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Conserved domains on  [gi|553762694|ref|WP_023095089|]
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MULTISPECIES: VWA domain-containing protein [Pseudomonas]

Protein Classification

vWA domain-containing protein( domain architecture ID 10008387)

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:  12579041|10830113|12388743
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
11-204 2.07e-62

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


:

Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 192.83  E-value: 2.07e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  11 TARPLPIIVLADTSGSMSVDgKIEALNKSLKDMISSFAGESRLRAELQVSLITFGSQAEVNLPLTPAHQLQgFTPLTAAG 90
Cdd:COG4245    2 PMRRLPVYLLLDTSGSMSGE-PIEALNEGLQALIDELRQDPYALETVEVSVITFDGEAKVLLPLTDLEDFQ-PPDLSASG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  91 ATPLGGALALASQMIEDK----DSIPSRAYKPVIVLVSDGHPTD-DWQGSFARLANGERSSKATRFAMAIGADADESMLG 165
Cdd:COG4245   80 GTPLGAALELLLDLIERRvqkyTAEGKGDWRPVVFLITDGEPTDsDWEAALQRLKDGEAAKKANIFAIGVGPDADTEVLK 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 553762694 166 DFANDpeAPLFRAENAADIHRFFRAVTMSVSARSRSATP 204
Cdd:COG4245  160 QLTDP--VRALDALDGLDFREFFKWLSASVSSVSRSVGP 196
 
Name Accession Description Interval E-value
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
11-204 2.07e-62

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 192.83  E-value: 2.07e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  11 TARPLPIIVLADTSGSMSVDgKIEALNKSLKDMISSFAGESRLRAELQVSLITFGSQAEVNLPLTPAHQLQgFTPLTAAG 90
Cdd:COG4245    2 PMRRLPVYLLLDTSGSMSGE-PIEALNEGLQALIDELRQDPYALETVEVSVITFDGEAKVLLPLTDLEDFQ-PPDLSASG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  91 ATPLGGALALASQMIEDK----DSIPSRAYKPVIVLVSDGHPTD-DWQGSFARLANGERSSKATRFAMAIGADADESMLG 165
Cdd:COG4245   80 GTPLGAALELLLDLIERRvqkyTAEGKGDWRPVVFLITDGEPTDsDWEAALQRLKDGEAAKKANIFAIGVGPDADTEVLK 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 553762694 166 DFANDpeAPLFRAENAADIHRFFRAVTMSVSARSRSATP 204
Cdd:COG4245  160 QLTDP--VRALDALDGLDFREFFKWLSASVSSVSRSVGP 196
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 13-178 4.76e-31

VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 112.05  E-value: 4.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  13 RPLPIIVLADTSGSMSVDgKIEALNKSLKDMISSFAGESRLRAELQVSLITFGSQAEVNLPLTPAHQLQgFTPLTAAGAT 92
Cdd:cd01464    2 RRLPIYLLLDTSGSMAGE-PIEALNQGLQMLQSELRQDPYALESVEISVITFDSAARVIVPLTPLESFQ-PPRLTASGGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  93 PLGGALALASQMIEDKDSIPSRA----YKPVIVLVSDGHPTDDWQGSFARLaNGERSSKATRFAMAIGADADESMLGDFA 168
Cdd:cd01464   80 SMGAALELALDCIDRRVQRYRADqkgdWRPWVFLLTDGEPTDDLTAAIERI-KEARDSKGRIVACAVGPKADLDTLKQIT 158

                        170
                 ....*....|
gi 553762694 169 NDPEAPLFRA 178
Cdd:cd01464  159 EGVPLLDDAL 168
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 17-171 5.31e-19

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: 80.58  E-value: 5.31e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694    17 IIVLADTSGSMSvDGKIEALNKSLKDMISSFAGESRLRaelQVSLITFGSQAEVNLPLTPAHQLQGF------TPLTAAG 90
Cdd:smart00327   2 VVFLLDGSGSMG-GNRFELAKEFVLKLVEQLDIGPDGD---RVGLVTFSDDARVLFPLNDSRSKDALlealasLSYKLGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694    91 ATPLGGALALASQMIEDKDSIPSRAYKPVIVLVSDGHPTDDWqGSFARLANGERSSKATRFAMAIGADADESMLGDFAND 170
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGP-KDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASA 156


                   .
gi 553762694   171 P 171
Cdd:smart00327 157 P 157
VWA pfam00092
von Willebrand factor type A domain;
17-190 5.67e-13

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 64.60  E-value: 5.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694   17 IIVLADTSGSMSvDGKIEALNKSLKDMISSFaGESRLRAelQVSLITFGSQAEVNLPLTPAH-------QLQGFTPLTAa 89
Cdd:pfam00092   2 IVFLLDGSGSIG-GDNFEKVKEFLKKLVESL-DIGPDGT--RVGLVQYSSDVRTEFPLNDYSskeellsAVDNLRYLGG- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694   90 GATPLGGALALASQMIEDKDSIPSRAYKPVIVLVSDGHPTDdwqGSFARLANGERSSKATRFAMAIGaDADESMLGDFAN 169
Cdd:pfam00092  77 GTTNTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQD---GDPEEVARELKSAGVTVFAVGVG-NADDEELRKIAS 152

                         170       180
                  ....*....|....*....|..
gi 553762694  170 DP-EAPLFRAENAADIHRFFRA 190
Cdd:pfam00092 153 EPgEGHVFTVSDFEALEDLQDQ 174
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 3-126 9.73e-06

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: 45.38  E-value: 9.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694    3 ELKKFQVQTARPLPIIVLADTSGSMSVDGKIEalnkslKDMISSFAGESrLRAELQVSLITFGSQAEVNLPLT-PAHQLQ 81
Cdd:TIGR03436  42 TIASFRRETDLPLTVGLVIDTSGSMRNDLDRA------RAAAIRFLKTV-LRPNDRVFVVTFNTRLRLLQDFTsDPRLLE 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553762694   82 ----------------GFTPLTAAGATPLGGALALAS--QMIEDKDSIPSRAykpVIVLVSDG 126
Cdd:TIGR03436 115 aalnrlkpplrtdynsSGAFVRDGGGTALYDAITLAAleQLANALAGIPGRK---ALIVISDG 174
bchD PRK13406
magnesium chelatase subunit D; Provisional
 58-192 3.90e-03

magnesium chelatase subunit D; Provisional


Pssm-ID: 237378 [Multi-domain]  Cd Length: 584  Bit Score: 37.70  E-value: 3.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  58 QVSLITF-GSQAEVNLPLTPA-----HQLQGftpLTAAGATPLGGALALASQMiedKDSIPSRAYKPVIVLVSDGHPTDD 131
Cdd:PRK13406 439 QVALVAFrGRGAELLLPPTRSlvrakRSLAG---LPGGGGTPLAAGLDAAAAL---ALQVRRKGMTPTVVLLTDGRANIA 512

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553762694 132 WQGSFARLANGERSSKATRfamAIGADADESMLGDFANDPEAP---LFRAENA-------ADIHRFFRAVT 192
Cdd:PRK13406 513 RDGTAGRAQAEEDALAAAR---ALRAAGLPALVIDTSPRPQPQaraLAEAMGArylplprADAGRLSQAVR 580
 
Name Accession Description Interval E-value
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
11-204 2.07e-62

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 192.83  E-value: 2.07e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  11 TARPLPIIVLADTSGSMSVDgKIEALNKSLKDMISSFAGESRLRAELQVSLITFGSQAEVNLPLTPAHQLQgFTPLTAAG 90
Cdd:COG4245    2 PMRRLPVYLLLDTSGSMSGE-PIEALNEGLQALIDELRQDPYALETVEVSVITFDGEAKVLLPLTDLEDFQ-PPDLSASG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  91 ATPLGGALALASQMIEDK----DSIPSRAYKPVIVLVSDGHPTD-DWQGSFARLANGERSSKATRFAMAIGADADESMLG 165
Cdd:COG4245   80 GTPLGAALELLLDLIERRvqkyTAEGKGDWRPVVFLITDGEPTDsDWEAALQRLKDGEAAKKANIFAIGVGPDADTEVLK 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 553762694 166 DFANDpeAPLFRAENAADIHRFFRAVTMSVSARSRSATP 204
Cdd:COG4245  160 QLTDP--VRALDALDGLDFREFFKWLSASVSSVSRSVGP 196
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 13-178 4.76e-31

VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 112.05  E-value: 4.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  13 RPLPIIVLADTSGSMSVDgKIEALNKSLKDMISSFAGESRLRAELQVSLITFGSQAEVNLPLTPAHQLQgFTPLTAAGAT 92
Cdd:cd01464    2 RRLPIYLLLDTSGSMAGE-PIEALNQGLQMLQSELRQDPYALESVEISVITFDSAARVIVPLTPLESFQ-PPRLTASGGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  93 PLGGALALASQMIEDKDSIPSRA----YKPVIVLVSDGHPTDDWQGSFARLaNGERSSKATRFAMAIGADADESMLGDFA 168
Cdd:cd01464   80 SMGAALELALDCIDRRVQRYRADqkgdWRPWVFLLTDGEPTDDLTAAIERI-KEARDSKGRIVACAVGPKADLDTLKQIT 158

                        170
                 ....*....|
gi 553762694 169 NDPEAPLFRA 178
Cdd:cd01464  159 EGVPLLDDAL 168
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 12-191 3.08e-22

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: 91.15  E-value: 3.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  12 ARPLPIIVLADTSGSMSVDGKIEAlnksLKDMISSFAGESRLRAelQVSLITFGSQAEVNLPLTPAHQL--QGFTPLTAA 89
Cdd:COG1240   90 QRGRDVVLVVDASGSMAAENRLEA----AKGALLDFLDDYRPRD--RVGLVAFGGEAEVLLPLTRDREAlkRALDELPPG 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  90 GATPLGGALALASQMIEDKDSipsrAYKPVIVLVSDGHPTDDwQGSFARLANGERSSKATRFAMAIGADA-DESMLGDFA 168
Cdd:COG1240  164 GGTPLGDALALALELLKRADP----ARRKVIVLLTDGRDNAG-RIDPLEAAELAAAAGIRIYTIGVGTEAvDEGLLREIA 238

                        170       180
                 ....*....|....*....|...
gi 553762694 169 NDPEAPLFRAENAADIHRFFRAV 191
Cdd:COG1240  239 EATGGRYFRADDLSELAAIYREI 261
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 17-176 7.91e-20

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: 82.61  E-value: 7.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  17 IIVLADTSGSMSvDGKIEALNKSLKDMISSFageSRLRAELQVSLITFGSQAEVNLPLTPAHQLQ------GFTPLTAAG 90
Cdd:cd00198    3 IVFLLDVSGSMG-GEKLDKAKEALKALVSSL---SASPPGDRVGLVTFGSNARVVLPLTTDTDKAdlleaiDALKKGLGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  91 ATPLGGALALASQMIedkDSIPSRAYKPVIVLVSDGHPTDDwQGSFARLANGERSSKATRFAMAIGADADESMLGDFAND 170
Cdd:cd00198   79 GTNIGAALRLALELL---KSAKRPNARRVIILLTDGEPNDG-PELLAEAARELRKLGITVYTIGIGDDANEDELKEIADK 154


                 ....*.
gi 553762694 171 PEAPLF 176
Cdd:cd00198  155 TTGGAV 160
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 17-171 5.31e-19

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: 80.58  E-value: 5.31e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694    17 IIVLADTSGSMSvDGKIEALNKSLKDMISSFAGESRLRaelQVSLITFGSQAEVNLPLTPAHQLQGF------TPLTAAG 90
Cdd:smart00327   2 VVFLLDGSGSMG-GNRFELAKEFVLKLVEQLDIGPDGD---RVGLVTFSDDARVLFPLNDSRSKDALlealasLSYKLGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694    91 ATPLGGALALASQMIEDKDSIPSRAYKPVIVLVSDGHPTDDWqGSFARLANGERSSKATRFAMAIGADADESMLGDFAND 170
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGP-KDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASA 156


                   .
gi 553762694   171 P 171
Cdd:smart00327 157 P 157
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 5-189 7.11e-18

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 79.76  E-value: 7.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694   5 KKFQVQTARPLPIIVLADTSGSMSVDgKIEALNKSLKDMISsfagesRLRAELQVSLITFGSQAEVNLPLTPAHQLQG-- 82
Cdd:COG2304   82 PKAAAEERPPLNLVFVIDVSGSMSGD-KLELAKEAAKLLVD------QLRPGDRVSIVTFAGDARVLLPPTPATDRAKil 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  83 --FTPLTAAGATPLGGALALASQMIEDKdsiPSRAYKPVIVLVSDGHPTDDWQ--GSFARLANGERSSKATRFAMAIGAD 158
Cdd:COG2304  155 aaIDRLQAGGGTALGAGLELAYELARKH---FIPGRVNRVILLTDGDANVGITdpEELLKLAEEAREEGITLTTLGVGSD 231

                        170       180       190
                 ....*....|....*....|....*....|.
gi 553762694 159 ADESMLGDFANDPEAPLFRAENAADIHRFFR 189
Cdd:COG2304  232 YNEDLLERLADAGGGNYYYIDDPEEAEKVFV 262
VWA pfam00092
von Willebrand factor type A domain;
17-190 5.67e-13

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 64.60  E-value: 5.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694   17 IIVLADTSGSMSvDGKIEALNKSLKDMISSFaGESRLRAelQVSLITFGSQAEVNLPLTPAH-------QLQGFTPLTAa 89
Cdd:pfam00092   2 IVFLLDGSGSIG-GDNFEKVKEFLKKLVESL-DIGPDGT--RVGLVQYSSDVRTEFPLNDYSskeellsAVDNLRYLGG- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694   90 GATPLGGALALASQMIEDKDSIPSRAYKPVIVLVSDGHPTDdwqGSFARLANGERSSKATRFAMAIGaDADESMLGDFAN 169
Cdd:pfam00092  77 GTTNTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQD---GDPEEVARELKSAGVTVFAVGVG-NADDEELRKIAS 152

                         170       180
                  ....*....|....*....|..
gi 553762694  170 DP-EAPLFRAENAADIHRFFRA 190
Cdd:pfam00092 153 EPgEGHVFTVSDFEALEDLQDQ 174
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 20-188 8.47e-12

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: 61.13  E-value: 8.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  20 LADTSGSMSvDGKIEALNKSLKDMISsfagesRLRAELQVSLITFGSQAEVNLPLTPAHQLQGF----TPLTAAGATPLG 95
Cdd:cd01465    6 VIDRSGSMD-GPKLPLVKSALKLLVD------QLRPDDRLAIVTYDGAAETVLPATPVRDKAAIlaaiDRLTAGGSTAGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  96 GALALASQMIeDKDSIPSRAYKpvIVLVSDGHPT---DDWQgSFARLANGERSSKATRFAMAIGADADESMLGDFANDPE 172
Cdd:cd01465   79 AGIQLGYQEA-QKHFVPGGVNR--ILLATDGDFNvgeTDPD-ELARLVAQKRESGITLSTLGFGDNYNEDLMEAIADAGN 154

                        170
                 ....*....|....*.
gi 553762694 173 APLFRAENAADIHRFF 188
Cdd:cd01465  155 GNTAYIDNLAEARKVF 170
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 3-168 8.18e-11

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 60.08  E-value: 8.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694   3 ELKKFQVQTARPLPIIVLADTSGSMSvDGKIEAlnksLKDMISSFAgeSRLRAELQVSLITFGSQAEVNLPLTPAHQLQG 82
Cdd:COG2425  107 AAPASAAVPLLEGPVVLCVDTSGSMA-GSKEAA----AKAAALALL--RALRPNRRFGVILFDTEVVEDLPLTADDGLED 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  83 F----TPLTAAGATPLGGALALASQMIEDkdsipSRAYKPVIVLVSDGHPTDDWQGSFARLAngERSSKATRFAMAIGAD 158
Cdd:COG2425  180 AieflSGLFAGGGTDIAPALRAALELLEE-----PDYRNADIVLITDGEAGVSPEELLREVR--AKESGVRLFTVAIGDA 252

                        170
                 ....*....|
gi 553762694 159 ADESMLGDFA 168
Cdd:COG2425  253 GNPGLLEALA 262
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 16-140 3.12e-09

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: 54.20  E-value: 3.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  16 PIIVLADTSGSMSVDGKIEAlnksLKDMISSFAGESRLRAElQVSLITF-GSQAEVNLPLT-----PAHQLQGftpLTAA 89
Cdd:cd01451    2 LVIFVVDASGSMAARHRMAA----AKGAVLSLLRDAYQRRD-KVALIAFrGTEAEVLLPPTrsvelAKRRLAR---LPTG 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 553762694  90 GATPLGGALALASQMIedKDSIPSRAYKPVIVLVSDGH---PTDDWQGSFARLA 140
Cdd:cd01451   74 GGTPLAAGLLAAYELA--AEQARDPGQRPLIVVITDGRanvGPDPTADRALAAA 125
VWA_2 pfam13519
von Willebrand factor type A domain;
17-123 8.91e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 51.52  E-value: 8.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694   17 IIVLADTSGSMSVDG----KIEALNKSLKDMISSFAGEsrlraelQVSLITFGSQAEVNLPLT--PAHQLQGFTPLTA-A 89
Cdd:pfam13519   1 LVFVLDTSGSMRNGDygptRLEAAKDAVLALLKSLPGD-------RVGLVTFGDGPEVLIPLTkdRAKILRALRRLEPkG 73

                          90       100       110
                  ....*....|....*....|....*....|....
gi 553762694   90 GATPLGGALALASQMIEDKdsipSRAYKPVIVLV 123
Cdd:pfam13519  74 GGTNLAAALQLARAALKHR----RKNQPRRIVLI 103
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 17-172 1.30e-08

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: 52.29  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  17 IIVLADTSGSMSVDGKIEALNkSLKDMISSFA-GESRLRaelqVSLITFGSQAEVNLPLT-------PAHQLQGFTPLTA 88
Cdd:cd01450    3 IVFLLDGSESVGPENFEKVKD-FIEKLVEKLDiGPDKTR----VGLVQYSDDVRVEFSLNdykskddLLKAVKNLKYLGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  89 AGaTPLGGALALASQMIEDKDSIPSRAYKpVIVLVSDGHPTDDwqGSFARLANGERSSKATRFAMAIGaDADESMLGDFA 168
Cdd:cd01450   78 GG-TNTGKALQYALEQLFSESNARENVPK-VIIVLTDGRSDDG--GDPKEAAAKLKDEGIKVFVVGVG-PADEEELREIA 152


                 ....
gi 553762694 169 NDPE 172
Cdd:cd01450  153 SCPS 156
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 3-126 9.73e-06

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: 45.38  E-value: 9.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694    3 ELKKFQVQTARPLPIIVLADTSGSMSVDGKIEalnkslKDMISSFAGESrLRAELQVSLITFGSQAEVNLPLT-PAHQLQ 81
Cdd:TIGR03436  42 TIASFRRETDLPLTVGLVIDTSGSMRNDLDRA------RAAAIRFLKTV-LRPNDRVFVVTFNTRLRLLQDFTsDPRLLE 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553762694   82 ----------------GFTPLTAAGATPLGGALALAS--QMIEDKDSIPSRAykpVIVLVSDG 126
Cdd:TIGR03436 115 aalnrlkpplrtdynsSGAFVRDGGGTALYDAITLAAleQLANALAGIPGRK---ALIVISDG 174
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 17-130 1.52e-05

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: 43.53  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  17 IIVLADTSGSMSVDgKIEALNKSLKDMISSFAGESRLraelqvSLITFGSQAEVNLPLTP-----AHQLQGFTP-LTAAG 90
Cdd:cd01466    3 LVAVLDVSGSMAGD-KLQLVKHALRFVISSLGDADRL------SIVTFSTSAKRLSPLRRmtakgKRSAKRVVDgLQAGG 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 553762694  91 ATPLGGALALASQMIEDkdsipSRAYKPV--IVLVSDGHPTD 130
Cdd:cd01466   76 GTNVVGGLKKALKVLGD-----RRQKNPVasIMLLSDGQDNH 112
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 18-190 1.79e-04

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: 40.78  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  18 IVLA-DTSGSMSV--DGKIEALNKSlKDMISSFAGEsrlRAELQVSLITFGSQAEVNLPLTPAH-----QLQGFTPLTAA 89
Cdd:cd01467    5 IMIAlDVSGSMLAqdFVKPSRLEAA-KEVLSDFIDR---RENDRIGLVVFAGAAFTQAPLTLDReslkeLLEDIKIGLAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  90 GATPLGGALALASQMIEdkdsiPSRAYKPVIVLVSDGHPTDDW--QGSFARLANGErssKATRFAMAIGADAD-ESMLGD 166
Cdd:cd01467   81 QGTAIGDAIGLAIKRLK-----NSEAKERVIVLLTDGENNAGEidPATAAELAKNK---GVRIYTIGVGKSGSgPKPDGS 152

                        170       180
                 ....*....|....*....|....
gi 553762694 167 FANDPEAPLFRAENAADihRFFRA 190
Cdd:cd01467  153 TILDEDSLVEIADKTGG--RIFRA 174
YeaD2 COG1721
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];
5-148 2.46e-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: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694   5 KKFQVQTARPlpIIVLADTSGSMsvDGKIEALNKSlkDMISSFA---GESRLRAELQVSLITFGSQAEVNL-PLTPAHQL 80
Cdd:COG1721  140 REFEEERELT--VVLLLDTSASM--RFGSGGPSKL--DLAVEAAaslAYLALRQGDRVGLLTFGDRVRRYLpPRRGRRHL 213

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553762694  81 QGF----TPLTAAGATPLGGALALASQMiedkdsIPSRAykpVIVLVSDGHPTDDWQGSFARLANGERSSKA 148
Cdd:COG1721  214 LRLlealARLEPAGETDLAAALRRLARR------LPRRS---LVVLISDFLDPEELGIDVVDVRTDEPLVAA 276
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 17-164 5.80e-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: 39.12  E-value: 5.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  17 IIVLADTSGSMS---VDGKIEALNKSLKDmissfagesrLRAELQVSLITFGSQAE----VNLPLTPA---------HQL 80
Cdd:cd01461    5 VVFVIDTSGSMSgtkIEQTKEALLTALKD----------LPPGDYFNIIGFSDTVEefspSSVSATAEnvaaaieyvNRL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  81 QgftpltAAGATPLGGALALAsqmIEDKDSIPSRAykPVIVLVSDGHPTDdwQGSFARLANGERSSKATRFAMAIGADAD 160
Cdd:cd01461   75 Q------ALGGTNMNDALEAA---LELLNSSPGSV--PQIILLTDGEVTN--ESQILKNVREALSGRIRLFTFGIGSDVN 141


                 ....
gi 553762694 161 ESML 164
Cdd:cd01461  142 TYLL 145
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 56-172 6.44e-04

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: 39.42  E-value: 6.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  56 ELQVSLITFGSQAEVNLPLTP--------AHQLQGFTPltaAGATPLGGALALASQMIEdKDSIPSRAYKPVIVLVSDGH 127
Cdd:cd01474   39 GLRFSFITFSTRATKILPLTDdssaiikgLEVLKKVTP---SGQTYIHEGLENANEQIF-NRNGGGRETVSVIIALTDGQ 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 553762694 128 PTDDWQGSFARLANGERSSKATRFAMAIgADADESMLGDFANDPE 172
Cdd:cd01474  115 LLLNGHKYPEHEAKLSRKLGAIVYCVGV-TDFLKSQLINIADSKE 158
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 19-184 1.07e-03

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: 38.46  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  19 VLADTSGSMSVDGKIEALN----------KSLKDM--ISSFAGESRLRAelQVSLITFGSQAEVNLPlTPAHQLQGFTPl 86
Cdd:cd01454    5 LLLDLSGSMRSDRRIDVAKkaavllaealEACGVPhaILGFTTDAGGRE--RVRWIKIKDFDESLHE-RARKRLAALSP- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  87 taAGATPLGGALALASQMIEdkdsipSRAYKPVIVLV-SDGHPTD--DWQGSFARLANGERSSKATR------FAMAIGA 157
Cdd:cd01454   81 --GGNTRDGAAIRHAAERLL------ARPEKRKILLViSDGEPNDldYYEGNVFATEDALRAVIEARklgievFGITIDR 152

                        170       180
                 ....*....|....*....|....*..
gi 553762694 158 DADESMLGDFANdpeapLFRAENAADI 184
Cdd:cd01454  153 DATTVDKEYLKN-----IFGEEGYALI 174
bchD PRK13406
magnesium chelatase subunit D; Provisional
 58-192 3.90e-03

magnesium chelatase subunit D; Provisional


Pssm-ID: 237378 [Multi-domain]  Cd Length: 584  Bit Score: 37.70  E-value: 3.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  58 QVSLITF-GSQAEVNLPLTPA-----HQLQGftpLTAAGATPLGGALALASQMiedKDSIPSRAYKPVIVLVSDGHPTDD 131
Cdd:PRK13406 439 QVALVAFrGRGAELLLPPTRSlvrakRSLAG---LPGGGGTPLAAGLDAAAAL---ALQVRRKGMTPTVVLLTDGRANIA 512

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553762694 132 WQGSFARLANGERSSKATRfamAIGADADESMLGDFANDPEAP---LFRAENA-------ADIHRFFRAVT 192
Cdd:PRK13406 513 RDGTAGRAQAEEDALAAAR---ALRAAGLPALVIDTSPRPQPQaraLAEAMGArylplprADAGRLSQAVR 580
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 17-171 6.02e-03

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: 36.05  E-value: 6.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  17 IIVLADTSGSMSVDGKiealnKSLKDMISSFAGESRLRAEL-QVSLITFGSQAEVNLPLTpahQLQGFTPLTAA------ 89
Cdd:cd01472    3 IVFLVDGSESIGLSNF-----NLVKDFVKRVVERLDIGPDGvRVGVVQYSDDPRTEFYLN---TYRSKDDVLEAvknlry 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  90 --GATPLGGALALASQMIEDKDSIPSRAYKPVIVLVSDGHPTDDwqgsFARLANGERSSKATRFAMAIgADADESMLGDF 167
Cdd:cd01472   75 igGGTNTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDD----VEEPAVELKQAGIEVFAVGV-KNADEEELKQI 149


                 ....
gi 553762694 168 ANDP 171
Cdd:cd01472  150 ASDP 153
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 16-126 8.42e-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: 35.79  E-value: 8.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553762694  16 PIIVLADTSGSMSvdGKIEALNKSLkdMISSFagESRLRAELQVSLITFGSQ---AEVNLPLTPAHQLQGFTPLTAAGAT 92
Cdd:cd01462    2 PVILLVDQSGSMY--GAPEEVAKAV--ALALL--RIALAENRDTYLILFDSEfqtKIVDKTDDLEEPVEFLSGVQLGGGT 75

                         90       100       110
                 ....*....|....*....|....*....|....
gi 553762694  93 PLGGALALASQMIEDKDsiPSRAykpVIVLVSDG 126
Cdd:cd01462   76 DINKALRYALELIERRD--PRKA---DIVLITDG 104
 
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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