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Conserved domains on  [gi|16130205|ref|NP_416773|]
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IPR002035/DUF3520 domain-containing protein YfbK [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

vWA domain-containing protein( domain architecture ID 13939702)

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
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 110-430 2.73e-99

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


:

Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 303.18  E-value: 2.73e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 110 DNPVKQVAQNPLATFSLDVDTGSYANVRRFLNQGLLPPPDAVRVEEIVNYFPSDWDikdkqsipaskpipfAMRYELAPA 189
Cdd:COG2304   2 EAGFAAADTVPLSTSSADVDAASSSNRRRLLVGGEPPPAAAVRLEELVNFFPYDYP---------------LPTGRLAQS 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 190 PWNEQRTLLKVDILAKDRKSEELPASNLVFLIDTSGSMiSDERLPLIQSSLKLLVKELREQDNIAIVTYAGDSRIALPSI 269
Cdd:COG2304  67 PWNPQTRLLLVGLQPPKAAAEERPPLNLVFVIDVSGSM-SGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPPT 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 270 SGSHKAEINAAIDSLDAEGSTNGGAGLELAYQQATKGFIKGGINRILLATDGDFNVGIDDPKSIESMVKKQRESGVTLST 349
Cdd:COG2304 146 PATDRAKILAAIDRLQAGGGTALGAGLELAYELARKHFIPGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTT 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 350 FGVGnSNYNEAMMVRIADVGNGNYSYIDTLSEAQKVLnsemrqmlitvakdvkaqiefnpawVTEYRQIGYEKRQLRVEH 429
Cdd:COG2304 226 LGVG-SDYNEDLLERLADAGGGNYYYIDDPEEAEKVF-------------------------VREFSRIGYENRALATED 279


                .
gi 16130205 430 F 430
Cdd:COG2304 280 F 280
DUF3520 pfam12034
Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. ...
 392-569 1.54e-91

Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 180 amino acids in length. This domain is found associated with pfam00092.


:

Pssm-ID: 432277  Cd Length: 182  Bit Score: 279.04  E-value: 1.54e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205   392 QMLITVAKDVKAQIEFNPAWVTEYRQIGYEKRQLRVEHFNNDNVDAGDIGAGKHITLLFELTLNGQKAS-IDKLRYAPDN 470
Cdd:pfam12034   1 STLFTIAKDVKIQVEFNPAQVKEYRLIGYENRLLAREDFNNDKVDAGEIGAGHTVTALYEIVPVGSKSDlVDPLKYQDAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205   471 KlAKSDKTKELAWLKIRWKYPQGKESQLVEFPL---GPTINAPSEDMRFRAAVAAYGQKLRGSEYLNNTSWQQIKQWAQQ 547
Cdd:pfam12034  81 A-AAAANSDELATVKLRYKLPDGDKSRLIEYPVadaATAFAQASDDFRFAAAVAGFGMLLRGSEYKGDASYDDVIELARG 159

                         170       180
                  ....*....|....*....|..
gi 16130205   548 AKGEDPQGYRAEFIRLIELADG 569
Cdd:pfam12034 160 AKGEDPDGYRAEFIRLVEKAKS 181
 
Name Accession Description Interval E-value
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 110-430 2.73e-99

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 303.18  E-value: 2.73e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 110 DNPVKQVAQNPLATFSLDVDTGSYANVRRFLNQGLLPPPDAVRVEEIVNYFPSDWDikdkqsipaskpipfAMRYELAPA 189
Cdd:COG2304   2 EAGFAAADTVPLSTSSADVDAASSSNRRRLLVGGEPPPAAAVRLEELVNFFPYDYP---------------LPTGRLAQS 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 190 PWNEQRTLLKVDILAKDRKSEELPASNLVFLIDTSGSMiSDERLPLIQSSLKLLVKELREQDNIAIVTYAGDSRIALPSI 269
Cdd:COG2304  67 PWNPQTRLLLVGLQPPKAAAEERPPLNLVFVIDVSGSM-SGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPPT 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 270 SGSHKAEINAAIDSLDAEGSTNGGAGLELAYQQATKGFIKGGINRILLATDGDFNVGIDDPKSIESMVKKQRESGVTLST 349
Cdd:COG2304 146 PATDRAKILAAIDRLQAGGGTALGAGLELAYELARKHFIPGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTT 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 350 FGVGnSNYNEAMMVRIADVGNGNYSYIDTLSEAQKVLnsemrqmlitvakdvkaqiefnpawVTEYRQIGYEKRQLRVEH 429
Cdd:COG2304 226 LGVG-SDYNEDLLERLADAGGGNYYYIDDPEEAEKVF-------------------------VREFSRIGYENRALATED 279


                .
gi 16130205 430 F 430
Cdd:COG2304 280 F 280
DUF3520 pfam12034
Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. ...
 392-569 1.54e-91

Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 180 amino acids in length. This domain is found associated with pfam00092.


Pssm-ID: 432277  Cd Length: 182  Bit Score: 279.04  E-value: 1.54e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205   392 QMLITVAKDVKAQIEFNPAWVTEYRQIGYEKRQLRVEHFNNDNVDAGDIGAGKHITLLFELTLNGQKAS-IDKLRYAPDN 470
Cdd:pfam12034   1 STLFTIAKDVKIQVEFNPAQVKEYRLIGYENRLLAREDFNNDKVDAGEIGAGHTVTALYEIVPVGSKSDlVDPLKYQDAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205   471 KlAKSDKTKELAWLKIRWKYPQGKESQLVEFPL---GPTINAPSEDMRFRAAVAAYGQKLRGSEYLNNTSWQQIKQWAQQ 547
Cdd:pfam12034  81 A-AAAANSDELATVKLRYKLPDGDKSRLIEYPVadaATAFAQASDDFRFAAAVAGFGMLLRGSEYKGDASYDDVIELARG 159

                         170       180
                  ....*....|....*....|..
gi 16130205   548 AKGEDPQGYRAEFIRLIELADG 569
Cdd:pfam12034 160 AKGEDPDGYRAEFIRLVEKAKS 181
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 215-386 2.62e-85

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: 262.59  E-value: 2.62e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 215 SNLVFLIDTSGSMiSDERLPLIQSSLKLLVKELREQDNIAIVTYAGDSRIALPSISGSHKAEINAAIDSLDAEGSTNGGA 294
Cdd:cd01465   1 LNLVFVIDRSGSM-DGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTAGGSTAGGA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 295 GLELAYQQATKGFIKGGINRILLATDGDFNVGIDDPKSIESMVKKQRESGVTLSTFGVGnSNYNEAMMVRIADVGNGNYS 374
Cdd:cd01465  80 GIQLGYQEAQKHFVPGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFG-DNYNEDLMEAIADAGNGNTA 158

                       170
                ....*....|..
gi 16130205 375 YIDTLSEAQKVL 386
Cdd:cd01465 159 YIDNLAEARKVF 170
vWF_A pfam12450
von Willebrand factor; This domain family is found in bacteria, and is approximately 100 amino ...
 99-199 6.51e-47

von Willebrand factor; This domain family is found in bacteria, and is approximately 100 amino acids in length. The family is found in association with pfam00092. There are two conserved sequence motifs: STF and DVD. There are two completely conserved residues (E and N) that may be functionally important. In hemostasis, platelet adhesion to the damaged vessel wall is mediated by several proteins, including von Willebrand factor. In solution vWF becomes immobilized via its A3 domain on the fibrillar collagen of the vessel wall and acts as an intermediary between collagen and the platelet receptor glycoprotein Ibalpha (GPIbalpha), which is the only platelet receptor that does not require prior activation for bond formation.


Pssm-ID: 432562 [Multi-domain]  Cd Length: 94  Bit Score: 159.24  E-value: 6.51e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205    99 NPGTARYQQFDDNPVKQVAQNPLATFSLDVDTGSYANVRRFLNQGLLPPPDAVRVEEIVNYFPSDWDIKDKQSipaskpi 178
Cdd:pfam12450   1 PFNTEEYKKIEENPFISVAENPLSTFSIDVDTASYSNVRRFINQGQLPPADAVRIEEMINYFDYDYPQPTGDD------- 73

                          90       100
                  ....*....|....*....|.
gi 16130205   179 PFAMRYELAPAPWNEQRTLLK 199
Cdd:pfam12450  74 PFSVTTEVAPCPWNPDHKLLR 94
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 216-383 1.84e-25

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 103.30  E-value: 1.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205    216 NLVFLIDTSGSMiSDERLPLIQSSLKLLVKELREQ---DNIAIVTYAGDSRIALPSISGSHKAEINAAIDSL--DAEGST 290
Cdd:smart00327   1 DVVFLLDGSGSM-GGNRFELAKEFVLKLVEQLDIGpdgDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLsyKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205    291 NGGAGLELAYQQ---ATKGFIKGGINRILLATDGDFNvgiDDPKSIESMVKKQRESGVTLSTFGVGNsNYNEAMMVRIAD 367
Cdd:smart00327  80 NLGAALQYALENlfsKSAGSRRGAPKVVILITDGESN---DGPKDLLKAAKELKRSGVKVFVVGVGN-DVDEEELKKLAS 155

                          170
                   ....*....|....*.
gi 16130205    368 VGNGNYSYIDTLSEAQ 383
Cdd:smart00327 156 APGGVYVFLPELLDLL 171
PRK13685 PRK13685
hypothetical protein; Provisional
 218-393 1.11e-07

hypothetical protein; Provisional


Pssm-ID: 184242 [Multi-domain]  Cd Length: 326  Bit Score: 53.94  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205  218 VFLIDTSGSM----ISDERLPLIQSSLKLLVKELREQDNIAIVTYAGDSRIaLPSISGSHKAEINAaIDSLDAEGSTNGG 293
Cdd:PRK13685  92 MLVIDVSQSMratdVEPNRLAAAQEAAKQFADELTPGINLGLIAFAGTATV-LVSPTTNREATKNA-IDKLQLADRTATG 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205  294 AGLELAYQQ-ATKGFIKGGIN-----RILLATDGDFNVG--IDDPKSIESMVKKQRESGVTLSTFGVGNSN--------- 356
Cdd:PRK13685 170 EAIFTALQAiATVGAVIGGGDtpppaRIVLMSDGKETVPtnPDNPRGAYTAARTAKDQGVPISTISFGTPYgsveingqr 249

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 16130205  357 ----YNEAMMVRIADVGNGNYSYIDTLSEAQKVLNSEMRQM 393
Cdd:PRK13685 250 qpvpVDDESLKKIAQLSGGEFYTAASLEELRAVYATLQQQI 290
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 207-392 9.71e-04

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: 41.52  E-value: 9.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205   207 RKSEELPASnLVFLIDTSGSMISDeRLPLIQSSLKLLVKELREQDNIAIVTYAGDSRIaLPSISGSHKaEINAAIDSLDA 286
Cdd:TIGR03436  47 RRETDLPLT-VGLVIDTSGSMRND-LDRARAAAIRFLKTVLRPNDRVFVVTFNTRLRL-LQDFTSDPR-LLEAALNRLKP 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205   287 ---------------EGSTNGGAGLELAYQQATKGFIKGGINR--ILLATDGDFNvgiddpksiESMVKKQR------ES 343
Cdd:TIGR03436 123 plrtdynssgafvrdGGGTALYDAITLAALEQLANALAGIPGRkaLIVISDGGDN---------RSRDTLERaidaaqRA 193

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130205   344 GVTL------------STFGVGNSNYNEAMMVRIADVGNGNYSYIDT--LSEAQKVLNSEMRQ 392
Cdd:TIGR03436 194 DVAIysidarglrapdLGAGAKAGLGGPEALERLAEETGGRAFYVNSndLDGAFAQIAEELRS 256
 
Name Accession Description Interval E-value
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 110-430 2.73e-99

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 303.18  E-value: 2.73e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 110 DNPVKQVAQNPLATFSLDVDTGSYANVRRFLNQGLLPPPDAVRVEEIVNYFPSDWDikdkqsipaskpipfAMRYELAPA 189
Cdd:COG2304   2 EAGFAAADTVPLSTSSADVDAASSSNRRRLLVGGEPPPAAAVRLEELVNFFPYDYP---------------LPTGRLAQS 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 190 PWNEQRTLLKVDILAKDRKSEELPASNLVFLIDTSGSMiSDERLPLIQSSLKLLVKELREQDNIAIVTYAGDSRIALPSI 269
Cdd:COG2304  67 PWNPQTRLLLVGLQPPKAAAEERPPLNLVFVIDVSGSM-SGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPPT 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 270 SGSHKAEINAAIDSLDAEGSTNGGAGLELAYQQATKGFIKGGINRILLATDGDFNVGIDDPKSIESMVKKQRESGVTLST 349
Cdd:COG2304 146 PATDRAKILAAIDRLQAGGGTALGAGLELAYELARKHFIPGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTT 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 350 FGVGnSNYNEAMMVRIADVGNGNYSYIDTLSEAQKVLnsemrqmlitvakdvkaqiefnpawVTEYRQIGYEKRQLRVEH 429
Cdd:COG2304 226 LGVG-SDYNEDLLERLADAGGGNYYYIDDPEEAEKVF-------------------------VREFSRIGYENRALATED 279


                .
gi 16130205 430 F 430
Cdd:COG2304 280 F 280
DUF3520 pfam12034
Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. ...
 392-569 1.54e-91

Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 180 amino acids in length. This domain is found associated with pfam00092.


Pssm-ID: 432277  Cd Length: 182  Bit Score: 279.04  E-value: 1.54e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205   392 QMLITVAKDVKAQIEFNPAWVTEYRQIGYEKRQLRVEHFNNDNVDAGDIGAGKHITLLFELTLNGQKAS-IDKLRYAPDN 470
Cdd:pfam12034   1 STLFTIAKDVKIQVEFNPAQVKEYRLIGYENRLLAREDFNNDKVDAGEIGAGHTVTALYEIVPVGSKSDlVDPLKYQDAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205   471 KlAKSDKTKELAWLKIRWKYPQGKESQLVEFPL---GPTINAPSEDMRFRAAVAAYGQKLRGSEYLNNTSWQQIKQWAQQ 547
Cdd:pfam12034  81 A-AAAANSDELATVKLRYKLPDGDKSRLIEYPVadaATAFAQASDDFRFAAAVAGFGMLLRGSEYKGDASYDDVIELARG 159

                         170       180
                  ....*....|....*....|..
gi 16130205   548 AKGEDPQGYRAEFIRLIELADG 569
Cdd:pfam12034 160 AKGEDPDGYRAEFIRLVEKAKS 181
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 215-386 2.62e-85

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: 262.59  E-value: 2.62e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 215 SNLVFLIDTSGSMiSDERLPLIQSSLKLLVKELREQDNIAIVTYAGDSRIALPSISGSHKAEINAAIDSLDAEGSTNGGA 294
Cdd:cd01465   1 LNLVFVIDRSGSM-DGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTAGGSTAGGA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 295 GLELAYQQATKGFIKGGINRILLATDGDFNVGIDDPKSIESMVKKQRESGVTLSTFGVGnSNYNEAMMVRIADVGNGNYS 374
Cdd:cd01465  80 GIQLGYQEAQKHFVPGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFG-DNYNEDLMEAIADAGNGNTA 158

                       170
                ....*....|..
gi 16130205 375 YIDTLSEAQKVL 386
Cdd:cd01465 159 YIDNLAEARKVF 170
vWF_A pfam12450
von Willebrand factor; This domain family is found in bacteria, and is approximately 100 amino ...
 99-199 6.51e-47

von Willebrand factor; This domain family is found in bacteria, and is approximately 100 amino acids in length. The family is found in association with pfam00092. There are two conserved sequence motifs: STF and DVD. There are two completely conserved residues (E and N) that may be functionally important. In hemostasis, platelet adhesion to the damaged vessel wall is mediated by several proteins, including von Willebrand factor. In solution vWF becomes immobilized via its A3 domain on the fibrillar collagen of the vessel wall and acts as an intermediary between collagen and the platelet receptor glycoprotein Ibalpha (GPIbalpha), which is the only platelet receptor that does not require prior activation for bond formation.


Pssm-ID: 432562 [Multi-domain]  Cd Length: 94  Bit Score: 159.24  E-value: 6.51e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205    99 NPGTARYQQFDDNPVKQVAQNPLATFSLDVDTGSYANVRRFLNQGLLPPPDAVRVEEIVNYFPSDWDIKDKQSipaskpi 178
Cdd:pfam12450   1 PFNTEEYKKIEENPFISVAENPLSTFSIDVDTASYSNVRRFINQGQLPPADAVRIEEMINYFDYDYPQPTGDD------- 73

                          90       100
                  ....*....|....*....|.
gi 16130205   179 PFAMRYELAPAPWNEQRTLLK 199
Cdd:pfam12450  74 PFSVTTEVAPCPWNPDHKLLR 94
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 144-389 1.26e-31

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: 123.12  E-value: 1.26e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 144 LLPPPDAVRVEEIVNYFPSDWDIKDKQSIPASKPIPFAMRYELAPAPWNEQRTLLKVDILAKDRKSEELPASNLVFLIDT 223
Cdd:COG1240  22 LLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDA 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 224 SGSMISDERLPLIQSSLKLLVKELREQDNIAIVTYAGDSRIALPsiSGSHKAEINAAIDSLDAEGSTNGGAGLELAYQQA 303
Cdd:COG1240 102 SGSMAAENRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEVLLP--LTRDREALKRALDELPPGGGTPLGDALALALELL 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 304 tKGFIKGGINRILLATDGDFNVGIDDPksiESMVKKQRESGVTLSTFGVGNSNYNEAMMVRIADVGNGNYSYIDTLSEAQ 383
Cdd:COG1240 180 -KRADPARRKVIVLLTDGRDNAGRIDP---LEAAELAAAAGIRIYTIGVGTEAVDEGLLREIAEATGGRYFRADDLSELA 255


                ....*.
gi 16130205 384 KVLNSE 389
Cdd:COG1240 256 AIYREI 261
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 216-375 2.36e-27

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: 108.04  E-value: 2.36e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 216 NLVFLIDTSGSMiSDERLPLIQSSLKLLVKEL---REQDNIAIVTYAGDSRIALPSISGSHKAEINAAIDSLD--AEGST 290
Cdd:cd00198   2 DIVFLLDVSGSM-GGEKLDKAKEALKALVSSLsasPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkgLGGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 291 NGGAGLELAYQQATKGFIKGGINRILLATDGDFNVGIDDPKSIESMVKKqreSGVTLSTFGVGnSNYNEAMMVRIADVGN 370
Cdd:cd00198  81 NIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRK---LGITVYTIGIG-DDANEDELKEIADKTT 156


                ....*
gi 16130205 371 GNYSY 375
Cdd:cd00198 157 GGAVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 216-383 1.84e-25

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 103.30  E-value: 1.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205    216 NLVFLIDTSGSMiSDERLPLIQSSLKLLVKELREQ---DNIAIVTYAGDSRIALPSISGSHKAEINAAIDSL--DAEGST 290
Cdd:smart00327   1 DVVFLLDGSGSM-GGNRFELAKEFVLKLVEQLDIGpdgDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLsyKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205    291 NGGAGLELAYQQ---ATKGFIKGGINRILLATDGDFNvgiDDPKSIESMVKKQRESGVTLSTFGVGNsNYNEAMMVRIAD 367
Cdd:smart00327  80 NLGAALQYALENlfsKSAGSRRGAPKVVILITDGESN---DGPKDLLKAAKELKRSGVKVFVVGVGN-DVDEEELKKLAS 155

                          170
                   ....*....|....*.
gi 16130205    368 VGNGNYSYIDTLSEAQ 383
Cdd:smart00327 156 APGGVYVFLPELLDLL 171
VWA pfam00092
von Willebrand factor type A domain;
216-389 4.18e-24

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 99.27  E-value: 4.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205   216 NLVFLIDTSGSMiSDERLPLIQSSLKLLVKEL---REQDNIAIVTYAGDSRIALPSISGSHKAEINAAIDSLDAE--GST 290
Cdd:pfam00092   1 DIVFLLDGSGSI-GGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLggGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205   291 NGGAGLELAYQQATK---GFIKGGINRILLATDGDFNVGiddpkSIESMVKKQRESGVTLSTFGVGNSNYNEamMVRIAD 367
Cdd:pfam00092  80 NTGKALKYALENLFSsaaGARPGAPKVVVLLTDGRSQDG-----DPEEVARELKSAGVTVFAVGVGNADDEE--LRKIAS 152

                         170       180
                  ....*....|....*....|..
gi 16130205   368 VGNGNYSYIDTLSEAQKVLNSE 389
Cdd:pfam00092 153 EPGEGHVFTVSDFEALEDLQDQ 174
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 216-376 1.81e-17

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: 79.95  E-value: 1.81e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 216 NLVFLIDTSGSMISDerlPLIQ--SSLKLLVKELREQDNIAIVTYAGDSRIALPSISGSHKAEINAAID---SLDAEGST 290
Cdd:cd01461   4 EVVFVIDTSGSMSGT---KIEQtkEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEyvnRLQALGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 291 NGGAGLELAYQQATKGfiKGGINRILLATDGDfnvgIDDPKSIESMVKKQRESGVTLSTFGVGNSnYNEAMMVRIADVGN 370
Cdd:cd01461  81 NMNDALEAALELLNSS--PGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSD-VNTYLLERLAREGR 153


                ....*.
gi 16130205 371 GNYSYI 376
Cdd:cd01461 154 GIARRI 159
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 100-367 2.62e-17

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 82.04  E-value: 2.62e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 100 PGTARYQQFDDNPVKQVAQNPLATFSLDVDTGSYANVRRfLNQGLLPPPDAVRVEEIVNYFPSDWDIKDKQSIPASKPIP 179
Cdd:COG2425   3 PDAAAAARLAALLLAPAPATALLLAGLLRAALALGLALA-LRAALLALLLLLLRAALALLTLLAGLVLLALDALLLAALL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 180 FAMRY--ELAPAPWNEQRTLLKVDILAKDRKSEELPASNLVFLIDTSGSMiSDERLPLIQSSLKLLVKELREQDNIAIVT 257
Cdd:COG2425  82 AALLDalLLAVLLLALLLLAALLLLAAPASAAVPLLEGPVVLCVDTSGSM-AGSKEAAAKAAALALLRALRPNRRFGVIL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 258 YAGDSRIALPSISGSHKAEINAAIDSLDAEGSTNGGAGLELAYQQATKGFIKGGInrILLATDGDfnVGIDDPKSIESMv 337
Cdd:COG2425 161 FDTEVVEDLPLTADDGLEDAIEFLSGLFAGGGTDIAPALRAALELLEEPDYRNAD--IVLITDGE--AGVSPEELLREV- 235

                       250       260       270
                ....*....|....*....|....*....|
gi 16130205 338 kKQRESGVTLSTFGVGNSNyNEAMMVRIAD 367
Cdd:COG2425 236 -RAKESGVRLFTVAIGDAG-NPGLLEALAD 263
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 216-375 4.03e-15

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 73.09  E-value: 4.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 216 NLVFLIDTSGSmISDERLPLIQSSLKLLVKELR---EQDNIAIVTYAGDSRIALPSISGSHKAEINAAIDSLDAEGS--T 290
Cdd:cd01450   2 DIVFLLDGSES-VGPENFEKVKDFIEKLVEKLDigpDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGggT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 291 NGGAGLELAYQQ-ATKGFIKGGINR-ILLATDGDfnvgIDDPKSIESMVKKQRESGVTLSTFGVGNSNYNEamMVRIADV 368
Cdd:cd01450  81 NTGKALQYALEQlFSESNARENVPKvIIVLTDGR----SDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEE--LREIASC 154


                ....*..
gi 16130205 369 GNGNYSY 375
Cdd:cd01450 155 PSERHVF 161
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 217-376 9.53e-15

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: 72.04  E-value: 9.53e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 217 LVFLIDTSGSMiSDERLPLIQSSLKLLVKELREQDNIAIVTYAGDSRIALP--SISGSHKAEINAAIDSLDAEGSTNGGA 294
Cdd:cd01466   3 LVAVLDVSGSM-AGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSPlrRMTAKGKRSAKRVVDGLQAGGGTNVVG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 295 GLELAYQQATKGFIKGGINRILLATDGDFNVGIDDPKSiesmvkkqRESGVTLSTFGVGNSNyNEAMMVRIADVGNGNYS 374
Cdd:cd01466  82 GLKKALKVLGDRRQKNPVASIMLLSDGQDNHGAVVLRA--------DNAPIPIHTFGLGASH-DPALLAFIAEITGGTFS 152


                ..
gi 16130205 375 YI 376
Cdd:cd01466 153 YV 154
VWA_3 pfam13768
von Willebrand factor type A domain;
215-374 1.46e-10

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 59.72  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205   215 SNLVFLIDTSGSMiSDERlPLIQSSLKLLVKELREQDNIAIVTYAGDSRIALP---SISGSHKAEINAAIDSLDAEgstN 291
Cdd:pfam13768   1 GDVVIVVDVSSSM-SGEP-KLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPgwrVVSPRSLQEAFQFIKTLQPP---L 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205   292 GGAGLELAYQQATKGFIKGGINR-ILLATDGdfNVGIDDPKSIESMVKKQREsgVTLSTFGVGNSnYNEAMMVRIADVGN 370
Cdd:pfam13768  76 GGSDLLGALKEAVRAPASPGYIRhVLLLTDG--SPMQGETRVSDLISRAPGK--IRFFAYGLGAS-ISAPMLQLLAEASN 150


                  ....
gi 16130205   371 GNYS 374
Cdd:pfam13768 151 GTYE 154
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 213-384 7.59e-10

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: 58.98  E-value: 7.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 213 PASNLVFLIDTSGSM-ISDE----RLPLIQSSLKLLVKELREQDNIAIVTYAG------DSRIALP------SISGSHKA 275
Cdd:cd01456  19 LPPNVAIVLDNSGSMrEVDGggetRLDNAKAALDETANALPDGTRLGLWTFSGdgdnplDVRVLVPkgcltaPVNGFPSA 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 276 EINAAIDSLDAEGSTNGGAGLELAYQQATKGFIKGGINRILLATDGDFNVGIDDPKSIESMVKKQRES-GVTLSTFGVGN 354
Cdd:cd01456  99 QRSALDAALNSLQTPTGWTPLAAALAEAAAYVDPGRVNVVVLITDGEDTCGPDPCEVARELAKRRTPApPIKVNVIDFGG 178

                       170       180       190
                ....*....|....*....|....*....|
gi 16130205 355 SNYNEAMMvRIADVGNGNYSYidTLSEAQK 384
Cdd:cd01456 179 DADRAELE-AIAEATGGTYAY--NQSDLAS 205
VWA_2 pfam13519
von Willebrand factor type A domain;
217-301 8.03e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 56.15  E-value: 8.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205   217 LVFLIDTSGSMISDE----RLPLIQSSLKLLVKELREqDNIAIVTYAGDSRIALPsiSGSHKAEINAAIDSLDAE-GSTN 291
Cdd:pfam13519   1 LVFVLDTSGSMRNGDygptRLEAAKDAVLALLKSLPG-DRVGLVTFGDGPEVLIP--LTKDRAKILRALRRLEPKgGGTN 77

                          90
                  ....*....|
gi 16130205   292 GGAGLELAYQ 301
Cdd:pfam13519  78 LAAALQLARA 87
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 216-373 6.68e-09

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: 55.31  E-value: 6.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 216 NLVFLIDTSGSmISDERLPLIQSSLKLLVKEL---REQDNIAIVTYAGDSRIALPSISGSHKAEINAAIDSLDAEGS-TN 291
Cdd:cd01472   2 DIVFLVDGSES-IGLSNFNLVKDFVKRVVERLdigPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGgTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 292 GGAGLELAYQQATKGF--IKGGINRIL-LATDGdfnvGIDDpkSIESMVKKQRESGVtlSTFGVGNSNYNEAMMVRIADV 368
Cdd:cd01472  81 TGKALKYVRENLFTEAsgSREGVPKVLvVITDG----KSQD--DVEEPAVELKQAGI--EVFAVGVKNADEEELKQIASD 152


                ....*
gi 16130205 369 GNGNY 373
Cdd:cd01472 153 PKELY 157
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
218-367 1.45e-08

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 54.93  E-value: 1.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 218 VFLIDTSGSMiSDERLPLIQSSLKLLVKELR------EQDNIAIVTYAGDSRIALP--SISgshkaeiNAAIDSLDAEGS 289
Cdd:COG4245   9 YLLLDTSGSM-SGEPIEALNEGLQALIDELRqdpyalETVEVSVITFDGEAKVLLPltDLE-------DFQPPDLSASGG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 290 TNGGAGLELAYQQATKGFIKGGINR-------ILLATDG---DfnvgIDDPKSIESMVKKQRESGVTLSTFGVGNsNYNE 359
Cdd:COG4245  81 TPLGAALELLLDLIERRVQKYTAEGkgdwrpvVFLITDGeptD----SDWEAALQRLKDGEAAKKANIFAIGVGP-DADT 155


                ....*...
gi 16130205 360 AMMVRIAD 367
Cdd:COG4245 156 EVLKQLTD 163
PRK13685 PRK13685
hypothetical protein; Provisional
 218-393 1.11e-07

hypothetical protein; Provisional


Pssm-ID: 184242 [Multi-domain]  Cd Length: 326  Bit Score: 53.94  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205  218 VFLIDTSGSM----ISDERLPLIQSSLKLLVKELREQDNIAIVTYAGDSRIaLPSISGSHKAEINAaIDSLDAEGSTNGG 293
Cdd:PRK13685  92 MLVIDVSQSMratdVEPNRLAAAQEAAKQFADELTPGINLGLIAFAGTATV-LVSPTTNREATKNA-IDKLQLADRTATG 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205  294 AGLELAYQQ-ATKGFIKGGIN-----RILLATDGDFNVG--IDDPKSIESMVKKQRESGVTLSTFGVGNSN--------- 356
Cdd:PRK13685 170 EAIFTALQAiATVGAVIGGGDtpppaRIVLMSDGKETVPtnPDNPRGAYTAARTAKDQGVPISTISFGTPYgsveingqr 249

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 16130205  357 ----YNEAMMVRIADVGNGNYSYIDTLSEAQKVLNSEMRQM 393
Cdd:PRK13685 250 qpvpVDDESLKKIAQLSGGEFYTAASLEELRAVYATLQQQI 290
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 214-388 2.13e-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: 51.36  E-value: 2.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 214 ASNLVFLIDTSGSMISDErlPLIQSSLKLLVKEL-REQDNIAIVTYAGDSRIALPsISGSHKAEINAA--IDSLDAEGST 290
Cdd:cd01474   4 HFDLYFVLDKSGSVAANW--IEIYDFVEQLVDRFnSPGLRFSFITFSTRATKILP-LTDDSSAIIKGLevLKKVTPSGQT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 291 NGGAGLELAYQQATK----GFIKGGInrILLATDGDFNvgIDDPKSIESMVKKQRESGVTLSTFGVgnSNYNEAMMVRIA 366
Cdd:cd01474  81 YIHEGLENANEQIFNrnggGRETVSV--IIALTDGQLL--LNGHKYPEHEAKLSRKLGAIVYCVGV--TDFLKSQLINIA 154

                       170       180
                ....*....|....*....|..
gi 16130205 367 DVGNGNYSYIDTLSEAQKVLNS 388
Cdd:cd01474 155 DSKEYVFPVTSGFQALSGIIES 176
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 216-379 5.66e-07

VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex.


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 50.09  E-value: 5.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 216 NLVFLIDTSGSMiSDERLPLIQSSLKLLVKELREQDNIAIVTYAGDSRIALPSISG-------SHKAEINAAIDSLDAEG 288
Cdd:cd01463  15 DIVILLDVSGSM-TGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDtlvqattSNKKVLKEALDMLEAKG 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 289 STNGGAGLELAYQQATKGFIKGGINR-------ILLATDGdfnvGIDDPKSIESMVKKQR--ESGVTLSTFGVGNSNYNE 359
Cdd:cd01463  94 IANYTKALEFAFSLLLKNLQSNHSGSrsqcnqaIMLITDG----VPENYKEIFDKYNWDKnsEIPVRVFTYLIGREVTDR 169

                       170       180
                ....*....|....*....|
gi 16130205 360 AMMVRIADVGNGNYSYIDTL 379
Cdd:cd01463 170 REIQWMACENKGYYSHIQSL 189
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 218-355 1.08e-06

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: 48.88  E-value: 1.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 218 VFLIDTSGSMISdERLPLIQSSLKLLVKELReQD-------NIAIVTYAGDSRIALPSISGShkaeiNAAIDSLDAEGST 290
Cdd:cd01464   7 YLLLDTSGSMAG-EPIEALNQGLQMLQSELR-QDpyalesvEISVITFDSAARVIVPLTPLE-----SFQPPRLTASGGT 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130205 291 NGGAGLELA----------YQQATKGFIKggiNRILLATDGdfnVGIDDPKSIESMVKKQRESGVTLSTFGVGNS 355
Cdd:cd01464  80 SMGAALELAldcidrrvqrYRADQKGDWR---PWVFLLTDG---EPTDDLTAAIERIKEARDSKGRIVACAVGPK 148
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 216-374 2.74e-06

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 48.09  E-value: 2.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 216 NLVFLIDTSGSM-ISD----ERLPLIQSSLKLLVKElREQDNIAIVTYAGDSRIALPsISGSHK--AEINAAIDSLDAEG 288
Cdd:cd01467   4 DIMIALDVSGSMlAQDfvkpSRLEAAKEVLSDFIDR-RENDRIGLVVFAGAAFTQAP-LTLDREslKELLEDIKIGLAGQ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 289 STNGGAGLELAY----QQATKGFIkgginrILLATDGDFNVGIDDPKSIESMVKkqrESGVTLSTFGVGNSNY------- 357
Cdd:cd01467  82 GTAIGDAIGLAIkrlkNSEAKERV------IVLLTDGENNAGEIDPATAAELAK---NKGVRIYTIGVGKSGSgpkpdgs 152

                       170       180
                ....*....|....*....|
gi 16130205 358 ---NEAMMVRIADVGNGNYS 374
Cdd:cd01467 153 tilDEDSLVEIADKTGGRIF 172
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 216-361 2.82e-06

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 48.15  E-value: 2.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 216 NLVFLIDTSGSMISDERLPLIQSSLKLLVKEL---REQDNIAIVTYAGDS--RIALPSISGSHKAEINAAIDSLDAEGST 290
Cdd:cd01471   2 DLYLLVDGSGSIGYSNWVTHVVPFLHTFVQNLnisPDEINLYLVTFSTNAkeLIRLSSPNSTNKDLALNAIRALLSLYYP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 291 NGGAGLELAYQQATKGFIKGGINR------ILLATDGDFNvgiDDPKSIESmVKKQRESGVTLSTFGVG---NSNYNEAM 361
Cdd:cd01471  82 NGSTNTTSALLVVEKHLFDTRGNRenapqlVIIMTDGIPD---SKFRTLKE-ARKLRERGVIIAVLGVGqgvNHEENRSL 157
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 216-383 2.07e-05

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: 45.34  E-value: 2.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 216 NLV-FLIDTSGSMISDERLPLIQSS-LKLLVKELREQDNIAIVTYAGD-SRIALPSISGSHKAEinAAIDSLDAEGSTNG 292
Cdd:cd01451   1 NLViFVVDASGSMAARHRMAAAKGAvLSLLRDAYQRRDKVALIAFRGTeAEVLLPPTRSVELAK--RRLARLPTGGGTPL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 293 GAGLELAYQQATKGFIKGGINRIL-LATDGDFNVGIDDP----KSIESMVKKQRESGVTLSTfgvGNSNYNEAMMVRIAD 367
Cdd:cd01451  79 AAGLLAAYELAAEQARDPGQRPLIvVITDGRANVGPDPTadraLAAARKLRARGISALVIDT---EGRPVRRGLAKDLAR 155

                       170
                ....*....|....*.
gi 16130205 368 VGNGNYSYIDTLSEAQ 383
Cdd:cd01451 156 ALGGQYVRLPDLSADA 171
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 215-377 2.30e-05

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: 45.08  E-value: 2.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 215 SNLVFLIDTSGSMIsderlPLIQSSLKLLVKELREQDNI------AIVTYAGDSRIALPSISGSH--KAEINAAIDSLDA 286
Cdd:cd01476   1 LDLLFVLDSSGSVR-----GKFEKYKKYIERIVEGLEIGptatrvALITYSGRGRQRVRFNLPKHndGEELLEKVDNLRF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 287 -EGSTNGGAGLELAYQQATKGF-IKGGINRILLA-TDGDFNvgiDDPKSIESMVKkqreSGVTLSTFGVGNSNYNEAMMV 363
Cdd:cd01476  76 iGGTTATGAAIEVALQQLDPSEgRREGIPKVVVVlTDGRSH---DDPEKQARILR----AVPNIETFAVGTGDPGTVDTE 148

                       170
                ....*....|....*
gi 16130205 364 RIADV-GNGNYSYID 377
Cdd:cd01476 149 ELHSItGNEDHIFTD 163
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 207-392 9.71e-04

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: 41.52  E-value: 9.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205   207 RKSEELPASnLVFLIDTSGSMISDeRLPLIQSSLKLLVKELREQDNIAIVTYAGDSRIaLPSISGSHKaEINAAIDSLDA 286
Cdd:TIGR03436  47 RRETDLPLT-VGLVIDTSGSMRND-LDRARAAAIRFLKTVLRPNDRVFVVTFNTRLRL-LQDFTSDPR-LLEAALNRLKP 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205   287 ---------------EGSTNGGAGLELAYQQATKGFIKGGINR--ILLATDGDFNvgiddpksiESMVKKQR------ES 343
Cdd:TIGR03436 123 plrtdynssgafvrdGGGTALYDAITLAALEQLANALAGIPGRkaLIVISDGGDN---------RSRDTLERaidaaqRA 193

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130205   344 GVTL------------STFGVGNSNYNEAMMVRIADVGNGNYSYIDT--LSEAQKVLNSEMRQ 392
Cdd:TIGR03436 194 DVAIysidarglrapdLGAGAKAGLGGPEALERLAEETGGRAFYVNSndLDGAFAQIAEELRS 256
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 220-388 1.36e-03

calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out AC found a row in 1A13.INFO that was not parsed out EC found a row in 1A13.INFO that was not parsed out GA found a row in 1A13.INFO that was not parsed out SO found a row in 1A13.INFO that was not parsed out RH found a row in 1A13.INFO that was not parsed out EN found a row in 1A13.INFO that was not parsed out GS found a row in 1A13.INFO that was not parsed out AL found a row in 1A13.INFO that was not parsed out The Epithelial Chloride Channel (E-ClC) Family (TC 1.A.13) found a row in 1A13.INFO that was not parsed out found a row in 1A13.INFO that was not parsed out Mammals have multiple isoforms of epithelial chloride channel proteins. The first member of this family to be characterized was a respiratory epithelium, Ca found a row in 1A13.INFO that was not parsed out 2+-regulated, chloride channel protein isolated from bovine tracheal apical membranes. It was biochemically characterized as a 140 kDa complex. The purified found a row in 1A13.INFO that was not parsed out complex when reconstituted in a planar lipid bilayer behaved as an anion-selective channel. It was regulated by Ca 2+ via a calmodulin kinase II-dependent found a row in 1A13.INFO that was not parsed out mechanism. When the cRNA was injected into Xenopus oocytes, an outward rectifying, DIDS-sensitive, anion conductance was measured. A related gene, found a row in 1A13.INFO that was not parsed out Lu-ECAM, was cloned from the bovine aortic endothelial cell line, BAEC. It is expressed in the lung and spleen but not in the trachea. Homologues are found in found a row in 1A13.INFO that was not parsed out several mammals, and at least three paralogues(hCaCC-1-3) are present in humans, each with different tissue distributions. found a row in 1A13.INFO that was not parsed out [Transport and binding proteins, Anions]


Pssm-ID: 129946 [Multi-domain]  Cd Length: 863  Bit Score: 41.79  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205   220 LIDTSGSMISDERLPLIQSSLKLLVKELREQDN-IAIVTYAGDSRIALPSISGSHKAEINAAIDSL--DAEGSTNGGAGL 296
Cdd:TIGR00868 310 VLDKSGSMTVEDRLKRMNQAAKLFLLQTVEKGSwVGMVTFDSAAYIKNELIQITSSAERDALTANLptAASGGTSICSGL 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205   297 ELAYQQATKGFIKGGINRILLATDGDFNvgiddpkSIESMVKKQRESGVTLSTFGVGNSNYNEamMVRIADVGNGNYSYI 376
Cdd:TIGR00868 390 KAAFQVIKKSYQSTDGSEIVLLTDGEDN-------TISSCFEEVKQSGAIIHTIALGPSAAKE--LEELSDMTGGLRFYA 460

                         170
                  ....*....|..
gi 16130205   377 DTLSEAQKVLNS 388
Cdd:TIGR00868 461 SDQADNNGLIDA 472
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 217-376 1.40e-03

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 39.58  E-value: 1.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 217 LVFLIDTSGSmISDERLPLIQSSLKLLVKEL---REQDNIAIVTYAGDSRIALPSISGSHKAEINAAIDSLDAE-GSTNG 292
Cdd:cd01482   3 IVFLVDGSWS-IGRSNFNLVRSFLSSVVEAFeigPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKgGNTRT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 293 GAGLELAYQQ-------ATKGFIKGGInrilLATDGDFNvgiDDpksIESMVKKQRESGVTLSTFGVGNSNYNEamMVRI 365
Cdd:cd01482  82 GKALTHVREKnftpdagARPGVPKVVI----LITDGKSQ---DD---VELPARVLRNLGVNVFAVGVKDADESE--LKMI 149

                       170
                ....*....|.
gi 16130205 366 ADVGNGNYSYI 376
Cdd:cd01482 150 ASKPSETHVFN 160
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 216-366 1.88e-03

VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238758  Cd Length: 165  Bit Score: 39.23  E-value: 1.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 216 NLVFLIDTSGSMISDErLPLIQSSLKLLVKELR---EQDNIAIVTYAGDSRIALPSISGSHKAEINAAIDSLDAEGST-- 290
Cdd:cd01481   2 DIVFLIDGSDNVGSGN-FPAIRDFIERIVQSLDvgpDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSql 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 291 NGGAGLELAYQ----QATKGFIKGGINRILLATDGDFNvgiDDPKSIESMVKKQreSGVTlsTFGVGNSNYNEAMMVRIA 366
Cdd:cd01481  81 NTGSALDYVVKnlftKSAGSRIEEGVPQFLVLITGGKS---QDDVERPAVALKR--AGIV--PFAIGARNADLAELQQIA 153
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 216-353 2.31e-03

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


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 39.58  E-value: 2.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 216 NLVFLIDTSGSmISDERLPLIQSSLKLLVKELREQD---NIAIVTYAGDSRIALpSISGSHKAEINAAIDSL-----DAE 287
Cdd:cd01470   2 NIYIALDASDS-IGEEDFDEAKNAIKTLIEKISSYEvspRYEIISYASDPKEIV-SIRDFNSNDADDVIKRLedfnyDDH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130205 288 GS---TNGGAGL-----ELAYQQATKgfiKGGINR----ILLATDGDFNVG---------IDDPKSIESMVKKQRESGVT 346
Cdd:cd01470  80 GDktgTNTAAALkkvyeRMALEKVRN---KEAFNEtrhvIILFTDGKSNMGgsplptvdkIKNLVYKNNKSDNPREDYLD 156


                ....*..
gi 16130205 347 LSTFGVG 353
Cdd:cd01470 157 VYVFGVG 163
 
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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