NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1104470122|ref|NP_001334276|]
View 

von Willebrand factor A domain-containing protein 7 isoform 2 precursor [Mus musculus]

Protein Classification

vWA domain-containing protein( domain architecture ID 1005168)

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
Gene Ontology:  GO:0009297
PubMed:  12579041|12388743
SCOP:  3000832

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ChlD super family cl34203
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 250-476 9.35e-05

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


The actual alignment was detected with superfamily member COG1240:

Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 44.93  E-value: 9.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104470122 250 FDQSSSQPPRGGINKDSTSPSFSPHHKLHLQAAEVALLASIEAFSLLRSRLGDKAFSRLLditpasslSFVLDTTGSMGE 329
Cdd:COG1240    36 LDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDV--------VLVVDASGSMAA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104470122 330 E--INAAKIQARRIVEQRQ-----------GSPmepvfYILVPFhdpgfgpvftTSDPDSFWQKLNEIHALGGgdepemc 396
Cdd:COG1240   108 EnrLEAAKGALLDFLDDYRprdrvglvafgGEA-----EVLLPL----------TRDREALKRALDELPPGGG------- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104470122 397 lSALEDALLT--NRVESLTRERRcRVTFLVTEDPSRTGGRRRREAL-----------------SPLRFEPYEAIARASGG 457
Cdd:COG1240   166 -TPLGDALALalELLKRADPARR-KVIVLLTDGRDNAGRIDPLEAAelaaaagiriytigvgtEAVDEGLLREIAEATGG 243

                         250
                  ....*....|....*....
gi 1104470122 458 EVIFTKDqyIQDVAAIVGE 476
Cdd:COG1240   244 RYFRADD--LSELAAIYRE 260
Het-C super family cl20332
Heterokaryon incompatibility protein Het-C; In filamentous fungi, het loci (for heterokaryon ...
 164-191 3.91e-04

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: 44.15  E-value: 3.91e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1104470122 164 LGAALHALQDFYSHSNWVEL-----GERQPHPH 191
Cdd:pfam07217 211 LGQALHCLEDFSAHSNYCELalremGYHNVFPH 243
 
Name Accession Description Interval E-value
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 250-476 9.35e-05

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: 44.93  E-value: 9.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104470122 250 FDQSSSQPPRGGINKDSTSPSFSPHHKLHLQAAEVALLASIEAFSLLRSRLGDKAFSRLLditpasslSFVLDTTGSMGE 329
Cdd:COG1240    36 LDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDV--------VLVVDASGSMAA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104470122 330 E--INAAKIQARRIVEQRQ-----------GSPmepvfYILVPFhdpgfgpvftTSDPDSFWQKLNEIHALGGgdepemc 396
Cdd:COG1240   108 EnrLEAAKGALLDFLDDYRprdrvglvafgGEA-----EVLLPL----------TRDREALKRALDELPPGGG------- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104470122 397 lSALEDALLT--NRVESLTRERRcRVTFLVTEDPSRTGGRRRREAL-----------------SPLRFEPYEAIARASGG 457
Cdd:COG1240   166 -TPLGDALALalELLKRADPARR-KVIVLLTDGRDNAGRIDPLEAAelaaaagiriytigvgtEAVDEGLLREIAEATGG 243

                         250
                  ....*....|....*....
gi 1104470122 458 EVIFTKDqyIQDVAAIVGE 476
Cdd:COG1240   244 RYFRADD--LSELAAIYRE 260
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 317-469 2.16e-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: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104470122 317 LSFVLDTTGSMGEE-INAAKIQARRIVEQRQGSPMEPVFYiLVPFHDPG--FGPVFTTSDPDSFWQKLNEIHALGGGDep 393
Cdd:cd00198     3 IVFLLDVSGSMGGEkLDKAKEALKALVSSLSASPPGDRVG-LVTFGSNArvVLPLTTDTDKADLLEAIDALKKGLGGG-- 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1104470122 394 emclSALEDALLT--NRVESLTRERRCRVTFLVTEDPSRTGGRRRREALSPLRFEPYEAIARASGGEVIFTKDQYIQD 469
Cdd:cd00198    80 ----TNIGAALRLalELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIAD 153
Het-C pfam07217
Heterokaryon incompatibility protein Het-C; In filamentous fungi, het loci (for heterokaryon ...
 164-191 3.91e-04

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: 44.15  E-value: 3.91e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1104470122 164 LGAALHALQDFYSHSNWVEL-----GERQPHPH 191
Cdd:pfam07217 211 LGQALHCLEDFSAHSNYCELalremGYHNVFPH 243
 
Name Accession Description Interval E-value
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 250-476 9.35e-05

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: 44.93  E-value: 9.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104470122 250 FDQSSSQPPRGGINKDSTSPSFSPHHKLHLQAAEVALLASIEAFSLLRSRLGDKAFSRLLditpasslSFVLDTTGSMGE 329
Cdd:COG1240    36 LDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDV--------VLVVDASGSMAA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104470122 330 E--INAAKIQARRIVEQRQ-----------GSPmepvfYILVPFhdpgfgpvftTSDPDSFWQKLNEIHALGGgdepemc 396
Cdd:COG1240   108 EnrLEAAKGALLDFLDDYRprdrvglvafgGEA-----EVLLPL----------TRDREALKRALDELPPGGG------- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104470122 397 lSALEDALLT--NRVESLTRERRcRVTFLVTEDPSRTGGRRRREAL-----------------SPLRFEPYEAIARASGG 457
Cdd:COG1240   166 -TPLGDALALalELLKRADPARR-KVIVLLTDGRDNAGRIDPLEAAelaaaagiriytigvgtEAVDEGLLREIAEATGG 243

                         250
                  ....*....|....*....
gi 1104470122 458 EVIFTKDqyIQDVAAIVGE 476
Cdd:COG1240   244 RYFRADD--LSELAAIYRE 260
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 317-469 2.16e-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: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104470122 317 LSFVLDTTGSMGEE-INAAKIQARRIVEQRQGSPMEPVFYiLVPFHDPG--FGPVFTTSDPDSFWQKLNEIHALGGGDep 393
Cdd:cd00198     3 IVFLLDVSGSMGGEkLDKAKEALKALVSSLSASPPGDRVG-LVTFGSNArvVLPLTTDTDKADLLEAIDALKKGLGGG-- 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1104470122 394 emclSALEDALLT--NRVESLTRERRCRVTFLVTEDPSRTGGRRRREALSPLRFEPYEAIARASGGEVIFTKDQYIQD 469
Cdd:cd00198    80 ----TNIGAALRLalELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIAD 153
Het-C pfam07217
Heterokaryon incompatibility protein Het-C; In filamentous fungi, het loci (for heterokaryon ...
 164-191 3.91e-04

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: 44.15  E-value: 3.91e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1104470122 164 LGAALHALQDFYSHSNWVEL-----GERQPHPH 191
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH