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Conserved domains on  [gi|1887643916|ref|WP_182195314|]
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VWA domain-containing protein [Pseudoalteromonas sp. 5Ae-yellow]

Protein Classification

vWA domain-containing protein( domain architecture ID 10106971)

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:  12388743|10830113|12579041
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 85-274 1.13e-73

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: 224.90  E-value: 1.13e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  85 EGRDIMLAVDLSGSMTEQDMAYngqyVDRLTMVKAVLSDFIEQRQGDRLGLILFGDTAFLQTPLTRDVKTVSKMLSEAQI 164
Cdd:cd01467     1 EGRDIMIALDVSGSMLAQDFVK----PSRLEAAKEVLSDFIDRRENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 165 GLVGRATAIGDALGLSVKRFANKDESNRIVVLLTDGQNTAGNLNPEDALLLAREEGIKVYTIGVGSDNPRgfsLFNVGGS 244
Cdd:cd01467    77 GLAGQGTAIGDAIGLAIKRLKNSEAKERVIVLLTDGENNAGEIDPATAAELAKNKGVRIYTIGVGKSGSG---PKPDGST 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 1887643916 245 SgsnLDERLLKKIAEQTGGLYFRAKDVAGL 274
Cdd:cd01467   154 I---LDEDSLVEIADKTGGRIFRALDGFEL 180
 
Name Accession Description Interval E-value
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 85-274 1.13e-73

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: 224.90  E-value: 1.13e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  85 EGRDIMLAVDLSGSMTEQDMAYngqyVDRLTMVKAVLSDFIEQRQGDRLGLILFGDTAFLQTPLTRDVKTVSKMLSEAQI 164
Cdd:cd01467     1 EGRDIMIALDVSGSMLAQDFVK----PSRLEAAKEVLSDFIDRRENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 165 GLVGRATAIGDALGLSVKRFANKDESNRIVVLLTDGQNTAGNLNPEDALLLAREEGIKVYTIGVGSDNPRgfsLFNVGGS 244
Cdd:cd01467    77 GLAGQGTAIGDAIGLAIKRLKNSEAKERVIVLLTDGENNAGEIDPATAAELAKNKGVRIYTIGVGKSGSG---PKPDGST 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 1887643916 245 SgsnLDERLLKKIAEQTGGLYFRAKDVAGL 274
Cdd:cd01467   154 I---LDEDSLVEIADKTGGRIFRALDGFEL 180
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1-282 1.67e-59

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: 191.69  E-value: 1.67e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916   1 MFEFSWPWLFLLLPLPLLLLLLKPAVSNASTRLRIPSFAKHNLTSQSIEPHARRLNPFEWIIWLLLVTAAANPTWLDEPI 80
Cdd:COG1240     7 LALLLLLALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLAL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  81 SLPNEGRDIMLAVDLSGSMTEQDmayngqyvdRLTMVKAVLSDFIEQ-RQGDRLGLILFGDTAFLQTPLTRDVKTVSKML 159
Cdd:COG1240    87 ARPQRGRDVVLVVDASGSMAAEN---------RLEAAKGALLDFLDDyRPRDRVGLVAFGGEAEVLLPLTRDREALKRAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 160 SEAQIGlvGRaTAIGDALGLSVKRFANKDES-NRIVVLLTDGQNTAGNLNPEDALLLAREEGIKVYTIGVGSDnprgfsl 238
Cdd:COG1240   158 DELPPG--GG-TPLGDALALALELLKRADPArRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTE------- 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1887643916 239 fnvggssgsNLDERLLKKIAEQTGGLYFRAKDVAGLQQIYAELD 282
Cdd:COG1240   228 ---------AVDEGLLREIAEATGGRYFRADDLSELAAIYREID 262
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 88-276 3.70e-25

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: 99.45  E-value: 3.70e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916   88 DIMLAVDLSGSMTEQDMAYngqyvdRLTMVKAVLSDFIEQRQGDRLGLILFGDTAFLQTPL--TRDVKTVSKMLSEAQIG 165
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFEL------AKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLndSRSKDALLEALASLSYK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  166 LVGRaTAIGDALGLSVKRFANKDESNR-----IVVLLTDGQNTAGNLNPEDALLLAREEGIKVYTIGVGSDNprgfslfn 240
Cdd:smart00327  75 LGGG-TNLGAALQYALENLFSKSAGSRrgapkVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDV-------- 145

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1887643916  241 vggssgsnlDERLLKKIAEQTGGLYFRAKDVAGLQQ 276
Cdd:smart00327 146 ---------DEEELKKLASAPGGVYVFLPELLDLLI 172
VWA pfam00092
von Willebrand factor type A domain;
88-280 1.12e-24

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 98.12  E-value: 1.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  88 DIMLAVDLSGSMTEQDMAYngqyvdRLTMVKAVLSDFIEQRQGDRLGLILFGDTAFLQTPLTrDVKTVSKMLSEAQIGLV 167
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEK------VKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLN-DYSSKEELLSAVDNLRY 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 168 --GRATAIGDALGLSVKRFANKDESNR-----IVVLLTDGQNTAGNlnPEDALLLAREEGIKVYTIGVGSDnprgfslfn 240
Cdd:pfam00092  74 lgGGTTNTGKALKYALENLFSSAAGARpgapkVVVLLTDGRSQDGD--PEEVARELKSAGVTVFAVGVGNA--------- 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1887643916 241 vggssgsnlDERLLKKIA-EQTGGLYFRAKDVAGLQQIYAE 280
Cdd:pfam00092 143 ---------DDEELRKIAsEPGEGHVFTVSDFEALEDLQDQ 174
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 89-304 7.32e-14

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 70.80  E-value: 7.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  89 IMLAVDLSGSMTEQdmayngqyvdrLTMVKAVLSDFIEQ--RQGDRLGLILFGDTAFLQTPLTRDVKTVSKMLSEAQIGL 166
Cdd:TIGR03436  56 VGLVIDTSGSMRND-----------LDRARAAAIRFLKTvlRPNDRVFVVTFNTRLRLLQDFTSDPRLLEAALNRLKPPL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 167 V------------GRATAIGDALGLSVKRFANKDESN----RIVVLLTDGQNTAGNLNPEDALLLAREEGIKVYTIGV-G 229
Cdd:TIGR03436 125 RtdynssgafvrdGGGTALYDAITLAALEQLANALAGipgrKALIVISDGGDNRSRDTLERAIDAAQRADVAIYSIDArG 204

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1887643916 230 SDNPRGFSlfnvgGSSGSNLDERLLKKIAEQTGGLYFRAkDVAGLQQIYAEldklepISADeqtFRPQSSLFYYP 304
Cdd:TIGR03436 205 LRAPDLGA-----GAKAGLGGPEALERLAEETGGRAFYV-NSNDLDGAFAQ------IAEE---LRSQYLIGYYP 264
PRK13685 PRK13685
hypothetical protein; Provisional
 64-281 7.70e-13

hypothetical protein; Provisional


Pssm-ID: 184242 [Multi-domain]  Cd Length: 326  Bit Score: 68.19  E-value: 7.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  64 LLLVTAAANPTwldEPISLPNEGRDIMLAVDLSGSMTEQDMAYNgqyvdRLTMVKAVLSDFIEQ-RQGDRLGLILFGDTA 142
Cdd:PRK13685   69 VLLTVAMAGPT---HDVRIPRNRAVVMLVIDVSQSMRATDVEPN-----RLAAAQEAAKQFADElTPGINLGLIAFAGTA 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 143 FLQTPLTRDVKTVSKMLSEAQIGlvgRATAIGDALGLSVKRFA---------NKDESNRIVvLLTDGQNTAGnLNPED-- 211
Cdd:PRK13685  141 TVLVSPTTNREATKNAIDKLQLA---DRTATGEAIFTALQAIAtvgavigggDTPPPARIV-LMSDGKETVP-TNPDNpr 215

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887643916 212 ----ALLLAREEGIKVYTIGVGSdnPRGFSLFNvGGSSGSNLDERLLKKIAEQTGGLYFRAKDVAGLQQIYAEL 281
Cdd:PRK13685  216 gaytAARTAKDQGVPISTISFGT--PYGSVEIN-GQRQPVPVDDESLKKIAQLSGGEFYTAASLEELRAVYATL 286
 
Name Accession Description Interval E-value
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 85-274 1.13e-73

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: 224.90  E-value: 1.13e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  85 EGRDIMLAVDLSGSMTEQDMAYngqyVDRLTMVKAVLSDFIEQRQGDRLGLILFGDTAFLQTPLTRDVKTVSKMLSEAQI 164
Cdd:cd01467     1 EGRDIMIALDVSGSMLAQDFVK----PSRLEAAKEVLSDFIDRRENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 165 GLVGRATAIGDALGLSVKRFANKDESNRIVVLLTDGQNTAGNLNPEDALLLAREEGIKVYTIGVGSDNPRgfsLFNVGGS 244
Cdd:cd01467    77 GLAGQGTAIGDAIGLAIKRLKNSEAKERVIVLLTDGENNAGEIDPATAAELAKNKGVRIYTIGVGKSGSG---PKPDGST 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 1887643916 245 SgsnLDERLLKKIAEQTGGLYFRAKDVAGL 274
Cdd:cd01467   154 I---LDEDSLVEIADKTGGRIFRALDGFEL 180
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1-282 1.67e-59

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: 191.69  E-value: 1.67e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916   1 MFEFSWPWLFLLLPLPLLLLLLKPAVSNASTRLRIPSFAKHNLTSQSIEPHARRLNPFEWIIWLLLVTAAANPTWLDEPI 80
Cdd:COG1240     7 LALLLLLALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLAL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  81 SLPNEGRDIMLAVDLSGSMTEQDmayngqyvdRLTMVKAVLSDFIEQ-RQGDRLGLILFGDTAFLQTPLTRDVKTVSKML 159
Cdd:COG1240    87 ARPQRGRDVVLVVDASGSMAAEN---------RLEAAKGALLDFLDDyRPRDRVGLVAFGGEAEVLLPLTRDREALKRAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 160 SEAQIGlvGRaTAIGDALGLSVKRFANKDES-NRIVVLLTDGQNTAGNLNPEDALLLAREEGIKVYTIGVGSDnprgfsl 238
Cdd:COG1240   158 DELPPG--GG-TPLGDALALALELLKRADPArRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTE------- 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1887643916 239 fnvggssgsNLDERLLKKIAEQTGGLYFRAKDVAGLQQIYAELD 282
Cdd:COG1240   228 ---------AVDEGLLREIAEATGGRYFRADDLSELAAIYREID 262
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 64-281 1.94e-27

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 108.65  E-value: 1.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  64 LLLVTAAAnptwlDEPISLPNEGRDIMLAVDLSGSMteqdmayNGqyvDRLTMVKAVLSDFIEQ-RQGDRLGLILFGDTA 142
Cdd:COG2304    74 LLLVGLQP-----PKAAAEERPPLNLVFVIDVSGSM-------SG---DKLELAKEAAKLLVDQlRPGDRVSIVTFAGDA 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 143 FLQTPLTR--DVKTVSKMLSEAQiglVGRATAIGDALGLSVKRFANKDESNRI--VVLLTDGQNTAGNLNPEDALLLA-- 216
Cdd:COG2304   139 RVLLPPTPatDRAKILAAIDRLQ---AGGGTALGAGLELAYELARKHFIPGRVnrVILLTDGDANVGITDPEELLKLAee 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887643916 217 -REEGIKVYTIGVGSDnprgfslfnvggssgsnLDERLLKKIAEQTGGLYFRAKDVAGLQQIYAEL 281
Cdd:COG2304   216 aREEGITLTTLGVGSD-----------------YNEDLLERLADAGGGNYYYIDDPEEAEKVFVRE 264
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 87-266 3.68e-25

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: 99.18  E-value: 3.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  87 RDIMLAVDLSGSMTEQDMAYngqyvdRLTMVKAVLSDFIEQRQGDRLGLILFGDTAFLQTPLT--RDVKTVSKMLSEAQI 164
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDK------AKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTtdTDKADLLEAIDALKK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 165 GLVGRaTAIGDALGLSVKRFANKDESN--RIVVLLTDGQNTAGNLNPEDALLLAREEGIKVYTIGVGSDNprgfslfnvg 242
Cdd:cd00198    75 GLGGG-TNIGAALRLALELLKSAKRPNarRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDA---------- 143

                         170       180
                  ....*....|....*....|....
gi 1887643916 243 gssgsnlDERLLKKIAEQTGGLYF 266
Cdd:cd00198   144 -------NEDELKEIADKTTGGAV 160
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 88-276 3.70e-25

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: 99.45  E-value: 3.70e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916   88 DIMLAVDLSGSMTEQDMAYngqyvdRLTMVKAVLSDFIEQRQGDRLGLILFGDTAFLQTPL--TRDVKTVSKMLSEAQIG 165
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFEL------AKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLndSRSKDALLEALASLSYK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  166 LVGRaTAIGDALGLSVKRFANKDESNR-----IVVLLTDGQNTAGNLNPEDALLLAREEGIKVYTIGVGSDNprgfslfn 240
Cdd:smart00327  75 LGGG-TNLGAALQYALENLFSKSAGSRrgapkVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDV-------- 145

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1887643916  241 vggssgsnlDERLLKKIAEQTGGLYFRAKDVAGLQQ 276
Cdd:smart00327 146 ---------DEEELKKLASAPGGVYVFLPELLDLLI 172
VWA pfam00092
von Willebrand factor type A domain;
88-280 1.12e-24

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 98.12  E-value: 1.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  88 DIMLAVDLSGSMTEQDMAYngqyvdRLTMVKAVLSDFIEQRQGDRLGLILFGDTAFLQTPLTrDVKTVSKMLSEAQIGLV 167
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEK------VKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLN-DYSSKEELLSAVDNLRY 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 168 --GRATAIGDALGLSVKRFANKDESNR-----IVVLLTDGQNTAGNlnPEDALLLAREEGIKVYTIGVGSDnprgfslfn 240
Cdd:pfam00092  74 lgGGTTNTGKALKYALENLFSSAAGARpgapkVVVLLTDGRSQDGD--PEEVARELKSAGVTVFAVGVGNA--------- 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1887643916 241 vggssgsnlDERLLKKIA-EQTGGLYFRAKDVAGLQQIYAE 280
Cdd:pfam00092 143 ---------DDEELRKIAsEPGEGHVFTVSDFEALEDLQDQ 174
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 52-236 2.52e-20

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 88.58  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  52 ARRLNPFEWIIWLLLVTAAANPTWLDEPISLPNEGRDIMLAVDLSGSMTEqdmayngqyvDRLTMVKAVLSDFIE-QRQG 130
Cdd:COG2425    84 LLDALLLAVLLLALLLLAALLLLAAPASAAVPLLEGPVVLCVDTSGSMAG----------SKEAAAKAAALALLRaLRPN 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 131 DRLGLILFGDTAFLQTPLTRDvKTVSKMLSEAQIGLVGRATAIGDALGLSVKRFANKDESNRIVVLLTDGQNtagNLNPE 210
Cdd:COG2425   154 RRFGVILFDTEVVEDLPLTAD-DGLEDAIEFLSGLFAGGGTDIAPALRAALELLEEPDYRNADIVLITDGEA---GVSPE 229

                         170       180
                  ....*....|....*....|....*...
gi 1887643916 211 D--ALLLAREEGIKVYTIGVGSDNPRGF 236
Cdd:COG2425   230 EllREVRAKESGVRLFTVAIGDAGNPGL 257
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 88-232 3.26e-16

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: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 74.64  E-value: 3.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  88 DIMLAVDLSGSMTEQDMAYngqyvdrltmVKAVLSDFIEQ----RQGDRLGLILFGDTAFLQTPLTR--DVKTVSKMLSE 161
Cdd:cd01450     2 DIVFLLDGSESVGPENFEK----------VKDFIEKLVEKldigPDKTRVGLVQYSDDVRVEFSLNDykSKDDLLKAVKN 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1887643916 162 AQIgLVGRATAIGDALGLSVKRFANKDES----NRIVVLLTDGQNTAGNlNPEDALLLAREEGIKVYTIGVGSDN 232
Cdd:cd01450    72 LKY-LGGGGTNTGKALQYALEQLFSESNArenvPKVIIVLTDGRSDDGG-DPKEAAAKLKDEGIKVFVVGVGPAD 144
VWA_2 pfam13519
von Willebrand factor type A domain;
89-197 2.70e-15

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 70.40  E-value: 2.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  89 IMLAVDLSGSMTEQDMAYNgqyvdRLTMVKAVLSDFIEQRQGDRLGLILFGDTAFLQTPLTRDVKTVSKMLSEAQIglVG 168
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPT-----RLEAAKDAVLALLKSLPGDRVGLVTFGDGPEVLIPLTKDRAKILRALRRLEP--KG 73

                          90       100       110
                  ....*....|....*....|....*....|
gi 1887643916 169 RATAIGDALGLSVKRFANKDES-NRIVVLL 197
Cdd:pfam13519  74 GGTNLAAALQLARAALKHRRKNqPRRIVLI 103
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 66-274 4.53e-15

VWA ywmD 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. Not much is known about the function of the members of this subgroup. All members of this subgroup however have a conserved MIDAS motif.


Pssm-ID: 238733 [Multi-domain]  Cd Length: 206  Bit Score: 72.85  E-value: 4.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  66 LVTAAANPTWLDEPISLPnegRDIMLAVDLSGSMTEQDmaynGQYVDRLTMVKAVLSDFIEQ-RQGDRLGLILFGDTA-- 142
Cdd:cd01456     3 LGSPAFALEPVETEPQLP---PNVAIVLDNSGSMREVD----GGGETRLDNAKAALDETANAlPDGTRLGLWTFSGDGdn 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 143 -------FLQTPLTRDV--------KTVSKMLSEAQIGLVGraTAIGDALgLSVKRFANKDESNRiVVLLTDGQNTAGNL 207
Cdd:cd01456    76 pldvrvlVPKGCLTAPVngfpsaqrSALDAALNSLQTPTGW--TPLAAAL-AEAAAYVDPGRVNV-VVLITDGEDTCGPD 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1887643916 208 NPEDALLLAREE----GIKVYTIGVGSDNPRGfslfnvggssgsnlderLLKKIAEQTGGLYFR-AKDVAGL 274
Cdd:cd01456   152 PCEVARELAKRRtpapPIKVNVIDFGGDADRA-----------------ELEAIAEATGGTYAYnQSDLASL 206
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 89-304 7.32e-14

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 70.80  E-value: 7.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  89 IMLAVDLSGSMTEQdmayngqyvdrLTMVKAVLSDFIEQ--RQGDRLGLILFGDTAFLQTPLTRDVKTVSKMLSEAQIGL 166
Cdd:TIGR03436  56 VGLVIDTSGSMRND-----------LDRARAAAIRFLKTvlRPNDRVFVVTFNTRLRLLQDFTSDPRLLEAALNRLKPPL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 167 V------------GRATAIGDALGLSVKRFANKDESN----RIVVLLTDGQNTAGNLNPEDALLLAREEGIKVYTIGV-G 229
Cdd:TIGR03436 125 RtdynssgafvrdGGGTALYDAITLAALEQLANALAGipgrKALIVISDGGDNRSRDTLERAIDAAQRADVAIYSIDArG 204

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1887643916 230 SDNPRGFSlfnvgGSSGSNLDERLLKKIAEQTGGLYFRAkDVAGLQQIYAEldklepISADeqtFRPQSSLFYYP 304
Cdd:TIGR03436 205 LRAPDLGA-----GAKAGLGGPEALERLAEETGGRAFYV-NSNDLDGAFAQ------IAEE---LRSQYLIGYYP 264
PRK13685 PRK13685
hypothetical protein; Provisional
 64-281 7.70e-13

hypothetical protein; Provisional


Pssm-ID: 184242 [Multi-domain]  Cd Length: 326  Bit Score: 68.19  E-value: 7.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  64 LLLVTAAANPTwldEPISLPNEGRDIMLAVDLSGSMTEQDMAYNgqyvdRLTMVKAVLSDFIEQ-RQGDRLGLILFGDTA 142
Cdd:PRK13685   69 VLLTVAMAGPT---HDVRIPRNRAVVMLVIDVSQSMRATDVEPN-----RLAAAQEAAKQFADElTPGINLGLIAFAGTA 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 143 FLQTPLTRDVKTVSKMLSEAQIGlvgRATAIGDALGLSVKRFA---------NKDESNRIVvLLTDGQNTAGnLNPED-- 211
Cdd:PRK13685  141 TVLVSPTTNREATKNAIDKLQLA---DRTATGEAIFTALQAIAtvgavigggDTPPPARIV-LMSDGKETVP-TNPDNpr 215

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887643916 212 ----ALLLAREEGIKVYTIGVGSdnPRGFSLFNvGGSSGSNLDERLLKKIAEQTGGLYFRAKDVAGLQQIYAEL 281
Cdd:PRK13685  216 gaytAARTAKDQGVPISTISFGT--PYGSVEIN-GQRQPVPVDDESLKKIAQLSGGEFYTAASLEELRAVYATL 286
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 88-265 1.98e-11

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: 61.25  E-value: 1.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  88 DIMLAVDLSGSMTeqdmayngqyVDRLTMVKAVLSDFIEQ-RQGDRLGLILFGDTAFLQTPLTRDVKTVSKMLSEAQIGL 166
Cdd:cd01466     2 DLVAVLDVSGSMA----------GDKLQLVKHALRFVISSlGDADRLSIVTFSTSAKRLSPLRRMTAKGKRSAKRVVDGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 167 V-GRATAIGDALGLSVKRFANKDESNRI--VVLLTDGQNtagnlNPEDALLLAREEGIKVYTIGVGSDNprgfslfnvgg 243
Cdd:cd01466    72 QaGGGTNVVGGLKKALKVLGDRRQKNPVasIMLLSDGQD-----NHGAVVLRADNAPIPIHTFGLGASH----------- 135

                         170       180
                  ....*....|....*....|..
gi 1887643916 244 ssgsnlDERLLKKIAEQTGGLY 265
Cdd:cd01466   136 ------DPALLAFIAEITGGTF 151
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 88-228 7.45e-11

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 60.22  E-value: 7.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  88 DIMLAVDLSGSMteqdmayNGQYVDRLTMVKAVLSDFIeqRQGDRLGLILFGDTAFLQTPLTRDVKTVSKMLSEAQIGLV 167
Cdd:cd01474     6 DLYFVLDKSGSV-------AANWIEIYDFVEQLVDRFN--SPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTP 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887643916 168 GRATAIGDALGLSVKRFANKD----ESNRIVVLLTDGQNTA-GNLNPEDALLLAREEGIKVYTIGV 228
Cdd:cd01474    77 SGQTYIHEGLENANEQIFNRNgggrETVSVIIALTDGQLLLnGHKYPEHEAKLSRKLGAIVYCVGV 142
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 91-266 7.12e-09

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: 54.20  E-value: 7.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  91 LAVDLSGSMTEQdmayngqyvdRLTMVKAVLSDFIEQ-RQGDRLGLILFGDTAFLQTPLTRdVKTVSKMLSEAQIGLVGR 169
Cdd:cd01465     5 FVIDRSGSMDGP----------KLPLVKSALKLLVDQlRPDDRLAIVTYDGAAETVLPATP-VRDKAAILAAIDRLTAGG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 170 ATAIGDALGLS---VKRFANKDESNRIVvLLTDGQNTAGNLNPEDALLLA---REEGIKVYTIGVgsdnprgfslfnvgg 243
Cdd:cd01465    74 STAGGAGIQLGyqeAQKHFVPGGVNRIL-LATDGDFNVGETDPDELARLVaqkRESGITLSTLGF--------------- 137

                         170       180
                  ....*....|....*....|...
gi 1887643916 244 ssGSNLDERLLKKIAEQTGGLYF 266
Cdd:cd01465   138 --GDNYNEDLMEAIADAGNGNTA 158
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
88-231 3.49e-08

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 52.62  E-value: 3.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  88 DIMLAVDLSGSMteqdmayNGQYVDRL-----TMVKAVLSDFIEqRQGDRLGLILFGDTAFLQTPLTrdvkTVSKmLSEA 162
Cdd:COG4245     7 PVYLLLDTSGSM-------SGEPIEALneglqALIDELRQDPYA-LETVEVSVITFDGEAKVLLPLT----DLED-FQPP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 163 QIGlVGRATAIGDALGLSVKRFANKDESNR---------IVVLLTDGQNTAGNLNPEDALLLAREEG--IKVYTIGVGSD 231
Cdd:COG4245    74 DLS-ASGGTPLGAALELLLDLIERRVQKYTaegkgdwrpVVFLITDGEPTDSDWEAALQRLKDGEAAkkANIFAIGVGPD 152
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 89-267 1.76e-06

Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). In chlorophyll biosynthesis, insertion of Mg2+ into protoporphyrin IX is catalysed by magnesium chelatase in an ATP-dependent reaction. Magnesium chelatase is a three sub-unit (BchI, BchD and BchH) enzyme with a novel arrangement of domains: the C-terminal helical domain is located behind the nucleotide binding site. The BchD domain contains a AAA domain at its N-terminus and a VWA domain at its C-terminus. The VWA domain has been speculated to be involved in mediating protein-protein interactions.


Pssm-ID: 238728 [Multi-domain]  Cd Length: 178  Bit Score: 47.66  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  89 IMLAVDLSGSMteqdmAYNgqyvDRLTMVK-AVLS---DFIEQRqgDRLGLILF-GDTAFLQTPLTRDVKTVSKMLSEAQ 163
Cdd:cd01451     3 VIFVVDASGSM-----AAR----HRMAAAKgAVLSllrDAYQRR--DKVALIAFrGTEAEVLLPPTRSVELAKRRLARLP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 164 IGlvGRaTAIGDAL--GLSVKRFANKDESNR-IVVLLTDGQNTAGNLNPEDALLLA----REEGIKVYTIGVGsDNPRGF 236
Cdd:cd01451    72 TG--GG-TPLAAGLlaAYELAAEQARDPGQRpLIVVITDGRANVGPDPTADRALAAarklRARGISALVIDTE-GRPVRR 147

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1887643916 237 SlfnvggssgsnlderLLKKIAEQTGGLYFR 267
Cdd:cd01451   148 G---------------LAKDLARALGGQYVR 163
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 87-233 3.48e-06

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 46.45  E-value: 3.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  87 RDIMLAVDLSGSMTEQdmayNGQYVdrLTMVKAVLSDFIEQRQGDRLGLILFGDTAFLQTPLT--RDVKTVSKMLSEaqI 164
Cdd:cd01472     1 ADIVFLVDGSESIGLS----NFNLV--KDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNtyRSKDDVLEAVKN--L 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887643916 165 GLVGRATAIGDALG-----LSVKRFANKDESNRIVVLLTDGQNTAGNlnPEDALLLAREeGIKVYTIGVGSDNP 233
Cdd:cd01472    73 RYIGGGTNTGKALKyvrenLFTEASGSREGVPKVLVVITDGKSQDDV--EEPAVELKQA-GIEVFAVGVKNADE 143
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 88-230 1.61e-05

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 44.68  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  88 DIMLAVDLSGSMTEQDMayngqyvdrLTMVKAVLSDFIEQ----RQGDRLGLILFGDTAFLQTPLtRDVKTVSKMLSEAQ 163
Cdd:cd01471     2 DLYLLVDGSGSIGYSNW---------VTHVVPFLHTFVQNlnisPDEINLYLVTFSTNAKELIRL-SSPNSTNKDLALNA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 164 IGLV------GRATAIGDALgLSVKRF-----ANKDESNRIVVLLTDGQNTagnlNPEDALLLA---REEGIKVYTIGVG 229
Cdd:cd01471    72 IRALlslyypNGSTNTTSAL-LVVEKHlfdtrGNRENAPQLVIIMTDGIPD----SKFRTLKEArklRERGVIIAVLGVG 146


                  .
gi 1887643916 230 S 230
Cdd:cd01471   147 Q 147
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 88-245 6.76e-05

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: 43.14  E-value: 6.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  88 DIMLAVDLSGSMTEQDMAYNGQYVDRLtmVKAVLSDF-IEQRQGD-RLGLILFGDTAFLQTPLTRDVKTVSKmLSEAQIG 165
Cdd:cd01480     4 DITFVLDSSESVGLQNFDITKNFVKRV--AERFLKDYyRKDPAGSwRVGVVQYSDQQEVEAGFLRDIRNYTS-LKEAVDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 166 L--VGRATAIGDAL--GLSVKRFANKDESNRIVVLLTDGQNTAGNLN-PEDALLLAREEGIKVYTIGVGSDNPRGFSLFN 240
Cdd:cd01480    81 LeyIGGGTFTDCALkyATEQLLEGSHQKENKFLLVITDGHSDGSPDGgIEKAVNEADHLGIKIFFVAVGSQNEEPLSRIA 160


                  ....*
gi 1887643916 241 VGGSS 245
Cdd:cd01480   161 CDGKS 165
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 87-276 1.26e-04

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: 41.82  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  87 RDIMLAVDLSGSMTEQdmayngqyvdRLTMVKAVLSDFIEQ-RQGDRLGLILFGDTAFLQTP---------LTRDVKTVS 156
Cdd:cd01461     3 KEVVFVIDTSGSMSGT----------KIEQTKEALLTALKDlPPGDYFNIIGFSDTVEEFSPssvsataenVAAAIEYVN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 157 KMlseaqigLVGRATAIGDALGLSVKRFANKDESNRIVVLLTDGQNTagnlNPEDALLLARE---EGIKVYTIGVGSDnp 233
Cdd:cd01461    73 RL-------QALGGTNMNDALEAALELLNSSPGSVPQIILLTDGEVT----NESQILKNVREalsGRIRLFTFGIGSD-- 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1887643916 234 rgfslfnvggssgsnLDERLLKKIAEQTGGLYFRAKDVAGLQQ 276
Cdd:cd01461   140 ---------------VNTYLLERLAREGRGIARRIYETDDIES 167
YeaD2 COG1721
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];
87-199 1.81e-04

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


Pssm-ID: 441327 [Multi-domain]  Cd Length: 287  Bit Score: 42.50  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  87 RDIMLAVDLSGSMTEQDMAYNgqYVDRLTMVKAVLSdFIEQRQGDRLGLILFGDTAFLQTPLTRDVKTVSKMLSE-AQIG 165
Cdd:COG1721   148 LTVVLLLDTSASMRFGSGGPS--KLDLAVEAAASLA-YLALRQGDRVGLLTFGDRVRRYLPPRRGRRHLLRLLEAlARLE 224

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1887643916 166 LVGRaTAIGDALGLSVKRFANKDesnrIVVLLTD 199
Cdd:COG1721   225 PAGE-TDLAAALRRLARRLPRRS----LVVLISD 253
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 168-248 2.58e-04

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 41.15  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 168 GRATAIGDALGLSVKRFANKDESN----RIVVLLTDGQNTAGNLNP-EDALLLAREEGIKVYTIGVG--SDNprgfSLFN 240
Cdd:cd01473    82 GGETYIVEALKYGLKNYTKHGNRRkdapKVTMLFTDGNDTSASKKElQDISLLYKEENVKLLVVGVGaaSEN----KLKL 157


                  ....*...
gi 1887643916 241 VGGSSGSN 248
Cdd:cd01473   158 LAGCDINN 165
VWA_3 pfam13768
von Willebrand factor type A domain;
88-265 4.64e-04

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 40.07  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  88 DIMLAVDLSGSMTeqdmayngqyvDRLTMVKAVLSDFIEQ-RQGDRLGLILFGDTAFLQTPLTRDVKTVSKMLSEAQI-- 164
Cdd:pfam13768   2 DVVIVVDVSSSMS-----------GEPKLQKDALSVALRQlPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIkt 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 165 -----GLVGRATAIGDALGLSVKRfankdESNRIVVLLTDGQNTAGNLNPEDALLLAREEgIKVYTIGVGSDnprgfslf 239
Cdd:pfam13768  71 lqpplGGSDLLGALKEAVRAPASP-----GYIRHVLLLTDGSPMQGETRVSDLISRAPGK-IRFFAYGLGAS-------- 136

                         170       180
                  ....*....|....*....|....*.
gi 1887643916 240 nvggssgsnLDERLLKKIAEQTGGLY 265
Cdd:pfam13768 137 ---------ISAPMLQLLAEASNGTY 153
vWA_F11C1-5a_type cd01455
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 91-277 7.92e-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. Not much is known about the functions of the members of this subgroup. The members of this subgroup are fused to the ancient AAA domain.


Pssm-ID: 238732  Cd Length: 191  Bit Score: 39.82  E-value: 7.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  91 LAVDLSGSMTEQDmAYNGQYVDRL---TMVKAVLSDFIEQRQGDRLG------LILFGDTAFLQTPLTRDVKTVSKMLSE 161
Cdd:cd01455     5 LVVDVSGSMYRFN-GYDGRLDRSLeavVMVMEAFDGFEDKIQYDIIGhsgdgpCVPFVKTNHPPKNNKERLETLKMMHAH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 162 AQIGLVGRATAigDALGLSVKRFANKDE-SNRIVVLLTDGQNTAGNLNPED-ALLLAREEGIKVYTIGVGSdnprgfslf 239
Cdd:cd01455    84 SQFCWSGDHTV--EATEFAIKELAAKEDfDEAIVIVLSDANLERYGIQPKKlADALAREPNVNAFVIFIGS--------- 152

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1887643916 240 nvggssgsnLDERLLKKIAEQTGGLYFRAKDVAGLQQI 277
Cdd:cd01455   153 ---------LSDEADQLQRELPAGKAFVCMDTSELPHI 181
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 88-234 1.05e-03

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: 38.87  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  88 DIMLAVDLSGSMTEQDMAYNGqyvdrlTMVKAVLSDFIeqRQGDRLGLILFGDTAFLQ-TPLTRDVKTVSKMLSEAQIGl 166
Cdd:cd01462     2 PVILLVDQSGSMYGAPEEVAK------AVALALLRIAL--AENRDTYLILFDSEFQTKiVDKTDDLEEPVEFLSGVQLG- 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1887643916 167 vGrATAIGDALGLSVKRFANKDESNRIVVLLTDGQNTAGNLNPEDALLLAREEGIKVYTIGVG-SDNPR 234
Cdd:cd01462    73 -G-GTDINKALRYALELIERRDPRKADIVLITDGYEGGVSDELLREVELKRSRVARFVALALGdHGNPG 139
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 88-278 1.61e-03

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 39.19  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  88 DIMLAVDLSGSMTEQDmayngqyvdrLTMVKAVLSDFIEQ----RQGDRLGLILFGDTAF----LQTPLTRDVKTVSKML 159
Cdd:cd01470     2 NIYIALDASDSIGEED----------FDEAKNAIKTLIEKissyEVSPRYEIISYASDPKeivsIRDFNSNDADDVIKRL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916 160 SEAQIGLVG--RATAIGDAL-----GLSVKRFANKDESNRI---VVLLTDGQ-NTAGN-----------LNPEDALLLAR 217
Cdd:cd01470    72 EDFNYDDHGdkTGTNTAAALkkvyeRMALEKVRNKEAFNETrhvIILFTDGKsNMGGSplptvdkiknlVYKNNKSDNPR 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1887643916 218 EEGIKVYTIGVGSDnprgfslfnvggssgsnLDERLLKKIAEQTGGL--YFRAKDVAGLQQIY 278
Cdd:cd01470   152 EDYLDVYVFGVGDD-----------------VNKEELNDLASKKDNErhFFKLKDYEDLQEVF 197
vWA_BABAM1 cd21502
Von-Willebrand factor A (vWA) domain found in BRISC and BRCA1-A complex member 1; BRISC and ...
 88-159 5.05e-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: 37.61  E-value: 5.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1887643916  88 DIMLAVDLSGSM-TEQDMAYNGQYVDRLTMVKAVLSDFIEQR----QGDRLGLILFGDTAFLQTPLTRDVKTVSKML 159
Cdd:cd21502     4 KIIFCIDLSEEMnTTPFESTNGSKYTRLDMLKRALELFVHTKsrinPRHEFALVVLNESASWLQDFTSDPKDILSAL 80
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 88-229 7.30e-03

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 36.61  E-value: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887643916  88 DIMLAVDLSGSMteqdmayNGQYVDRLTMVKAVLSDFIEQRQGDRLGLILFG--DTAFLQTPLTR--DVKTVSKMLSEAQ 163
Cdd:cd01476     2 DLLFVLDSSGSV-------RGKFEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKhnDGEELLEKVDNLR 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1887643916 164 igLVGRATAIGDALGLSVKRFAN----KDESNRIVVLLTDGQNtagNLNPEDALLLAREE-GIKVYTIGVG 229
Cdd:cd01476    75 --FIGGTTATGAAIEVALQQLDPsegrREGIPKVVVVLTDGRS---HDDPEKQARILRAVpNIETFAVGTG 140
 
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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