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Conserved domains on  [gi|153945852|ref|NP_079534|]
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von Willebrand factor A domain-containing protein 7 precursor [Homo sapiens]

Protein Classification

vWA domain-containing protein( domain architecture ID 630)

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
SCOP:  3000832

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
316-422 2.35e-04

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.


The actual alignment was detected with superfamily member cd00198:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 161  Bit Score: 42.55  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945852 316 LSFVLDTTGSMGEE-INAAKIQARHLVEQRRGSPmEPVHYVLVPFHDPGFgPVFTTSDPDSFWQQLNEIHAL----GGGD 390
Cdd:cd00198    3 IVFLLDVSGSMGGEkLDKAKEALKALVSSLSASP-PGDRVGLVTFGSNAR-VVLPLTTDTDKADLLEAIDALkkglGGGT 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 153945852 391 EPEmclSALQLAL------LHTPPLSDIFVFTDASPKD 422
Cdd:cd00198   81 NIG---AALRLALellksaKRPNARRVIILLTDGEPND 115
Het-C super family cl20332
Heterokaryon incompatibility protein Het-C; In filamentous fungi, het loci (for heterokaryon ...
163-190 2.02e-03

Heterokaryon incompatibility protein Het-C; In filamentous fungi, het loci (for heterokaryon incompatibility) are believed to regulate self/nonself-recognition during vegetative growth. As filamentous fungi grow, hyphal fusion occurs within an individual colony to form a network. Hyphal fusion can occur also between different individuals to form a heterokaryon, in which genetically distinct nuclei occupy a common cytoplasm. However, heterokaryotic cells are viable only if the individuals involved have identical alleles at all het loci.


The actual alignment was detected with superfamily member pfam07217:

Pssm-ID: 399889  Cd Length: 560  Bit Score: 41.84  E-value: 2.02e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 153945852  163 LGAALHALQDFYSHSNWVEL-----GEQQPHPH 190
Cdd:pfam07217 211 LGQALHCLEDFSAHSNYCELalremGYHNVFPH 243
 
Name Accession Description Interval E-value
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
316-422 2.35e-04

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: 42.55  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945852 316 LSFVLDTTGSMGEE-INAAKIQARHLVEQRRGSPmEPVHYVLVPFHDPGFgPVFTTSDPDSFWQQLNEIHAL----GGGD 390
Cdd:cd00198    3 IVFLLDVSGSMGGEkLDKAKEALKALVSSLSASP-PGDRVGLVTFGSNAR-VVLPLTTDTDKADLLEAIDALkkglGGGT 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 153945852 391 EPEmclSALQLAL------LHTPPLSDIFVFTDASPKD 422
Cdd:cd00198   81 NIG---AALRLALellksaKRPNARRVIILLTDGEPND 115
Het-C pfam07217
Heterokaryon incompatibility protein Het-C; In filamentous fungi, het loci (for heterokaryon ...
163-190 2.02e-03

Heterokaryon incompatibility protein Het-C; In filamentous fungi, het loci (for heterokaryon incompatibility) are believed to regulate self/nonself-recognition during vegetative growth. As filamentous fungi grow, hyphal fusion occurs within an individual colony to form a network. Hyphal fusion can occur also between different individuals to form a heterokaryon, in which genetically distinct nuclei occupy a common cytoplasm. However, heterokaryotic cells are viable only if the individuals involved have identical alleles at all het loci.


Pssm-ID: 399889  Cd Length: 560  Bit Score: 41.84  E-value: 2.02e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 153945852  163 LGAALHALQDFYSHSNWVEL-----GEQQPHPH 190
Cdd:pfam07217 211 LGQALHCLEDFSAHSNYCELalremGYHNVFPH 243
 
Name Accession Description Interval E-value
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
316-422 2.35e-04

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: 42.55  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945852 316 LSFVLDTTGSMGEE-INAAKIQARHLVEQRRGSPmEPVHYVLVPFHDPGFgPVFTTSDPDSFWQQLNEIHAL----GGGD 390
Cdd:cd00198    3 IVFLLDVSGSMGGEkLDKAKEALKALVSSLSASP-PGDRVGLVTFGSNAR-VVLPLTTDTDKADLLEAIDALkkglGGGT 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 153945852 391 EPEmclSALQLAL------LHTPPLSDIFVFTDASPKD 422
Cdd:cd00198   81 NIG---AALRLALellksaKRPNARRVIILLTDGEPND 115
Het-C pfam07217
Heterokaryon incompatibility protein Het-C; In filamentous fungi, het loci (for heterokaryon ...
163-190 2.02e-03

Heterokaryon incompatibility protein Het-C; In filamentous fungi, het loci (for heterokaryon incompatibility) are believed to regulate self/nonself-recognition during vegetative growth. As filamentous fungi grow, hyphal fusion occurs within an individual colony to form a network. Hyphal fusion can occur also between different individuals to form a heterokaryon, in which genetically distinct nuclei occupy a common cytoplasm. However, heterokaryotic cells are viable only if the individuals involved have identical alleles at all het loci.


Pssm-ID: 399889  Cd Length: 560  Bit Score: 41.84  E-value: 2.02e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 153945852  163 LGAALHALQDFYSHSNWVEL-----GEQQPHPH 190
Cdd:pfam07217 211 LGQALHCLEDFSAHSNYCELalremGYHNVFPH 243
 
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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