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Conserved domains on  [gi|490480609|ref|WP_004350938|]
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MULTISPECIES: VWA domain-containing protein [Pseudomonas]

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 ...
 89-277 5.17e-68

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: 211.03  E-value: 5.17e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  89 GRDLLLAVDVSGSMDYRDMRwqddEISRLELIKKLFGDFIEDRRGDRVGLILFGSQAYLQAPLTFDRHTVRVWLDEAQIG 168
Cdd:cd01467    2 GRDIMIALDVSGSMLAQDFV----KPSRLEAAKEVLSDFIDRRENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKIG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609 169 IAGKNTAIGDAIGLAVKRLRQRPAESRVLVLITDGANTGGQIAPQIAAQLAAEQQVKIYTIGIGADPQQggvpglFGFNP 248
Cdd:cd01467   78 LAGQGTAIGDAIGLAIKRLKNSEAKERVIVLLTDGENNAGEIDPATAAELAKNKGVRIYTIGVGKSGSG------PKPDG 151

                        170       180
                 ....*....|....*....|....*....
gi 490480609 249 GLDLDEPTLRGIAESTGGEYFRARSSAEL 277
Cdd:cd01467  152 STILDEDSLVEIADKTGGRIFRALDGFEL 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 ...
 89-277 5.17e-68

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: 211.03  E-value: 5.17e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  89 GRDLLLAVDVSGSMDYRDMRwqddEISRLELIKKLFGDFIEDRRGDRVGLILFGSQAYLQAPLTFDRHTVRVWLDEAQIG 168
Cdd:cd01467    2 GRDIMIALDVSGSMLAQDFV----KPSRLEAAKEVLSDFIDRRENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKIG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609 169 IAGKNTAIGDAIGLAVKRLRQRPAESRVLVLITDGANTGGQIAPQIAAQLAAEQQVKIYTIGIGADPQQggvpglFGFNP 248
Cdd:cd01467   78 LAGQGTAIGDAIGLAIKRLKNSEAKERVIVLLTDGENNAGEIDPATAAELAKNKGVRIYTIGVGKSGSG------PKPDG 151

                        170       180
                 ....*....|....*....|....*....
gi 490480609 249 GLDLDEPTLRGIAESTGGEYFRARSSAEL 277
Cdd:cd01467  152 STILDEDSLVEIADKTGGRIFRALDGFEL 180
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1-285 8.89e-52

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: 172.05  E-value: 8.89e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609   1 MFEFAWPWVFALAPLPWLLRLVLPAADSGEAALKVSFLDELESLAGRRARARLPAWRQQVRFALLWFLLLLAAARPQWVG 80
Cdd:COG1240    4 LALLALLLLLALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  81 DPLPLPASGRDLLLAVDVSGSMDYRDmrwqddeisRLELIKKLFGDFIED-RRGDRVGLILFGSQAYLQAPLTFDRHTVR 159
Cdd:COG1240   84 LALARPQRGRDVVLVVDASGSMAAEN---------RLEAAKGALLDFLDDyRPRDRVGLVAFGGEAEVLLPLTRDREALK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609 160 VWLDEAQigiAGKNTAIGDAIGLAVKRLRQ-RPAESRVLVLITDGANTGGQIAPQIAAQLAAEQQVKIYTIGIGADpqqg 238
Cdd:COG1240  155 RALDELP---PGGGTPLGDALALALELLKRaDPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTE---- 227

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 490480609 239 gvpglfgfnpglDLDEPTLRGIAESTGGEYFRARSSAELESISATLD 285
Cdd:COG1240  228 ------------AVDEGLLREIAEATGGRYFRADDLSELAAIYREID 262
VWA pfam00092
von Willebrand factor type A domain;
91-280 1.09e-27

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 106.59  E-value: 1.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609   91 DLLLAVDVSGSMDYRDMRwqddeiSRLELIKKLFGDFIEDRRGDRVGLILFGSQAYLQAPLTFDRH--TVRVWLDEAQIg 168
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFE------KVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSkeELLSAVDNLRY- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  169 IAGKNTAIGDAIGLAVKRLRQRPAESR-----VLVLITDGANTGGQIAPqiAAQLAAEQQVKIYTIGIGADpqqggvpgl 243
Cdd:pfam00092  74 LGGGTTNTGKALKYALENLFSSAAGARpgapkVVVLLTDGRSQDGDPEE--VARELKSAGVTVFAVGVGNA--------- 142

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 490480609  244 fgfnpgldlDEPTLRGIA-ESTGGEYFRARSSAELESI 280
Cdd:pfam00092 143 ---------DDEELRKIAsEPGEGHVFTVSDFEALEDL 171
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 91-277 3.48e-24

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: 97.14  E-value: 3.48e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609    91 DLLLAVDVSGSMDYRDMRWQddeisrLELIKKLFGDFIEDRRGDRVGLILFGSQAYLQAPL--TFDRHTVRVWLDEAQIG 168
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELA------KEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLndSRSKDALLEALASLSYK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609   169 iAGKNTAIGDAIGLAVKRL-----RQRPAESRVLVLITDGANTGGQIAPQIAAQLAAEQQVKIYTIGIGADPqqggvpgl 243
Cdd:smart00327  75 -LGGGTNLGAALQYALENLfsksaGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDV-------- 145

                          170       180       190
                   ....*....|....*....|....*....|....
gi 490480609   244 fgfnpgldlDEPTLRGIAESTGGEYFRARSSAEL 277
Cdd:smart00327 146 ---------DEEELKKLASAPGGVYVFLPELLDL 170
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 94-274 2.81e-13

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: 69.26  E-value: 2.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609   94 LAVDVSGSM-DYRDMrwqddeiSRLELIKklfgdFIED--RRGDRVGLILFGSQAYLQAPLTFDRHTVRVWLDEAQIGIA 170
Cdd:TIGR03436  58 LVIDTSGSMrNDLDR-------ARAAAIR-----FLKTvlRPNDRVFVVTFNTRLRLLQDFTSDPRLLEAALNRLKPPLR 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  171 GKN------------TAIGDAIGLAVKRLRQR----PAESRVLVLITDGANTGGQIAPQIAAQLAAEQQVKIYTIGI--- 231
Cdd:TIGR03436 126 TDYnssgafvrdgggTALYDAITLAALEQLANalagIPGRKALIVISDGGDNRSRDTLERAIDAAQRADVAIYSIDArgl 205

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 490480609  232 -GADPQQGGVPGLFGfnpgldldEPTLRGIAESTGGEYFRARSS 274
Cdd:TIGR03436 206 rAPDLGAGAKAGLGG--------PEALERLAEETGGRAFYVNSN 241
PRK13685 PRK13685
hypothetical protein; Provisional
 93-318 9.35e-13

hypothetical protein; Provisional


Pssm-ID: 184242 [Multi-domain]  Cd Length: 326  Bit Score: 68.19  E-value: 9.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  93 LLAVDVSGSMdyrdmRWQDDEISRLELIK---KLFGDfiEDRRGDRVGLILFGSQAYLQAPLTFDRHTVRVWLDEAQIGi 169
Cdd:PRK13685  92 MLVIDVSQSM-----RATDVEPNRLAAAQeaaKQFAD--ELTPGINLGLIAFAGTATVLVSPTTNREATKNAIDKLQLA- 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609 170 agKNTAIGDAIGLAVKRLR---------QRPAESRVlVLITDGANTGGQ--IAPQ---IAAQLAAEQQVKIYTIGIGA-- 233
Cdd:PRK13685 164 --DRTATGEAIFTALQAIAtvgavigggDTPPPARI-VLMSDGKETVPTnpDNPRgayTAARTAKDQGVPISTISFGTpy 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609 234 -----DPQQGGVPglfgfnpgldLDEPTLRGIAESTGGEYFRARSSAELESISATLDrlEPVAQQTTRA---RPALALYS 305
Cdd:PRK13685 241 gsveiNGQRQPVP----------VDDESLKKIAQLSGGEFYTAASLEELRAVYATLQ--QQIGYETIKGdasVGWLRLGA 308

                        250
                 ....*....|...
gi 490480609 306 WPLAAALGLSVLL 318
Cdd:PRK13685 309 LVLALAALAALLI 321
 
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 ...
 89-277 5.17e-68

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: 211.03  E-value: 5.17e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  89 GRDLLLAVDVSGSMDYRDMRwqddEISRLELIKKLFGDFIEDRRGDRVGLILFGSQAYLQAPLTFDRHTVRVWLDEAQIG 168
Cdd:cd01467    2 GRDIMIALDVSGSMLAQDFV----KPSRLEAAKEVLSDFIDRRENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKIG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609 169 IAGKNTAIGDAIGLAVKRLRQRPAESRVLVLITDGANTGGQIAPQIAAQLAAEQQVKIYTIGIGADPQQggvpglFGFNP 248
Cdd:cd01467   78 LAGQGTAIGDAIGLAIKRLKNSEAKERVIVLLTDGENNAGEIDPATAAELAKNKGVRIYTIGVGKSGSG------PKPDG 151

                        170       180
                 ....*....|....*....|....*....
gi 490480609 249 GLDLDEPTLRGIAESTGGEYFRARSSAEL 277
Cdd:cd01467  152 STILDEDSLVEIADKTGGRIFRALDGFEL 180
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1-285 8.89e-52

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: 172.05  E-value: 8.89e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609   1 MFEFAWPWVFALAPLPWLLRLVLPAADSGEAALKVSFLDELESLAGRRARARLPAWRQQVRFALLWFLLLLAAARPQWVG 80
Cdd:COG1240    4 LALLALLLLLALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  81 DPLPLPASGRDLLLAVDVSGSMDYRDmrwqddeisRLELIKKLFGDFIED-RRGDRVGLILFGSQAYLQAPLTFDRHTVR 159
Cdd:COG1240   84 LALARPQRGRDVVLVVDASGSMAAEN---------RLEAAKGALLDFLDDyRPRDRVGLVAFGGEAEVLLPLTRDREALK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609 160 VWLDEAQigiAGKNTAIGDAIGLAVKRLRQ-RPAESRVLVLITDGANTGGQIAPQIAAQLAAEQQVKIYTIGIGADpqqg 238
Cdd:COG1240  155 RALDELP---PGGGTPLGDALALALELLKRaDPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTE---- 227

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 490480609 239 gvpglfgfnpglDLDEPTLRGIAESTGGEYFRARSSAELESISATLD 285
Cdd:COG1240  228 ------------AVDEGLLREIAEATGGRYFRADDLSELAAIYREID 262
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 81-280 2.57e-28

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 111.35  E-value: 2.57e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  81 DPLPLPASGRDLLLAVDVSGSMDYrdmrwqddeiSRLELIKKLFGDFIED-RRGDRVGLILFGSQAYLQAPLTF--DRHT 157
Cdd:COG2304   83 KAAAEERPPLNLVFVIDVSGSMSG----------DKLELAKEAAKLLVDQlRPGDRVSIVTFAGDARVLLPPTPatDRAK 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609 158 VRVWLDEAQigiAGKNTAIGDAIGLAVKRLRQRPAESRV--LVLITDGANTGGQIAPQIAAQLAAEQQ---VKIYTIGIG 232
Cdd:COG2304  153 ILAAIDRLQ---AGGGTALGAGLELAYELARKHFIPGRVnrVILLTDGDANVGITDPEELLKLAEEAReegITLTTLGVG 229

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 490480609 233 AdpqqggvpglfgfnpglDLDEPTLRGIAESTGGEYFRARSSAELESI 280
Cdd:COG2304  230 S-----------------DYNEDLLERLADAGGGNYYYIDDPEEAEKV 260
VWA pfam00092
von Willebrand factor type A domain;
91-280 1.09e-27

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 106.59  E-value: 1.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609   91 DLLLAVDVSGSMDYRDMRwqddeiSRLELIKKLFGDFIEDRRGDRVGLILFGSQAYLQAPLTFDRH--TVRVWLDEAQIg 168
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFE------KVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSkeELLSAVDNLRY- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  169 IAGKNTAIGDAIGLAVKRLRQRPAESR-----VLVLITDGANTGGQIAPqiAAQLAAEQQVKIYTIGIGADpqqggvpgl 243
Cdd:pfam00092  74 LGGGTTNTGKALKYALENLFSSAAGARpgapkVVVLLTDGRSQDGDPEE--VARELKSAGVTVFAVGVGNA--------- 142

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 490480609  244 fgfnpgldlDEPTLRGIA-ESTGGEYFRARSSAELESI 280
Cdd:pfam00092 143 ---------DDEELRKIAsEPGEGHVFTVSDFEALEDL 171
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 90-235 1.23e-24

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: 98.02  E-value: 1.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  90 RDLLLAVDVSGSMdyRDMRWQddeiSRLELIKKLFGDFIEDRRGDRVGLILFGSQAYLQAPLTFDRHTVRVW--LDEAQI 167
Cdd:cd00198    1 ADIVFLLDVSGSM--GGEKLD----KAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLeaIDALKK 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609 168 GIAGkNTAIGDAIGLAVKRLRQ--RPAESRVLVLITDGANTGGQIAPQIAAQLAAEQQVKIYTIGIGADP 235
Cdd:cd00198   75 GLGG-GTNIGAALRLALELLKSakRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDA 143
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 91-277 3.48e-24

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: 97.14  E-value: 3.48e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609    91 DLLLAVDVSGSMDYRDMRWQddeisrLELIKKLFGDFIEDRRGDRVGLILFGSQAYLQAPL--TFDRHTVRVWLDEAQIG 168
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELA------KEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLndSRSKDALLEALASLSYK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609   169 iAGKNTAIGDAIGLAVKRL-----RQRPAESRVLVLITDGANTGGQIAPQIAAQLAAEQQVKIYTIGIGADPqqggvpgl 243
Cdd:smart00327  75 -LGGGTNLGAALQYALENLfsksaGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDV-------- 145

                          170       180       190
                   ....*....|....*....|....*....|....
gi 490480609   244 fgfnpgldlDEPTLRGIAESTGGEYFRARSSAEL 277
Cdd:smart00327 146 ---------DEEELKKLASAPGGVYVFLPELLDL 170
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 3-235 2.42e-18

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 83.19  E-value: 2.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609   3 EFAWPWVFALAPLPWLLRLVLPAADSGEAALKVSFLDELESLAGRRARARLPAWRQQVRFALLWFLLLLAAARPQWVGDP 82
Cdd:COG2425   32 AALALGLALALRAALLALLLLLLRAALALLTLLAGLVLLALDALLLAALLAALLDALLLAVLLLALLLLAALLLLAAPAS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  83 LPLPASGRDLLLAVDVSGSMDYRDMRWQDDEIsrLELIKKLfgdfiedRRGDRVGLILFGSQAYLQAPLTFDRhTVRVWL 162
Cdd:COG2425  112 AAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAA--LALLRAL-------RPNRRFGVILFDTEVVEDLPLTADD-GLEDAI 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490480609 163 DEAQIGIAGKNTAIGDAIGLAVKRLRQRPAESRVLVLITDGANTGGQiaPQIAAQLAA-EQQVKIYTIGIGADP 235
Cdd:COG2425  182 EFLSGLFAGGGTDIAPALRAALELLEEPDYRNADIVLITDGEAGVSP--EELLREVRAkESGVRLFTVAIGDAG 253
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 91-269 4.71e-17

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: 77.33  E-value: 4.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  91 DLLLAVDVSGSMDYRDMrwqddEISRlELIKKLFGDFIEDRRGDRVGLILFGSQAYLQAPLT--FDRHTVRVWLDEAQIg 168
Cdd:cd01450    2 DIVFLLDGSESVGPENF-----EKVK-DFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNdyKSKDDLLKAVKNLKY- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609 169 IAGKNTAIGDAIGLAVKRLRQ----RPAESRVLVLITDGANTGGQIAPQIAAQLAAEqQVKIYTIGIGadpqqggvpglf 244
Cdd:cd01450   75 LGGGGTNTGKALQYALEQLFSesnaRENVPKVIIVLTDGRSDDGGDPKEAAAKLKDE-GIKVFVVGVG------------ 141

                        170       180
                 ....*....|....*....|....*
gi 490480609 245 gfnpglDLDEPTLRGIAESTGGEYF 269
Cdd:cd01450  142 ------PADEEELREIASCPSERHV 160
VWA_2 pfam13519
von Willebrand factor type A domain;
92-200 2.59e-16

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 73.48  E-value: 2.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609   92 LLLAVDVSGSMdyrdmRWQDDEISRLELIKKLFGDFIEDRRGDRVGLILFGSQAYLQAPLTFDRHTVRVWLDEaqIGIAG 171
Cdd:pfam13519   1 LVFVLDTSGSM-----RNGDYGPTRLEAAKDAVLALLKSLPGDRVGLVTFGDGPEVLIPLTKDRAKILRALRR--LEPKG 73

                          90       100       110
                  ....*....|....*....|....*....|
gi 490480609  172 KNTAIGDAIGLAVKRLRQRPA-ESRVLVLI 200
Cdd:pfam13519  74 GGTNLAAALQLARAALKHRRKnQPRRIVLI 103
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 94-274 2.81e-13

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: 69.26  E-value: 2.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609   94 LAVDVSGSM-DYRDMrwqddeiSRLELIKklfgdFIED--RRGDRVGLILFGSQAYLQAPLTFDRHTVRVWLDEAQIGIA 170
Cdd:TIGR03436  58 LVIDTSGSMrNDLDR-------ARAAAIR-----FLKTvlRPNDRVFVVTFNTRLRLLQDFTSDPRLLEAALNRLKPPLR 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  171 GKN------------TAIGDAIGLAVKRLRQR----PAESRVLVLITDGANTGGQIAPQIAAQLAAEQQVKIYTIGI--- 231
Cdd:TIGR03436 126 TDYnssgafvrdgggTALYDAITLAALEQLANalagIPGRKALIVISDGGDNRSRDTLERAIDAAQRADVAIYSIDArgl 205

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 490480609  232 -GADPQQGGVPGLFGfnpgldldEPTLRGIAESTGGEYFRARSS 274
Cdd:TIGR03436 206 rAPDLGAGAKAGLGG--------PEALERLAEETGGRAFYVNSN 241
PRK13685 PRK13685
hypothetical protein; Provisional
 93-318 9.35e-13

hypothetical protein; Provisional


Pssm-ID: 184242 [Multi-domain]  Cd Length: 326  Bit Score: 68.19  E-value: 9.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  93 LLAVDVSGSMdyrdmRWQDDEISRLELIK---KLFGDfiEDRRGDRVGLILFGSQAYLQAPLTFDRHTVRVWLDEAQIGi 169
Cdd:PRK13685  92 MLVIDVSQSM-----RATDVEPNRLAAAQeaaKQFAD--ELTPGINLGLIAFAGTATVLVSPTTNREATKNAIDKLQLA- 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609 170 agKNTAIGDAIGLAVKRLR---------QRPAESRVlVLITDGANTGGQ--IAPQ---IAAQLAAEQQVKIYTIGIGA-- 233
Cdd:PRK13685 164 --DRTATGEAIFTALQAIAtvgavigggDTPPPARI-VLMSDGKETVPTnpDNPRgayTAARTAKDQGVPISTISFGTpy 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609 234 -----DPQQGGVPglfgfnpgldLDEPTLRGIAESTGGEYFRARSSAELESISATLDrlEPVAQQTTRA---RPALALYS 305
Cdd:PRK13685 241 gsveiNGQRQPVP----------VDDESLKKIAQLSGGEFYTAASLEELRAVYATLQ--QQIGYETIKGdasVGWLRLGA 308

                        250
                 ....*....|...
gi 490480609 306 WPLAAALGLSVLL 318
Cdd:PRK13685 309 LVLALAALAALLI 321
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 86-280 2.25e-12

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: 65.14  E-value: 2.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  86 PASGRDLLLAVDVSGSMDYRDmrwqDDEISRLELIKKLFGDFIEDRR-GDRVGLILFGSQAYLQA---------PLTFDR 155
Cdd:cd01456   17 PQLPPNVAIVLDNSGSMREVD----GGGETRLDNAKAALDETANALPdGTRLGLWTFSGDGDNPLdvrvlvpkgCLTAPV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609 156 HTV----RVWLDEA--QIGIAGKNTAIGDAIGLAVKRLRqrPAESRVLVLITDGANTGGQIAPQIAAQLAAEQQ----VK 225
Cdd:cd01456   93 NGFpsaqRSALDAAlnSLQTPTGWTPLAAALAEAAAYVD--PGRVNVVVLITDGEDTCGPDPCEVARELAKRRTpappIK 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490480609 226 IYTIGIGADPqqggvpglfgfnpgldlDEPTLRGIAESTGGEYfrARSSAELESI 280
Cdd:cd01456  171 VNVIDFGGDA-----------------DRAELEAIAEATGGTY--AYNQSDLASL 206
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
96-234 3.65e-12

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 64.56  E-value: 3.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  96 VDVSGSMdyrdmrwQDDEISRL-----ELIKKLFGDFIEDRRgDRVGLILFGSQAYLQAPLTFdrhtvrvwLDEAQIGI- 169
Cdd:COG4245   12 LDTSGSM-------SGEPIEALneglqALIDELRQDPYALET-VEVSVITFDGEAKVLLPLTD--------LEDFQPPDl 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490480609 170 -AGKNTAIGDAIGLAVKRLRQRPAESR---------VLVLITDGANTGGQIAPQIAAQLAAEQQVK--IYTIGIGAD 234
Cdd:COG4245   76 sASGGTPLGAALELLLDLIERRVQKYTaegkgdwrpVVFLITDGEPTDSDWEAALQRLKDGEAAKKanIFAIGVGPD 152
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 91-268 3.22e-08

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: 52.01  E-value: 3.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  91 DLLLAVDVSGSMDYRdmrwqddeisRLELIKKLFGDFIED-RRGDRVGLILFGSQAYLQAPLTF-DRHTVRVWLDEAQIG 168
Cdd:cd01466    2 DLVAVLDVSGSMAGD----------KLQLVKHALRFVISSlGDADRLSIVTFSTSAKRLSPLRRmTAKGKRSAKRVVDGL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609 169 IAGKNTAIGDAIGLAVKRLRQRPAESRV--LVLITDGANTGGQIAPQiaaqlAAEQQVKIYTIGIGAdpqqggvpglfgf 246
Cdd:cd01466   72 QAGGGTNVVGGLKKALKVLGDRRQKNPVasIMLLSDGQDNHGAVVLR-----ADNAPIPIHTFGLGA------------- 133

                        170       180
                 ....*....|....*....|..
gi 490480609 247 npglDLDEPTLRGIAESTGGEY 268
Cdd:cd01466  134 ----SHDPALLAFIAEITGGTF 151
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 87-231 4.61e-07

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: 49.43  E-value: 4.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  87 ASGRDLLLAVDVSGSMDyrdmrwqDDEISRLELIKKLFGDFIEDrrGDRVGLILFGSQAYLQAPLTFDRHTVRVWLDEAQ 166
Cdd:cd01474    2 AGHFDLYFVLDKSGSVA-------ANWIEIYDFVEQLVDRFNSP--GLRFSFITFSTRATKILPLTDDSSAIIKGLEVLK 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609 167 IGIAGKNTAIGDAIGLAVKRLRQRPA----ESRVLVLITDGANTG-GQIAPQIAAQLAAEQQVKIYTIGI 231
Cdd:cd01474   73 KVTPSGQTYIHEGLENANEQIFNRNGggreTVSVIIALTDGQLLLnGHKYPEHEAKLSRKLGAIVYCVGV 142
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 92-280 2.53e-06

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: 46.88  E-value: 2.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  92 LLLAVDVSGSMDYRdmrwqddeisRLELIKKLFGDFIED-RRGDRVGLILFGSQAYLQAPLTF--DRHTVRVWLDEAQig 168
Cdd:cd01465    3 LVFVIDRSGSMDGP----------KLPLVKSALKLLVDQlRPDDRLAIVTYDGAAETVLPATPvrDKAAILAAIDRLT-- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609 169 iAGKNTAIGDAIGLAVKRLRQRPAESRV--LVLITDG-ANTGGQIAPQIAAQLAAEQQVKIYTIGigadpqqggvpglFG 245
Cdd:cd01465   71 -AGGSTAGGAGIQLGYQEAQKHFVPGGVnrILLATDGdFNVGETDPDELARLVAQKRESGITLST-------------LG 136

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 490480609 246 FnpGLDLDEPTLRGIAESTGGEYFRARSSAELESI 280
Cdd:cd01465  137 F--GDNYNEDLMEAIADAGNGNTAYIDNLAEARKV 169
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 92-204 1.57e-05

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: 44.62  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  92 LLLAVDVSGSMDyrdmrwqddEISRLELIKK---LFGDFIEdRRGDRVGLILFGSQAY------LQAPLTFDRHtvRVWL 162
Cdd:cd01454    3 VTLLLDLSGSMR---------SDRRIDVAKKaavLLAEALE-ACGVPHAILGFTTDAGgrervrWIKIKDFDES--LHER 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490480609 163 DEAQIGI--AGKNTAIGDAIGLAVKRLRQRPAESRVLVLITDGA 204
Cdd:cd01454   71 ARKRLAAlsPGGNTRDGAAIRHAAERLLARPEKRKILLVISDGE 114
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 90-237 8.99e-05

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: 42.22  E-value: 8.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  90 RDLLLAVDVSGSMDYRDMRWQddeisrLELIKKLFGDFIEDRRGDRVGLILFGSQAYLQAPLtfDRHTVRVWLDEA--QI 167
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLV------KDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYL--NTYRSKDDVLEAvkNL 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490480609 168 GIAGKNTAIGDAIGLAVKRLRQRPAESR-----VLVLITDGANTGGQIAPqiaAQLAAEQQVKIYTIGIG-ADPQQ 237
Cdd:cd01472   73 RYIGGGTNTGKALKYVRENLFTEASGSRegvpkVLVVITDGKSQDDVEEP---AVELKQAGIEVFAVGVKnADEEE 145
NorD COG4548
Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];
89-203 3.90e-04

Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];


Pssm-ID: 443612 [Multi-domain]  Cd Length: 439  Bit Score: 42.01  E-value: 3.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  89 GRDL--LLAVDVSGSMDyrdmRWQDDEISRLELIKK---LFGDFIeDRRGDRVGLILFGSQAylqapltfdRHTVRV--- 160
Cdd:COG4548  246 ERDLavLLLLDLSLSTD----AWVGSGRRVLDVEREallLLAEAL-EALGDPFAIYGFSSDG---------RHRVRYyri 311

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490480609 161 ------WLDEAQIGIA----GKNTAIGDAIGLAVKRLRQRPAESRVLVLITDG 203
Cdd:COG4548  312 kdfdepYDDAVRARIAglepGYYTRMGAAIRHATALLAAQPARRRLLLVLTDG 364
YeaD2 COG1721
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];
90-202 5.97e-04

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


Pssm-ID: 441327 [Multi-domain]  Cd Length: 287  Bit Score: 40.96  E-value: 5.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  90 RDLLLAVDVSGSMDYRDmrwqdDEISRLELIKKLFGDFIED--RRGDRVGLILFGSQAYLQAPLTFDRHTVRVWLDEaqi 167
Cdd:COG1721  148 LTVVLLLDTSASMRFGS-----GGPSKLDLAVEAAASLAYLalRQGDRVGLLTFGDRVRRYLPPRRGRRHLLRLLEA--- 219

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490480609 168 gIAGKNTAIGDAIGLAVKRLRQRPAESRVLVLITD 202
Cdd:COG1721  220 -LARLEPAGETDLAAALRRLARRLPRRSLVVLISD 253
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 90-235 9.15e-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: 39.51  E-value: 9.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  90 RDLLLAVDVSGSMDYRDMRwQDDEiSRLELIKKLfgdfiedRRGDRVGLILFGSqaylqapltfdrhTVRVW------LD 163
Cdd:cd01461    3 KEVVFVIDTSGSMSGTKIE-QTKE-ALLTALKDL-------PPGDYFNIIGFSD-------------TVEEFspssvsAT 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609 164 EAQIGIA---------GKNTAIGDAIGLAVKRLRQRPAESRVLVLITDGANTG-GQIapQIAAQLAAEQQVKIYTIGIGA 233
Cdd:cd01461   61 AENVAAAieyvnrlqaLGGTNMNDALEAALELLNSSPGSVPQIILLTDGEVTNeSQI--LKNVREALSGRIRLFTFGIGS 138


                 ..
gi 490480609 234 DP 235
Cdd:cd01461  139 DV 140
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 91-203 1.04e-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: 39.30  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  91 DLLLAVDVSGSMD--YRDMRwqddeisrlELIKKLFGDFIEDRRGDRVGLILFGSQAYLQAPLTFDRHTVRVWLDEA--Q 166
Cdd:cd01476    2 DLLFVLDSSGSVRgkFEKYK---------KYIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLPKHNDGEELLEKvdN 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490480609 167 IGIAGKNTAIGDAIGLAVKRLR----QRPAESRVLVLITDG 203
Cdd:cd01476   73 LRFIGGTTATGAAIEVALQQLDpsegRREGIPKVVVVLTDG 113
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 92-270 1.96e-03

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: 38.80  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  92 LLLAVDVSGSMDYRdmrwqddeiSRLELIKKLFGDFIED--RRGDRVGLILF-GSQAYLQAPLTFDRHTVRVWLDEAQIG 168
Cdd:cd01451    3 VIFVVDASGSMAAR---------HRMAAAKGAVLSLLRDayQRRDKVALIAFrGTEAEVLLPPTRSVELAKRRLARLPTG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609 169 ----IAGKNTAIGDAIGLAVKRLRQRPaesrVLVLITDGANTGGQIAPQIAAQLAAEqqvKIYTIGIGA---DPQQGGVp 241
Cdd:cd01451   74 ggtpLAAGLLAAYELAAEQARDPGQRP----LIVVITDGRANVGPDPTADRALAAAR---KLRARGISAlviDTEGRPV- 145

                        170       180
                 ....*....|....*....|....*....
gi 490480609 242 glfgfnpgldlDEPTLRGIAESTGGEYFR 270
Cdd:cd01451  146 -----------RRGLAKDLARALGGQYVR 163
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 91-244 3.25e-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: 37.71  E-value: 3.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490480609  91 DLLLAVDVSGSMDYRDMRWqddeisrlelIKKLFGDFIED--RRGDRVGLILFGSQAYLQ-APLTFDrhtVRVWLDEAQI 167
Cdd:cd01462    2 PVILLVDQSGSMYGAPEEV----------AKAVALALLRIalAENRDTYLILFDSEFQTKiVDKTDD---LEEPVEFLSG 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490480609 168 GIAGKNTAIGDAIGLAVKRLRQRPAESRVLVLITDGANTGGQIAPQIAAQLAAEQQVKIYTIGIGADpqqgGVPGLF 244
Cdd:cd01462   69 VQLGGGTDINKALRYALELIERRDPRKADIVLITDGYEGGVSDELLREVELKRSRVARFVALALGDH----GNPGYD 141
 
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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