 105
Cdd:COG2304   157 IDRLQAGGGTALGAGLELAYELARkhfipgrVNRVI 192
YeaD2 COG1721
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];
4-93 1.88e-03

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


Pssm-ID: 441327 [Multi-domain]  Cd Length: 287  Bit Score: 36.34  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673777   4 LLFLIDTSASMNQRTDlGTSYLDIAKGAVELFLKLRARdpasRGDRYMLVTYDEPPYC-IKAGWKENHAT-FMSELKNLQ 81
Cdd:COG1721   150 VVLLLDTSASMRFGSG-GPSKLDLAVEAAASLAYLALR----QGDRVGLLTFGDRVRRyLPPRRGRRHLLrLLEALARLE 224

                          90
                  ....*....|..
gi 1034673777  82 ASGLTTLGQALR 93
Cdd:COG1721   225 PAGETDLAAALR 236
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 4-99 1.95e-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: 36.20  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673777   4 LLFLIDTSASMnqrtdlGTSYLDIAKGAVELFLKLRArdpasRGDRYMLVTYDEPPYC-IKAGWKENHATFMSELKNLQA 82
Cdd:COG2425   121 VVLCVDTSGSM------AGSKEAAAKAAALALLRALR-----PNRRFGVILFDTEVVEdLPLTADDGLEDAIEFLSGLFA 189

                          90
                  ....*....|....*..
gi 1034673777  83 SGLTTLGQALRSSFDLL 99
Cdd:COG2425   190 GGGTDIAPALRAALELL 206
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 2-99 3.65e-03

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 35.05  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673777   2 PI-LLFLIDTSASM-NQRTDlgtSYLDIAKGAVELFLKLRARDPASRGDRYMLVTY-DEP-PYCIKAGWKENHATFMSEL 77
Cdd:cd01480     2 PVdITFVLDSSESVgLQNFD---ITKNFVKRVAERFLKDYYRKDPAGSWRVGVVQYsDQQeVEAGFLRDIRNYTSLKEAV 78

                          90       100
                  ....*....|....*....|...
gi 1034673777  78 KNLQ-ASGLTTLGQALRSSFDLL 99
Cdd:cd01480    79 DNLEyIGGGTFTDCALKYATEQL 101
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 4-89 9.24e-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: 33.79  E-value: 9.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673777   4 LLFLIDTSASMNQRTdlgtsyLDIAKGAVELFL-KLRARDPASrgdrymLVTYD-EPPYCIKAGWKENHATFMSELKNLQ 81
Cdd:cd01465     3 LVFVIDRSGSMDGPK------LPLVKSALKLLVdQLRPDDRLA------IVTYDgAAETVLPATPVRDKAAILAAIDRLT 70


                  ....*...
gi 1034673777  82 ASGLTTLG 89
Cdd:cd01465    71 AGGSTAGG 78
 
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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