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Conserved domains on  [gi|13878870|sp|P76396|]
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RecName: Full=Uncharacterized protein YegL

Protein Classification

vWA domain-containing protein( domain architecture ID 10106962)

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:  10830113|12388743|12579041
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 17-189 7.25e-88

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: 256.88  E-value: 7.25e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  17 EPRCPCILLLDVSGSMNGRPINELNAGLVTFRDELLADPLALKRVELGIVTF-GPVHVEQPFTSAANFFPPILFAQGDTP 95
Cdd:cd01464   1 MRRLPIYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPYALESVEISVITFdSAARVIVPLTPLESFQPPRLTASGGTS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  96 MGAAITKALDMVEERKREYRANGISYYRPWIFLITDGAPTDEWQAAAnKVFRGEED--KRFAFFSIGVqGADMKTLAQIS 173
Cdd:cd01464  81 MGAALELALDCIDRRVQRYRADQKGDWRPWVFLLTDGEPTDDLTAAI-ERIKEARDskGRIVACAVGP-KADLDTLKQIT 158

                       170
                ....*....|....*.
gi 13878870 174 VRQPLPLQGLQFRELF 189
Cdd:cd01464 159 EGVPLLDDALSGLNFF 174
 
Name Accession Description Interval E-value
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 17-189 7.25e-88

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: 256.88  E-value: 7.25e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  17 EPRCPCILLLDVSGSMNGRPINELNAGLVTFRDELLADPLALKRVELGIVTF-GPVHVEQPFTSAANFFPPILFAQGDTP 95
Cdd:cd01464   1 MRRLPIYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPYALESVEISVITFdSAARVIVPLTPLESFQPPRLTASGGTS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  96 MGAAITKALDMVEERKREYRANGISYYRPWIFLITDGAPTDEWQAAAnKVFRGEED--KRFAFFSIGVqGADMKTLAQIS 173
Cdd:cd01464  81 MGAALELALDCIDRRVQRYRADQKGDWRPWVFLLTDGEPTDDLTAAI-ERIKEARDskGRIVACAVGP-KADLDTLKQIT 158

                       170
                ....*....|....*.
gi 13878870 174 VRQPLPLQGLQFRELF 189
Cdd:cd01464 159 EGVPLLDDALSGLNFF 174
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
15-189 1.65e-81

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 241.37  E-value: 1.65e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  15 NPEPRCPCILLLDVSGSMNGRPINELNAGLVTFRDELLADPLALKRVELGIVTF-GPVHVEQPFTSAANFFPPILFAQGD 93
Cdd:COG4245   1 NPMRRLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYALETVEVSVITFdGEAKVLLPLTDLEDFQPPDLSASGG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  94 TPMGAAITKALDMVEERKREYRANGISYYRPWIFLITDGAPTD-EWQAAANKVFRGEEDKRFAFFSIGV-QGADMKTLAQ 171
Cdd:COG4245  81 TPLGAALELLLDLIERRVQKYTAEGKGDWRPVVFLITDGEPTDsDWEAALQRLKDGEAAKKANIFAIGVgPDADTEVLKQ 160

                       170       180
                ....*....|....*....|
gi 13878870 172 IS--VRQPLPLQGLQFRELF 189
Cdd:COG4245 161 LTdpVRALDALDGLDFREFF 180
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 23-173 1.88e-17

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: 76.34  E-value: 1.88e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870     23 ILLLDVSGSMNGRPINELNAGLVTFRDELLADPlalKRVELGIVTFG-PVHVEQPFT---------SAANFFPPilFAQG 92
Cdd:smart00327   3 VFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGP---DGDRVGLVTFSdDARVLFPLNdsrskdallEALASLSY--KLGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870     93 DTPMGAAITKALDMVEERKREYRANGisyyRPWIFLITDGAPTDEWQAAAnKVFRGEEDKRFAFFSIGV-QGADMKTLAQ 171
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGSRRGA----PKVVILITDGESNDGPKDLL-KAAKELKRSGVKVFVVGVgNDVDEEELKK 152


                   ..
gi 13878870    172 IS 173
Cdd:smart00327 153 LA 154
VWA pfam00092
von Willebrand factor type A domain;
23-173 1.20e-12

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 63.45  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870    23 ILLLDVSGSMNGRPINELNAGLVTFRDELLADPlalKRVELGIVTF-GPVHVEQPFTSAANF-------FPPILFAQGDT 94
Cdd:pfam00092   3 VFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGP---DGTRVGLVQYsSDVRTEFPLNDYSSKeellsavDNLRYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870    95 PMGAAITKALDMVEERKREYRANGISYyrpwIFLITDGAPTD-EWQAAANKVfrgeEDKRFAFFSIGVQGADMKTLAQIS 173
Cdd:pfam00092  80 NTGKALKYALENLFSSAAGARPGAPKV----VVLLTDGRSQDgDPEEVAREL----KSAGVTVFAVGVGNADDEELRKIA 151
 
Name Accession Description Interval E-value
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 17-189 7.25e-88

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: 256.88  E-value: 7.25e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  17 EPRCPCILLLDVSGSMNGRPINELNAGLVTFRDELLADPLALKRVELGIVTF-GPVHVEQPFTSAANFFPPILFAQGDTP 95
Cdd:cd01464   1 MRRLPIYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPYALESVEISVITFdSAARVIVPLTPLESFQPPRLTASGGTS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  96 MGAAITKALDMVEERKREYRANGISYYRPWIFLITDGAPTDEWQAAAnKVFRGEED--KRFAFFSIGVqGADMKTLAQIS 173
Cdd:cd01464  81 MGAALELALDCIDRRVQRYRADQKGDWRPWVFLLTDGEPTDDLTAAI-ERIKEARDskGRIVACAVGP-KADLDTLKQIT 158

                       170
                ....*....|....*.
gi 13878870 174 VRQPLPLQGLQFRELF 189
Cdd:cd01464 159 EGVPLLDDALSGLNFF 174
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
15-189 1.65e-81

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 241.37  E-value: 1.65e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  15 NPEPRCPCILLLDVSGSMNGRPINELNAGLVTFRDELLADPLALKRVELGIVTF-GPVHVEQPFTSAANFFPPILFAQGD 93
Cdd:COG4245   1 NPMRRLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYALETVEVSVITFdGEAKVLLPLTDLEDFQPPDLSASGG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  94 TPMGAAITKALDMVEERKREYRANGISYYRPWIFLITDGAPTD-EWQAAANKVFRGEEDKRFAFFSIGV-QGADMKTLAQ 171
Cdd:COG4245  81 TPLGAALELLLDLIERRVQKYTAEGKGDWRPVVFLITDGEPTDsDWEAALQRLKDGEAAKKANIFAIGVgPDADTEVLKQ 160

                       170       180
                ....*....|....*....|
gi 13878870 172 IS--VRQPLPLQGLQFRELF 189
Cdd:COG4245 161 LTdpVRALDALDGLDFREFF 180
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 23-173 1.88e-17

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: 76.34  E-value: 1.88e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870     23 ILLLDVSGSMNGRPINELNAGLVTFRDELLADPlalKRVELGIVTFG-PVHVEQPFT---------SAANFFPPilFAQG 92
Cdd:smart00327   3 VFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGP---DGDRVGLVTFSdDARVLFPLNdsrskdallEALASLSY--KLGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870     93 DTPMGAAITKALDMVEERKREYRANGisyyRPWIFLITDGAPTDEWQAAAnKVFRGEEDKRFAFFSIGV-QGADMKTLAQ 171
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGSRRGA----PKVVILITDGESNDGPKDLL-KAAKELKRSGVKVFVVGVgNDVDEEELKK 152


                   ..
gi 13878870    172 IS 173
Cdd:smart00327 153 LA 154
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 23-173 3.25e-14

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: 67.59  E-value: 3.25e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  23 ILLLDVSGSMNGRPINELNAGLVTFRDELLADPlalKRVELGIVTFG-PVHVEQPFTSAANFFPPILFAQ-------GDT 94
Cdd:cd00198   4 VFLLDVSGSMGGEKLDKAKEALKALVSSLSASP---PGDRVGLVTFGsNARVVLPLTTDTDKADLLEAIDalkkglgGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  95 PMGAAITKALDMVEERKREYRangisyyRPWIFLITDGAPTDEWQAAANKVfRGEEDKRFAFFSIGV-QGADMKTLAQIS 173
Cdd:cd00198  81 NIGAALRLALELLKSAKRPNA-------RRVIILLTDGEPNDGPELLAEAA-RELRKLGITVYTIGIgDDANEDELKEIA 152
VWA pfam00092
von Willebrand factor type A domain;
23-173 1.20e-12

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 63.45  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870    23 ILLLDVSGSMNGRPINELNAGLVTFRDELLADPlalKRVELGIVTF-GPVHVEQPFTSAANF-------FPPILFAQGDT 94
Cdd:pfam00092   3 VFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGP---DGTRVGLVQYsSDVRTEFPLNDYSSKeellsavDNLRYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870    95 PMGAAITKALDMVEERKREYRANGISYyrpwIFLITDGAPTD-EWQAAANKVfrgeEDKRFAFFSIGVQGADMKTLAQIS 173
Cdd:pfam00092  80 NTGKALKYALENLFSSAAGARPGAPKV----VVLLTDGRSQDgDPEEVAREL----KSAGVTVFAVGVGNADDEELRKIA 151
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 23-171 2.88e-12

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 63.93  E-value: 2.88e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  23 ILLLDVSGSMNGRPINELNAGLVtfrdELLAdpLALKRVELGIVTFG-PVHVEQPFTSAANFFPPI-----LFAQGDTPM 96
Cdd:COG2425 122 VLCVDTSGSMAGSKEAAAKAAAL----ALLR--ALRPNRRFGVILFDtEVVEDLPLTADDGLEDAIeflsgLFAGGGTDI 195

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13878870  97 GAAITKALDMVEERKREYRAngisyyrpwIFLITDGAPTDEWQAAANKVFRGEEDKRFAFFSIGVQGAD--MKTLAQ 171
Cdd:COG2425 196 APALRAALELLEEPDYRNAD---------IVLITDGEAGVSPEELLREVRAKESGVRLFTVAIGDAGNPglLEALAD 263
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 23-173 1.69e-11

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: 61.88  E-value: 1.69e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  23 ILLLDVSGSMNGRP-INELNAGLVTFRDELladplaLKRVELGIVTF-GPVHVEQPFTSAANFFPPILF---AQGDTPMG 97
Cdd:COG1240  96 VLVVDASGSMAAENrLEAAKGALLDFLDDY------RPRDRVGLVAFgGEAEVLLPLTRDREALKRALDelpPGGGTPLG 169

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13878870  98 AAITKALDMVEERKREyrangisyYRPWIFLITDGAPTD---EWQAAANKVfrGEEDKRFAFFSIGVQGADMKTLAQIS 173
Cdd:COG1240 170 DALALALELLKRADPA--------RRKVIVLLTDGRDNAgriDPLEAAELA--AAAGIRIYTIGVGTEAVDEGLLREIA 238
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 23-171 1.82e-11

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 62.04  E-value: 1.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  23 ILLLDVSGSMNGRPINELNAGLVTFRDELLADplalkrVELGIVTF-GPVHVEQPFTSAANfFPPI------LFAQGDTP 95
Cdd:COG2304  95 VFVIDVSGSMSGDKLELAKEAAKLLVDQLRPG------DRVSIVTFaGDARVLLPPTPATD-RAKIlaaidrLQAGGGTA 167

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  96 MGAAITKALDMVEERKREYRANgisyyRpwIFLITDGAPTDEWQAAAN--KVFRGEEDKRFAFFSIGVqGAD-----MKT 168
Cdd:COG2304 168 LGAGLELAYELARKHFIPGRVN-----R--VILLTDGDANVGITDPEEllKLAEEAREEGITLTTLGV-GSDynedlLER 239


                ...
gi 13878870 169 LAQ 171
Cdd:COG2304 240 LAD 242
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 24-153 1.27e-08

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


Pssm-ID: 238731 [Multi-domain]  Cd Length: 174  Bit Score: 52.71  E-value: 1.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  24 LLLDVSGSMNG-RPINELNAGLVTFRDELLA--DPLAL----------KRVEL-GIVTFGPVHVEQPFTSAANFFPpilf 89
Cdd:cd01454   5 LLLDLSGSMRSdRRIDVAKKAAVLLAEALEAcgVPHAIlgfttdaggrERVRWiKIKDFDESLHERARKRLAALSP---- 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13878870  90 aQGDTPMGAAITKALDMVEERKREyrangisyyRPWIFLITDGAPTDeWQAAANKVFRGEEDKR 153
Cdd:cd01454  81 -GGNTRDGAAIRHAAERLLARPEK---------RKILLVISDGEPND-LDYYEGNVFATEDALR 133
VWA_2 pfam13519
von Willebrand factor type A domain;
23-116 1.18e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 48.44  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870    23 ILLLDVSGSMNGRPINELNAGLVT-FRDELLAdplALKRVELGIVTFG-PVHVEQPFTS----AANFFPPILFAQGDTPM 96
Cdd:pfam13519   2 VFVLDTSGSMRNGDYGPTRLEAAKdAVLALLK---SLPGDRVGLVTFGdGPEVLIPLTKdrakILRALRRLEPKGGGTNL 78

                          90       100
                  ....*....|....*....|
gi 13878870    97 GAAITKALDMVEERKREYRA 116
Cdd:pfam13519  79 AAALQLARAALKHRRKNQPR 98
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 23-136 1.83e-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: 43.15  E-value: 1.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  23 ILLLDVSGSMNGRPINELNAGLvTFRDELLADplalkRVELGIVTFGpvhveqpfTSAANFFP----------------P 86
Cdd:cd01466   4 VAVLDVSGSMAGDKLQLVKHAL-RFVISSLGD-----ADRLSIVTFS--------TSAKRLSPlrrmtakgkrsakrvvD 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 13878870  87 ILFAQGDTPMGAAITKALDMVEERKREYRAngisyyrPWIFLITDGAPTD 136
Cdd:cd01466  70 GLQAGGGTNVVGGLKKALKVLGDRRQKNPV-------ASIMLLSDGQDNH 112
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 24-135 2.97e-05

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: 43.03  E-value: 2.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  24 LLLDVSGSMNGRPINELNAGLVTFRDELLADPlalkrvELGIVTF-GPVHVEQPFTSAANfFPPI------LFAQGDTPM 96
Cdd:cd01465   5 FVIDRSGSMDGPKLPLVKSALKLLVDQLRPDD------RLAIVTYdGAAETVLPATPVRD-KAAIlaaidrLTAGGSTAG 77

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 13878870  97 GAAITKALDMVEERKREYRANgisyyRpwIFLITDGAPT 135
Cdd:cd01465  78 GAGIQLGYQEAQKHFVPGGVN-----R--ILLATDGDFN 109
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 21-164 1.46e-04

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: 40.79  E-value: 1.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  21 PCILLLDVSGSMNGRPInELNAGLVTfrdeLLADPLALKRVELGIVTFGPVHVEQPFTSAANFFPPI-----LFAQGDTP 95
Cdd:cd01462   2 PVILLVDQSGSMYGAPE-EVAKAVAL----ALLRIALAENRDTYLILFDSEFQTKIVDKTDDLEEPVeflsgVQLGGGTD 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13878870  96 MGAAITKALDMVEERKREyraNGIsyyrpwIFLITDG---APTDEWQAAANKVFRGeeDKRFAFFSIGVQGA 164
Cdd:cd01462  77 INKALRYALELIERRDPR---KAD------IVLITDGyegGVSDELLREVELKRSR--VARFVALALGDHGN 137
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 23-173 2.70e-04

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 39.97  E-value: 2.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  23 ILLLDVSGSMNgrpinelNAGLVTFRD--ELLADPL--ALKRVELGIVTF-GPVHVEQPFTSAANF------FPPILFAQ 91
Cdd:cd01450   4 VFLLDGSESVG-------PENFEKVKDfiEKLVEKLdiGPDKTRVGLVQYsDDVRVEFSLNDYKSKddllkaVKNLKYLG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  92 GDTPM-GAAITKALDMV-EERKREYRANGIsyyrpwIFLITDGAPTDEWQA--AANKvfrgEEDKRFAFFSIGVQGADMK 167
Cdd:cd01450  77 GGGTNtGKALQYALEQLfSESNARENVPKV------IIVLTDGRSDDGGDPkeAAAK----LKDEGIKVFVVGVGPADEE 146


                ....*.
gi 13878870 168 TLAQIS 173
Cdd:cd01450 147 ELREIA 152
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 23-173 3.47e-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: 39.89  E-value: 3.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  23 ILLLDVSGSMNGRPINELNAGLVTFRDELLADPLalkrveLGIVTFG---------PVHVEQPFTSAANFFPPILFAQGD 93
Cdd:cd01461   6 VFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDY------FNIIGFSdtveefspsSVSATAENVAAAIEYVNRLQALGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878870  94 TPMGAAITKALDMVEerkreyRANGISyyrPWIFLITDGAPTDEWQAAANkvFRGEEDKRFAFFSIGV-QGAD---MKTL 169
Cdd:cd01461  80 TNMNDALEAALELLN------SSPGSV---PQIILLTDGEVTNESQILKN--VREALSGRIRLFTFGIgSDVNtylLERL 148


                ....
gi 13878870 170 AQIS 173
Cdd:cd01461 149 AREG 152
 
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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