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Conserved domains on  [gi|1799459548|gb|QHL87295|]
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hypothetical protein GU926_07555 [Nibribacter ruber]

Protein Classification

VWA domain-containing protein( domain architecture ID 11469209)

VWA (von Willebrand factor type A) domain-containing protein similar to Mycobacterium tuberculosis uncharacterized protein MT0986

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4867 COG4867
Uncharacterized conserved protein, contains von Willebrand factor type A (vWFA) domain ...
 1-366 0e+00

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


:

Pssm-ID: 443895 [Multi-domain]  Cd Length: 371  Bit Score: 547.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548   1 MSAGYRFTNFVPE---EPT-----QKGFEGLLNIFLQIITLTAGDVAEamswLNQLDQKYRLTD--DSYGMGDFFEDLKK 70
Cdd:COG4867     1 MMRGFRYGRYEPLglgDATgamqdLAELDALLEQLSQLLPGARLDDID----LDALDRQLGDTAavDARTLRDLERELRE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548  71 QGYIDDkGPDGQFQLQAKGEQKIRKSALEEIFGKLKKGGRGSHTTPKSGIGDEPNADRREFRFGDaPEQIELTESIRNAQ 150
Cdd:COG4867    77 QGYLRR-EADGGLELTPKAERRLGKSALRDIFGKLKKGRRGNHDTRRAGAGGELTGETRPWEFGD-TLPLDVTRTLRNAV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 151 IHHGLSDDFFLTENDLEVTEREHKTQTSTVLMIDISHSMILYGedRITPAKKVAMALAELVKLKYPKDNLDIIVFGNDAW 230
Cdd:COG4867   155 LRHGPGGPVRLDEEDLEVEETEYRTQAATVLMVDTSHSMILYG--RWTPAKKVALALAHLIRTRFPGDTLDIIVFGNDAW 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 231 QITVKDLPYLM-VGPYHTNTVAGLELAMDLLRRRKTSNKQIFMITDGKPTCLKE-GLKYYKNSFGLDRKVVNKTLNLAAQ 308
Cdd:COG4867   233 EVEIKELPYLQwVGPYGTNTHHGLLLARRLLRRHPNANKQILMITDGEPTAHLEpDGEYYKFSYPPDPETLAKTLAEVDR 312

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1799459548 309 CRRLNIPITTFMIASDPYLQQFVEEFTQVNNGQAYYSSLQGLGDLVFRDYGRNRKKRV 366
Cdd:COG4867   313 CRRLGIPITTFMLARDPYLARFVDEFTRRNGGRAYFPDLDGLGAYVVEDYLRNRRKRV 370
 
Name Accession Description Interval E-value
COG4867 COG4867
Uncharacterized conserved protein, contains von Willebrand factor type A (vWFA) domain ...
 1-366 0e+00

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


Pssm-ID: 443895 [Multi-domain]  Cd Length: 371  Bit Score: 547.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548   1 MSAGYRFTNFVPE---EPT-----QKGFEGLLNIFLQIITLTAGDVAEamswLNQLDQKYRLTD--DSYGMGDFFEDLKK 70
Cdd:COG4867     1 MMRGFRYGRYEPLglgDATgamqdLAELDALLEQLSQLLPGARLDDID----LDALDRQLGDTAavDARTLRDLERELRE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548  71 QGYIDDkGPDGQFQLQAKGEQKIRKSALEEIFGKLKKGGRGSHTTPKSGIGDEPNADRREFRFGDaPEQIELTESIRNAQ 150
Cdd:COG4867    77 QGYLRR-EADGGLELTPKAERRLGKSALRDIFGKLKKGRRGNHDTRRAGAGGELTGETRPWEFGD-TLPLDVTRTLRNAV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 151 IHHGLSDDFFLTENDLEVTEREHKTQTSTVLMIDISHSMILYGedRITPAKKVAMALAELVKLKYPKDNLDIIVFGNDAW 230
Cdd:COG4867   155 LRHGPGGPVRLDEEDLEVEETEYRTQAATVLMVDTSHSMILYG--RWTPAKKVALALAHLIRTRFPGDTLDIIVFGNDAW 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 231 QITVKDLPYLM-VGPYHTNTVAGLELAMDLLRRRKTSNKQIFMITDGKPTCLKE-GLKYYKNSFGLDRKVVNKTLNLAAQ 308
Cdd:COG4867   233 EVEIKELPYLQwVGPYGTNTHHGLLLARRLLRRHPNANKQILMITDGEPTAHLEpDGEYYKFSYPPDPETLAKTLAEVDR 312

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1799459548 309 CRRLNIPITTFMIASDPYLQQFVEEFTQVNNGQAYYSSLQGLGDLVFRDYGRNRKKRV 366
Cdd:COG4867   313 CRRLGIPITTFMLARDPYLARFVDEFTRRNGGRAYFPDLDGLGAYVVEDYLRNRRKRV 370
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 180-343 3.37e-15

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: 72.60  E-value: 3.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 180 VLMIDISHSMilyGEDRITPAKKVAMALAELVKLKYPKDNLDIIVFGNDA-----------WQITVKDLPYLMVGP-YHT 247
Cdd:cd00198     4 VFLLDVSGSM---GGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNArvvlplttdtdKADLLEAIDALKKGLgGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 248 NTVAGLELAMDLLRRRKTSN--KQIFMITDGKPTCLKEGLKyyknsfgldrkvvnktlNLAAQCRRLNIPITTFMIASDP 325
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNarRVIILLTDGEPNDGPELLA-----------------EAARELRKLGITVYTIGIGDDA 143

                         170
                  ....*....|....*...
gi 1799459548 326 YLQQFVEEFTQVNNGQAY 343
Cdd:cd00198   144 NEDELKEIADKTTGGAVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 180-286 3.85e-09

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: 55.54  E-value: 3.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548  180 VLMIDISHSMilyGEDRITPAKKVAMALAELVKLKYPKDNLDIIVFGNDAWQIT--------------VKDLPYLMVGPy 245
Cdd:smart00327   3 VFLLDGSGSM---GGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFplndsrskdalleaLASLSYKLGGG- 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1799459548  246 hTNTVAGLELAMDLL-----RRRKTSNKQIFMITDGKPTCLKEGLK 286
Cdd:smart00327  79 -TNLGAALQYALENLfsksaGSRRGAPKVVILITDGESNDGPKDLL 123
VWA_2 pfam13519
von Willebrand factor type A domain;
179-273 3.04e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 42.66  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 179 TVLMIDISHSMiLYGEDRITPAKKVAMALAELVKlKYPKDNLDIIVFGNDAwQITV---KDLPYLM-----VGPYH--TN 248
Cdd:pfam13519   1 LVFVLDTSGSM-RNGDYGPTRLEAAKDAVLALLK-SLPGDRVGLVTFGDGP-EVLIpltKDRAKILralrrLEPKGggTN 77

                          90       100
                  ....*....|....*....|....*.
gi 1799459548 249 TVAGLELAMDLL-RRRKTSNKQIFMI 273
Cdd:pfam13519  78 LAAALQLARAALkHRRKNQPRRIVLI 103
 
Name Accession Description Interval E-value
COG4867 COG4867
Uncharacterized conserved protein, contains von Willebrand factor type A (vWFA) domain ...
 1-366 0e+00

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


Pssm-ID: 443895 [Multi-domain]  Cd Length: 371  Bit Score: 547.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548   1 MSAGYRFTNFVPE---EPT-----QKGFEGLLNIFLQIITLTAGDVAEamswLNQLDQKYRLTD--DSYGMGDFFEDLKK 70
Cdd:COG4867     1 MMRGFRYGRYEPLglgDATgamqdLAELDALLEQLSQLLPGARLDDID----LDALDRQLGDTAavDARTLRDLERELRE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548  71 QGYIDDkGPDGQFQLQAKGEQKIRKSALEEIFGKLKKGGRGSHTTPKSGIGDEPNADRREFRFGDaPEQIELTESIRNAQ 150
Cdd:COG4867    77 QGYLRR-EADGGLELTPKAERRLGKSALRDIFGKLKKGRRGNHDTRRAGAGGELTGETRPWEFGD-TLPLDVTRTLRNAV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 151 IHHGLSDDFFLTENDLEVTEREHKTQTSTVLMIDISHSMILYGedRITPAKKVAMALAELVKLKYPKDNLDIIVFGNDAW 230
Cdd:COG4867   155 LRHGPGGPVRLDEEDLEVEETEYRTQAATVLMVDTSHSMILYG--RWTPAKKVALALAHLIRTRFPGDTLDIIVFGNDAW 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 231 QITVKDLPYLM-VGPYHTNTVAGLELAMDLLRRRKTSNKQIFMITDGKPTCLKE-GLKYYKNSFGLDRKVVNKTLNLAAQ 308
Cdd:COG4867   233 EVEIKELPYLQwVGPYGTNTHHGLLLARRLLRRHPNANKQILMITDGEPTAHLEpDGEYYKFSYPPDPETLAKTLAEVDR 312

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1799459548 309 CRRLNIPITTFMIASDPYLQQFVEEFTQVNNGQAYYSSLQGLGDLVFRDYGRNRKKRV 366
Cdd:COG4867   313 CRRLGIPITTFMLARDPYLARFVDEFTRRNGGRAYFPDLDGLGAYVVEDYLRNRRKRV 370
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 180-343 3.37e-15

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: 72.60  E-value: 3.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 180 VLMIDISHSMilyGEDRITPAKKVAMALAELVKLKYPKDNLDIIVFGNDA-----------WQITVKDLPYLMVGP-YHT 247
Cdd:cd00198     4 VFLLDVSGSM---GGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNArvvlplttdtdKADLLEAIDALKKGLgGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 248 NTVAGLELAMDLLRRRKTSN--KQIFMITDGKPTCLKEGLKyyknsfgldrkvvnktlNLAAQCRRLNIPITTFMIASDP 325
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNarRVIILLTDGEPNDGPELLA-----------------EAARELRKLGITVYTIGIGDDA 143

                         170
                  ....*....|....*...
gi 1799459548 326 YLQQFVEEFTQVNNGQAY 343
Cdd:cd00198   144 NEDELKEIADKTTGGAVF 161
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 123-354 1.82e-13

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: 69.58  E-value: 1.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 123 EPNADRREFRFGDAPEQIELTESIRNAQIHHGLSDDFFLTENDLEVTEREHKTQTSTVLMIDISHSMilYGEDRITPAKK 202
Cdd:COG1240    39 LLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSM--AAENRLEAAKG 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 203 vamALAELVKLKYPKDNLDIIVFGNDAWQI--------TVKD-LPYLMVGPYhTNTVAGLELAMDLLRR-RKTSNKQIFM 272
Cdd:COG1240   117 ---ALLDFLDDYRPRDRVGLVAFGGEAEVLlpltrdreALKRaLDELPPGGG-TPLGDALALALELLKRaDPARRKVIVL 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 273 ITDGKPTCLKEGLkyyknsfgldrkvvnktLNLAAQCRRLNIPITTFMIASDPYLQQFVEEFTQVNNGQAYY-SSLQGLG 351
Cdd:COG1240   193 LTDGRDNAGRIDP-----------------LEAAELAAAAGIRIYTIGVGTEAVDEGLLREIAEATGGRYFRaDDLSELA 255


                  ...
gi 1799459548 352 DLV 354
Cdd:COG1240   256 AIY 258
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 180-325 1.46e-10

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 61.23  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 180 VLMIDISHSMilyGEDRITPAKKVAMALAELVKlkyPKDNLDIIVFGNDA-WQITVKDLP-------YLMVGPYH--TNT 249
Cdd:COG2425   122 VLCVDTSGSM---AGSKEAAAKAAALALLRALR---PNRRFGVILFDTEVvEDLPLTADDgledaieFLSGLFAGggTDI 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799459548 250 VAGLELAMDLLRRRKTSNKQIFMITDGKPTCLKEGLkyyknsfgldrkvvnktLNLAAQcRRLNIPITTFMIASDP 325
Cdd:COG2425   196 APALRAALELLEEPDYRNADIVLITDGEAGVSPEEL-----------------LREVRA-KESGVRLFTVAIGDAG 253
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 180-286 3.85e-09

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: 55.54  E-value: 3.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548  180 VLMIDISHSMilyGEDRITPAKKVAMALAELVKLKYPKDNLDIIVFGNDAWQIT--------------VKDLPYLMVGPy 245
Cdd:smart00327   3 VFLLDGSGSM---GGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFplndsrskdalleaLASLSYKLGGG- 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1799459548  246 hTNTVAGLELAMDLL-----RRRKTSNKQIFMITDGKPTCLKEGLK 286
Cdd:smart00327  79 -TNLGAALQYALENLfsksaGSRRGAPKVVILITDGESNDGPKDLL 123
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 177-279 3.79e-08

norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate reductases. Denitrification plays a major role in completing the nitrogen cycle by converting nitrate or nitrite to nitrogen gas. The pathway for microbial denitrification has been established as NO3- ------> NO2- ------> NO -------> N2O ---------> N2. This reaction generally occurs under oxygen limiting conditions. Genetic and biochemical studies have shown that the first srep of the biochemical pathway is catalyzed by periplasmic nitrate reductases. This family is widely present in proteobacteria and firmicutes. This version of the domain is also present in some archaeal members. The function of the vWA domain in this sub-group is not known. Members of this subgroup have a conserved MIDAS motif.


Pssm-ID: 238731 [Multi-domain]  Cd Length: 174  Bit Score: 52.33  E-value: 3.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 177 TSTVLMIDISHSMilYGEDRITPAKKVAMALAElvKLKYPKDNLDIIVFGNDA-----------------WQITVKDLPY 239
Cdd:cd01454     1 LAVTLLLDLSGSM--RSDRRIDVAKKAAVLLAE--ALEACGVPHAILGFTTDAggrervrwikikdfdesLHERARKRLA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1799459548 240 LMVGPYHTNTVAGLELAMDLLRRRKTSNKQIFMITDGKPT 279
Cdd:cd01454    77 ALSPGGNTRDGAAIRHAAERLLARPEKRKILLVISDGEPN 116
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
180-279 1.05e-07

Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 51.46  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 180 VLMIDISHSMIlyGEdRITPAKK-VAMALAELVKLKYPKDNLDI--IVFGNDAWQI----TVKDL--PYLMVGPYhTNTV 250
Cdd:COG4245     9 YLLLDTSGSMS--GE-PIEALNEgLQALIDELRQDPYALETVEVsvITFDGEAKVLlpltDLEDFqpPDLSASGG-TPLG 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1799459548 251 AGLELAMDLLRRRKTSNKQ---------IFMITDGKPT 279
Cdd:COG4245    85 AALELLLDLIERRVQKYTAegkgdwrpvVFLITDGEPT 122
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 180-345 7.45e-07

VWA C3HC4-type: 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. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 48.54  E-value: 7.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 180 VLMIDISHSMilygedritPAKKVAM---ALAELVKLKYPKDNLDIIVFGNDA------WQITVKDLPYL--MVG---PY 245
Cdd:cd01466     4 VAVLDVSGSM---------AGDKLQLvkhALRFVISSLGDADRLSIVTFSTSAkrlsplRRMTAKGKRSAkrVVDglqAG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 246 H-TNTVAGLELAMDLLRRRKTSNK--QIFMITDGKPtclkeglkyyknsfgldrkvvnktlNLAAQCRRLN---IPITTF 319
Cdd:cd01466    75 GgTNVVGGLKKALKVLGDRRQKNPvaSIMLLSDGQD-------------------------NHGAVVLRADnapIPIHTF 129

                         170       180
                  ....*....|....*....|....*...
gi 1799459548 320 MIAS--DPYLQQFVEEFTqvnNGQAYYS 345
Cdd:cd01466   130 GLGAshDPALLAFIAEIT---GGTFSYV 154
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 180-276 8.18e-06

VWA BatA type: 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. Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif.


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 45.78  E-value: 8.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 180 VLMIDISHSMI---LYGEDRITPAKKVAMALAElvklKYPKDNLDIIVFGNDAWQ---ITV---------KDLPYLMVGP 244
Cdd:cd01467     6 MIALDVSGSMLaqdFVKPSRLEAAKEVLSDFID----RRENDRIGLVVFAGAAFTqapLTLdreslkellEDIKIGLAGQ 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1799459548 245 yHTNTVAGLELAMDLLRRRKTSNKQIFMITDG 276
Cdd:cd01467    82 -GTAIGDAIGLAIKRLKNSEAKERVIVLLTDG 112
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 180-276 1.81e-05

VWA YIEM type: 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. Members of this subgroup have a conserved MIDAS motif, however, their biochemical function is not well characterised.


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 44.26  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 180 VLMIDISHSMilyGEDRITPAKKVAMALAELvklkYPKDNLDI--IVFgNDAWQITVKDLP--------YLMVGPYH--T 247
Cdd:cd01462     4 ILLVDQSGSM---YGAPEEVAKAVALALLRI----ALAENRDTylILF-DSEFQTKIVDKTddleepveFLSGVQLGggT 75

                          90       100
                  ....*....|....*....|....*....
gi 1799459548 248 NTVAGLELAMDLLRRRKTSNKQIFMITDG 276
Cdd:cd01462    76 DINKALRYALELIERRDPRKADIVLITDG 104
VWA_2 pfam13519
von Willebrand factor type A domain;
179-273 3.04e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 42.66  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 179 TVLMIDISHSMiLYGEDRITPAKKVAMALAELVKlKYPKDNLDIIVFGNDAwQITV---KDLPYLM-----VGPYH--TN 248
Cdd:pfam13519   1 LVFVLDTSGSM-RNGDYGPTRLEAAKDAVLALLK-SLPGDRVGLVTFGDGP-EVLIpltKDRAKILralrrLEPKGggTN 77

                          90       100
                  ....*....|....*....|....*.
gi 1799459548 249 TVAGLELAMDLL-RRRKTSNKQIFMI 273
Cdd:pfam13519  78 LAAALQLARAALkHRRKNQPRRIVLI 103
YeaD2 COG1721
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];
111-275 1.31e-04

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


Pssm-ID: 441327 [Multi-domain]  Cd Length: 287  Bit Score: 43.27  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 111 GSHTTPKSGIGDEPnADRREFRFGDapeqielteSIRNaqIHHGLS---DDFFltendleVTEREHKTQTSTVLMIDISH 187
Cdd:COG1721    98 GEHRSRRRGDGTEF-AELREYQPGD---------DLRR--IDWKATartGELY-------VREFEEERELTVVLLLDTSA 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 188 SMiLYGEDRITP---AKKVAMALAELVKLKypKDNLDIIVFGNDAWQIT-----VKDLPYLM--VGPYHTNTVAGLELAM 257
Cdd:COG1721   159 SM-RFGSGGPSKldlAVEAAASLAYLALRQ--GDRVGLLTFGDRVRRYLpprrgRRHLLRLLeaLARLEPAGETDLAAAL 235

                         170
                  ....*....|....*...
gi 1799459548 258 DLLRRRKTSNKQIFMITD 275
Cdd:COG1721   236 RRLARRLPRRSLVVLISD 253
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 179-279 3.27e-04

VWA subfamily: 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. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 41.17  E-value: 3.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 179 TVLMIDISHSMIlyGEdritPAKKV----AMALAELVKLKYPKDN--LDIIVFGNDAWQITvkDLPYLM-------VGPY 245
Cdd:cd01464     6 IYLLLDTSGSMA--GE----PIEALnqglQMLQSELRQDPYALESveISVITFDSAARVIV--PLTPLEsfqpprlTASG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1799459548 246 HTNTVAGLELAMDLLRRRK--TSNKQ-------IFMITDGKPT 279
Cdd:cd01464    78 GTSMGAALELALDCIDRRVqrYRADQkgdwrpwVFLLTDGEPT 120
VWA pfam00092
von Willebrand factor type A domain;
180-279 3.85e-04

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 40.72  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 180 VLMIDISHSMilyGEDRITPAKKVAMALAELVKLKYPKDNLDIIVFGNDA---WQIT-----------VKDLPYLMVGPy 245
Cdd:pfam00092   3 VFLLDGSGSI---GGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVrteFPLNdysskeellsaVDNLRYLGGGT- 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1799459548 246 hTNTVAGLELAMDLLRR-----RKTSNKQIFMITDGKPT 279
Cdd:pfam00092  79 -TNTGKALKYALENLFSsaagaRPGAPKVVVLLTDGRSQ 116
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 180-344 2.28e-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: 38.41  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 180 VLMIDISHSMilyGEDRITPAKKvamALAELVKLKYPKDNLDIIVFGNDAWQI----TVKDLPYLM--VGPYH----TNT 249
Cdd:cd01465     4 VFVIDRSGSM---DGPKLPLVKS---ALKLLVDQLRPDDRLAIVTYDGAAETVlpatPVRDKAAILaaIDRLTaggsTAG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799459548 250 VAGLELAMDLLRR--RKTSNKQIFMITDGKPT-------CLKEglkyyknsfgldrkvvnktlnLAAQCRRLNIPITTFM 320
Cdd:cd01465    78 GAGIQLGYQEAQKhfVPGGVNRILLATDGDFNvgetdpdELAR---------------------LVAQKRESGITLSTLG 136

                         170       180
                  ....*....|....*....|....
gi 1799459548 321 IASDpYLQQFVEEFTQVNNGQAYY 344
Cdd:cd01465   137 FGDN-YNEDLMEAIADAGNGNTAY 159
 
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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