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Conserved domains on  [gi|31542984|ref|NP_002209|]
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inter-alpha-trypsin inhibitor heavy chain H4 isoform 1 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 271-452 7.01e-79

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: 253.29  E-value: 7.01e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 271 MPKNVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEATQWRPSLVPASAENVNKARSFAAGIQALGGT 350
Cdd:cd01461   1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 351 NINDAMLMAVQLLDSSNqeerlpeGSVSLIILLTDGDptvgETNPRSIQNNVREAVSGRYSLFCLGFGFDVSYAFLEKLA 430
Cdd:cd01461  81 NMNDALEAALELLNSSP-------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                       170       180
                ....*....|....*....|..
gi 31542984 431 LDNGGLARRIHEDSDSALQLQD 452
Cdd:cd01461 150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
21-148 7.12e-68

Vault protein Inter-alpha-Trypsin domain;


:

Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 221.85  E-value: 7.12e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984     21 AIHQTTTAEKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRANTVQEATFQMELPKKAFITNFSMIIDGMTYPGIIKEKAE 100
Cdd:smart00609   3 GKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEV 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 31542984    101 AQAQYSAAVAKGKSAGLVKATGRNMEQFQVSVSVAPNAKITFELVYEE 148
Cdd:smart00609  83 AQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
ITI_HC_C super family cl46397
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 764-928 1.43e-03

Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal region of inter-alpha-trypsin inhibitor heavy chains. Inter-alpha-trypsin inhibitors are glycoproteins with a high inhibitory activity against trypsin, built up from different combinations of four polypeptides: bikunin and the three heavy chains that belong to this family (HC1, HC2, HC3). The heavy chains do not have any protease inhibitory properties but have the capacity to interact in vitro and in vivo with hyaluronic acid, which promotes the stability of the extra-cellular matrix. All family members contain the pfam00092 domain.


The actual alignment was detected with superfamily member pfam06668:

Pssm-ID: 480737  Cd Length: 189  Bit Score: 40.65  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   764 EQGVEVTGQYEREKAG----------FSWIEVTFKNPLVWVHASPEHVVVTRNRRSSAYKWKETLFSVMPGLKMTMDKTG 833
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPpgshkklrtyFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   834 LLLLSDPDKVTIgllfwdgrgegLRLLLR-----------------DTDRFSSHVGGTLGQFYQEV---LWGSPAASDDG 893
Cdd:pfam06668  81 NVTVTIGDGISF-----------VVLLHRvwkkhpyqvdhlgfyilNSKGLSPSVHGLLGQFLHEPeveVTDVRPGSDPE 149

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 31542984   894 RR--TLRVQGNDHSATRERRLDY-QEGPPGVEISCWSV 928
Cdd:pfam06668 150 KPdaTMKVKGHKLPVTRGWQKDYrGDRKHGTNVPCWFV 187
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 271-452 7.01e-79

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: 253.29  E-value: 7.01e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 271 MPKNVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEATQWRPSLVPASAENVNKARSFAAGIQALGGT 350
Cdd:cd01461   1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 351 NINDAMLMAVQLLDSSNqeerlpeGSVSLIILLTDGDptvgETNPRSIQNNVREAVSGRYSLFCLGFGFDVSYAFLEKLA 430
Cdd:cd01461  81 NMNDALEAALELLNSSP-------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                       170       180
                ....*....|....*....|..
gi 31542984 431 LDNGGLARRIHEDSDSALQLQD 452
Cdd:cd01461 150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
21-148 7.12e-68

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 221.85  E-value: 7.12e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984     21 AIHQTTTAEKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRANTVQEATFQMELPKKAFITNFSMIIDGMTYPGIIKEKAE 100
Cdd:smart00609   3 GKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEV 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 31542984    101 AQAQYSAAVAKGKSAGLVKATGRNMEQFQVSVSVAPNAKITFELVYEE 148
Cdd:smart00609  83 AQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 244-471 5.08e-47

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 169.90  E-value: 5.08e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 244 DRAISGGSIQIENGYFVHYFAPEGLTT---MPKNVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEAT 320
Cdd:COG2304  60 TGRLAQSPWNPQTRLLLVGLQPPKAAAeerPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDAR 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 321 QWRPslvPASAENVNKARSFAAGIQALGGTNINDAMLMAVQLLdssnqEERLPEGSVSLIILLTDGDPTVGETNPRSIQN 400
Cdd:COG2304 140 VLLP---PTPATDRAKILAAIDRLQAGGGTALGAGLELAYELA-----RKHFIPGRVNRVILLTDGDANVGITDPEELLK 211

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31542984 401 NVREAVSGRYSLFCLGFGFDVSYAFLEKLALDNGGLARRIHEDSDSALQLQDFYQEVANPLLTAVTFEYPS 471
Cdd:COG2304 212 LAEEAREEGITLTTLGVGSDYNEDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPL 282
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 35-146 3.56e-42

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


Pssm-ID: 462492 [Multi-domain]  Cd Length: 111  Bit Score: 149.17  E-value: 3.56e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984    35 IYSLTVDSRVSSRFAHTVVTSRVVNRANTVQEATFQMELPKKAFITNFSMIIDGMTYPGIIKEKAEAQAQYSAAVAKGKS 114
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 31542984   115 AGLVKATGrnMEQFQVSV-SVAPNAKITFELVY 146
Cdd:pfam08487  81 AGLLEQDT--PDVFTTSVgNIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 274-452 1.66e-29

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: 115.63  E-value: 1.66e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984    274 NVVFVIDKSGSMSGRKIQQTREALIKILDDLS---PRDQFNLIVFSTEATQWRPSLVPASAENVNKArsfaagIQAL--- 347
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSKDALLEA------LASLsyk 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984    348 --GGTNINDAMLMAVQLLDSSNQEERlpEGSVSLIILLTDGDPTVGETNPRSIqnnVREAVSGRYSLFCLGFGFDVSYAF 425
Cdd:smart00327  75 lgGGTNLGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDGPKDLLKA---AKELKRSGVKVFVVGVGNDVDEEE 149

                          170       180
                   ....*....|....*....|....*..
gi 31542984    426 LEKLALDNGGlaRRIHEDSDSALQLQD 452
Cdd:smart00327 150 LKKLASAPGG--VYVFLPELLDLLIDL 174
VWA pfam00092
von Willebrand factor type A domain;
274-456 8.73e-29

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 113.52  E-value: 8.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   274 NVVFVIDKSGSMSGRKIQQTREALIKILDDLS---PRDQFNLIVFSTEATQWRPSLVPASAENVNKArsfaagIQAL--- 347
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSA------VDNLryl 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   348 --GGTNINDAMLMAVQLLDSSNQEERlpEGSVSLIILLTDGDPTVGetnprSIQNNVREAVSGRYSLFCLGFGFDVSYAf 425
Cdd:pfam00092  75 ggGTTNTGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDG-----DPEEVARELKSAGVTVFAVGVGNADDEE- 146

                         170       180       190
                  ....*....|....*....|....*....|.
gi 31542984   426 LEKLALDNGglARRIHEDSDSAlQLQDFYQE 456
Cdd:pfam00092 147 LRKIASEPG--EGHVFTVSDFE-ALEDLQDQ 174
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 262-437 7.04e-06

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


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 48.84  E-value: 7.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   262 YFAPEglTTMPKNVVFVIDKSGSMSgRKIQQTREALIKILDD-LSPRDQFNLIVFSTEA----------TQWRPSLVPAS 330
Cdd:TIGR03436  45 SFRRE--TDLPLTVGLVIDTSGSMR-NDLDRARAAAIRFLKTvLRPNDRVFVVTFNTRLrllqdftsdpRLLEAALNRLK 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   331 AENVNKARSFAAGIQALGGTNINDAMLMAVqlLDSSNQEERLPEGSVSLIIlLTDG-----DPTVGETNPRSIQNNVreA 405
Cdd:TIGR03436 122 PPLRTDYNSSGAFVRDGGGTALYDAITLAA--LEQLANALAGIPGRKALIV-ISDGgdnrsRDTLERAIDAAQRADV--A 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 31542984   406 VsgrYSL-------FCLGFGFDVSYA---FLEKLALDNGGLA 437
Cdd:TIGR03436 197 I---YSIdarglraPDLGAGAKAGLGgpeALERLAEETGGRA 235
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 764-928 1.43e-03

Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal region of inter-alpha-trypsin inhibitor heavy chains. Inter-alpha-trypsin inhibitors are glycoproteins with a high inhibitory activity against trypsin, built up from different combinations of four polypeptides: bikunin and the three heavy chains that belong to this family (HC1, HC2, HC3). The heavy chains do not have any protease inhibitory properties but have the capacity to interact in vitro and in vivo with hyaluronic acid, which promotes the stability of the extra-cellular matrix. All family members contain the pfam00092 domain.


Pssm-ID: 461981  Cd Length: 189  Bit Score: 40.65  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   764 EQGVEVTGQYEREKAG----------FSWIEVTFKNPLVWVHASPEHVVVTRNRRSSAYKWKETLFSVMPGLKMTMDKTG 833
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPpgshkklrtyFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   834 LLLLSDPDKVTIgllfwdgrgegLRLLLR-----------------DTDRFSSHVGGTLGQFYQEV---LWGSPAASDDG 893
Cdd:pfam06668  81 NVTVTIGDGISF-----------VVLLHRvwkkhpyqvdhlgfyilNSKGLSPSVHGLLGQFLHEPeveVTDVRPGSDPE 149

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 31542984   894 RR--TLRVQGNDHSATRERRLDY-QEGPPGVEISCWSV 928
Cdd:pfam06668 150 KPdaTMKVKGHKLPVTRGWQKDYrGDRKHGTNVPCWFV 187
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 271-452 7.01e-79

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: 253.29  E-value: 7.01e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 271 MPKNVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEATQWRPSLVPASAENVNKARSFAAGIQALGGT 350
Cdd:cd01461   1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 351 NINDAMLMAVQLLDSSNqeerlpeGSVSLIILLTDGDptvgETNPRSIQNNVREAVSGRYSLFCLGFGFDVSYAFLEKLA 430
Cdd:cd01461  81 NMNDALEAALELLNSSP-------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                       170       180
                ....*....|....*....|..
gi 31542984 431 LDNGGLARRIHEDSDSALQLQD 452
Cdd:cd01461 150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
21-148 7.12e-68

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 221.85  E-value: 7.12e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984     21 AIHQTTTAEKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRANTVQEATFQMELPKKAFITNFSMIIDGMTYPGIIKEKAE 100
Cdd:smart00609   3 GKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEV 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 31542984    101 AQAQYSAAVAKGKSAGLVKATGRNMEQFQVSVSVAPNAKITFELVYEE 148
Cdd:smart00609  83 AQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 244-471 5.08e-47

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 169.90  E-value: 5.08e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 244 DRAISGGSIQIENGYFVHYFAPEGLTT---MPKNVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEAT 320
Cdd:COG2304  60 TGRLAQSPWNPQTRLLLVGLQPPKAAAeerPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDAR 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 321 QWRPslvPASAENVNKARSFAAGIQALGGTNINDAMLMAVQLLdssnqEERLPEGSVSLIILLTDGDPTVGETNPRSIQN 400
Cdd:COG2304 140 VLLP---PTPATDRAKILAAIDRLQAGGGTALGAGLELAYELA-----RKHFIPGRVNRVILLTDGDANVGITDPEELLK 211

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31542984 401 NVREAVSGRYSLFCLGFGFDVSYAFLEKLALDNGGLARRIHEDSDSALQLQDFYQEVANPLLTAVTFEYPS 471
Cdd:COG2304 212 LAEEAREEGITLTTLGVGSDYNEDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPL 282
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 35-146 3.56e-42

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


Pssm-ID: 462492 [Multi-domain]  Cd Length: 111  Bit Score: 149.17  E-value: 3.56e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984    35 IYSLTVDSRVSSRFAHTVVTSRVVNRANTVQEATFQMELPKKAFITNFSMIIDGMTYPGIIKEKAEAQAQYSAAVAKGKS 114
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 31542984   115 AGLVKATGrnMEQFQVSV-SVAPNAKITFELVY 146
Cdd:pfam08487  81 AGLLEQDT--PDVFTTSVgNIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 274-452 1.66e-29

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: 115.63  E-value: 1.66e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984    274 NVVFVIDKSGSMSGRKIQQTREALIKILDDLS---PRDQFNLIVFSTEATQWRPSLVPASAENVNKArsfaagIQAL--- 347
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSKDALLEA------LASLsyk 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984    348 --GGTNINDAMLMAVQLLDSSNQEERlpEGSVSLIILLTDGDPTVGETNPRSIqnnVREAVSGRYSLFCLGFGFDVSYAF 425
Cdd:smart00327  75 lgGGTNLGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDGPKDLLKA---AKELKRSGVKVFVVGVGNDVDEEE 149

                          170       180
                   ....*....|....*....|....*..
gi 31542984    426 LEKLALDNGGlaRRIHEDSDSALQLQD 452
Cdd:smart00327 150 LKKLASAPGG--VYVFLPELLDLLIDL 174
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 272-458 5.10e-29

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: 116.96  E-value: 5.10e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 272 PKNVVFVIDKSGSMSGR-KIQQTREALIKILDDLSPRDQFNLIVFSTEATQwrpsLVPASAeNVNKARSFAAGIQALGGT 350
Cdd:COG1240  92 GRDVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEV----LLPLTR-DREALKRALDELPPGGGT 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 351 NINDAMLMAVQLLDSSNQEERlpegsvSLIILLTDGDPTVGETNPRSIqnnVREAVSGRYSLFCLGFGFD-VSYAFLEKL 429
Cdd:COG1240 167 PLGDALALALELLKRADPARR------KVIVLLTDGRDNAGRIDPLEA---AELAAAAGIRIYTIGVGTEaVDEGLLREI 237

                       170       180
                ....*....|....*....|....*....
gi 31542984 430 ALDNGGLARRIhedsDSALQLQDFYQEVA 458
Cdd:COG1240 238 AEATGGRYFRA----DDLSELAAIYREID 262
VWA pfam00092
von Willebrand factor type A domain;
274-456 8.73e-29

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 113.52  E-value: 8.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   274 NVVFVIDKSGSMSGRKIQQTREALIKILDDLS---PRDQFNLIVFSTEATQWRPSLVPASAENVNKArsfaagIQAL--- 347
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSA------VDNLryl 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   348 --GGTNINDAMLMAVQLLDSSNQEERlpEGSVSLIILLTDGDPTVGetnprSIQNNVREAVSGRYSLFCLGFGFDVSYAf 425
Cdd:pfam00092  75 ggGTTNTGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDG-----DPEEVARELKSAGVTVFAVGVGNADDEE- 146

                         170       180       190
                  ....*....|....*....|....*....|.
gi 31542984   426 LEKLALDNGglARRIHEDSDSAlQLQDFYQE 456
Cdd:pfam00092 147 LRKIASEPG--EGHVFTVSDFE-ALEDLQDQ 174
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 264-430 7.84e-28

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 113.62  E-value: 7.84e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 264 APEGLTTMPKNVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEATQwrPSLVPASAeNVNKARSFAAG 343
Cdd:COG2425 110 ASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE--DLPLTADD-GLEDAIEFLSG 186

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 344 IQALGGTNINDAMLMAVQLLDSSNQEERlpegsvsLIILLTDGDPTVGETnprSIQNNVREAVSGrYSLFCLGFGFDVSY 423
Cdd:COG2425 187 LFAGGGTDIAPALRAALELLEEPDYRNA-------DIVLITDGEAGVSPE---ELLREVRAKESG-VRLFTVAIGDAGNP 255


                ....*..
gi 31542984 424 AFLEKLA 430
Cdd:COG2425 256 GLLEALA 262
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 274-435 1.88e-27

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: 109.67  E-value: 1.88e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 274 NVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEATqwrpSLVPASAENvNKARsFAAGIQAL---GGT 350
Cdd:cd01465   2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAE----TVLPATPVR-DKAA-ILAAIDRLtagGST 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 351 NINDAMLMAVQLLdssnQEERLPEGsVSLIILLTDGDPTVGETNPRSIQNNVREAVSGRYSLFCLGFGFDVSYAFLEKLA 430
Cdd:cd01465  76 AGGAGIQLGYQEA----QKHFVPGG-VNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAIA 150


                ....*
gi 31542984 431 LDNGG 435
Cdd:cd01465 151 DAGNG 155
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 274-435 4.55e-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: 4.55e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 274 NVVFVIDKSGSMSGRKIQQTREALIKILDDLS---PRDQFNLIVFSTEATQWRPSLVPASAENVNKARSfAAGIQALGGT 350
Cdd:cd00198   2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSaspPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAID-ALKKGLGGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 351 NINDAMLMAVQLLDSSNQeerlpEGSVSLIILLTDGDPTVGETNPRSIQNNVREAvsgRYSLFCLGFGFDVSYAFLEKLA 430
Cdd:cd00198  81 NIGAALRLALELLKSAKR-----PNARRVIILLTDGEPNDGPELLAEAARELRKL---GITVYTIGIGDDANEDELKEIA 152


                ....*
gi 31542984 431 LDNGG 435
Cdd:cd00198 153 DKTTG 157
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 275-436 4.56e-20

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: 87.83  E-value: 4.56e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 275 VVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEATQWRPsLVPASAENVNKARSFAAGIQALGGTNIND 354
Cdd:cd01466   3 LVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSP-LRRMTAKGKRSAKRVVDGLQAGGGTNVVG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 355 AMLMAVQLLdssnqEERLPEGSVSLIILLTDGDPTVGETNPRSIQnnvreavsGRYSLFCLGFGFDVSYAFLEKLALDNG 434
Cdd:cd01466  82 GLKKALKVL-----GDRRQKNPVASIMLLSDGQDNHGAVVLRADN--------APIPIHTFGLGASHDPALLAFIAEITG 148


                ..
gi 31542984 435 GL 436
Cdd:cd01466 149 GT 150
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
274-459 4.12e-17

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 80.74  E-value: 4.12e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 274 NVVFVIDKSGSMSGRKIQQTREALIKILDDLSP------RDQFNLIVFSTEATQWRPsLVPASAENVNKarsfaagIQAL 347
Cdd:COG4245   7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQdpyaleTVEVSVITFDGEAKVLLP-LTDLEDFQPPD-------LSAS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 348 GGTNINDAMLMAVQLLDSSNQEERlPEGSVS---LIILLTDGDPTVGETNP--RSIQNNVReavSGRYSLFCLGFGFDVS 422
Cdd:COG4245  79 GGTPLGAALELLLDLIERRVQKYT-AEGKGDwrpVVFLITDGEPTDSDWEAalQRLKDGEA---AKKANIFAIGVGPDAD 154

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 31542984 423 YAFLEKLALDNGGLarriheDSDSALQLQDFYQEVAN 459
Cdd:COG4245 155 TEVLKQLTDPVRAL------DALDGLDFREFFKWLSA 185
VWA_3 pfam13768
von Willebrand factor type A domain;
273-438 2.64e-15

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 73.97  E-value: 2.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   273 KNVVFVIDKSGSMSGRKIQQtREALIKILDDLSPRDQFNLIVFSTEATQWRPSLVPASAENVNKARSFAAGIQA-LGGTN 351
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPpLGGSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   352 INDAMLMAVQLLDssnqeerlPEGSVSLIILLTDGDPTVGETnprSIQNNVREAVsGRYSLFCLGFGFDVSYAFLEKLAL 431
Cdd:pfam13768  80 LLGALKEAVRAPA--------SPGYIRHVLLLTDGSPMQGET---RVSDLISRAP-GKIRFFAYGLGASISAPMLQLLAE 147


                  ....*..
gi 31542984   432 DNGGLAR 438
Cdd:pfam13768 148 ASNGTYE 154
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 274-430 3.54e-13

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: 68.09  E-value: 3.54e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 274 NVVFVIDKSGSMSGRKIQQTREALIKILDDLSP---RDQFNLIVFSTEATQWRPSLVPASAENVNKArsfaagIQAL--- 347
Cdd:cd01450   2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIgpdKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKA------VKNLkyl 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 348 --GGTNINDAMLMAVQLLDSSNQEErlpEGSVSLIILLTDGDPTVGeTNPRSIQNNVREAvsgRYSLFCLGFGfDVSYAF 425
Cdd:cd01450  76 ggGGTNTGKALQYALEQLFSESNAR---ENVPKVIIVLTDGRSDDG-GDPKEAAAKLKDE---GIKVFVVGVG-PADEEE 147


                ....*
gi 31542984 426 LEKLA 430
Cdd:cd01450 148 LREIA 152
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 270-388 1.07e-10

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: 61.64  E-value: 1.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 270 TMPKNVVFVIDKSGSMSGRK---IQQTREAlikILDDLSPRDQFNLIVFSTEATQWRP----SLVPASAENVNKARSFAA 342
Cdd:cd01463  11 TSPKDIVILLDVSGSMTGQRlhlAKQTVSS---ILDTLSDNDFFNIITFSNEVNPVVPcfndTLVQATTSNKKVLKEALD 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 31542984 343 GIQALGGTNINDAMLMAVQLL---DSSNQEERLPEGSvSLIILLTDGDP 388
Cdd:cd01463  88 MLEAKGIANYTKALEFAFSLLlknLQSNHSGSRSQCN-QAIMLITDGVP 135
VWA_2 pfam13519
von Willebrand factor type A domain;
275-364 7.43e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 56.92  E-value: 7.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   275 VVFVIDKSGSMSGRKIQQTR-EALIKILDDLS---PRDQFNLIVFSTEATQwrpsLVPASaENVNKARSFAAGIQAL-GG 349
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRlEAAKDAVLALLkslPGDRVGLVTFGDGPEV----LIPLT-KDRAKILRALRRLEPKgGG 75

                          90
                  ....*....|....*
gi 31542984   350 TNINDAMLMAVQLLD 364
Cdd:pfam13519  76 TNLAAALQLARAALK 90
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 273-386 1.63e-08

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: 54.66  E-value: 1.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 273 KNVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQ-FNLIVFSTEatqWRPSLVPASAeNVNKARSFAAGIQALGGTN 351
Cdd:cd01462   1 GPVILLVDQSGSMYGAPEEVAKAVALALLRIALAENRdTYLILFDSE---FQTKIVDKTD-DLEEPVEFLSGVQLGGGTD 76

                        90       100       110
                ....*....|....*....|....*....|....*
gi 31542984 352 INDAMLMAVQLLdssnqEERLPEGSVslIILLTDG 386
Cdd:cd01462  77 INKALRYALELI-----ERRDPRKAD--IVLITDG 104
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 275-391 2.55e-08

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


Pssm-ID: 238728 [Multi-domain]  Cd Length: 178  Bit Score: 54.59  E-value: 2.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 275 VVFVIDKSGSMSGR-KIQQTREALIKILDD-LSPRDQFNLIVF-STEATqwrpSLVPASaENVNKARSFAAGIQALGGTN 351
Cdd:cd01451   3 VIFVVDASGSMAARhRMAAAKGAVLSLLRDaYQRRDKVALIAFrGTEAE----VLLPPT-RSVELAKRRLARLPTGGGTP 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 31542984 352 INDAMLMAVQLLdssnQEERLPEGSVSLIILLTDGDPTVG 391
Cdd:cd01451  78 LAAGLLAAYELA----AEQARDPGQRPLIVVITDGRANVG 113
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 263-446 1.44e-07

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: 52.82  E-value: 1.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 263 FAPEGLTTMPK---NVVFVIDKSGSMS------GRKIQQTREALIKILDDLSPRDQFNLIVFSTEA---TQWRPSLVPAS 330
Cdd:cd01456   8 FALEPVETEPQlppNVAIVLDNSGSMRevdgggETRLDNAKAALDETANALPDGTRLGLWTFSGDGdnpLDVRVLVPKGC 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 331 -AENVN-----KARSFAAGIQAL----GGTNINDAMLMAVQLLDssnqeerlpEGSVSLIILLTDGDPTVGETNPRSIQN 400
Cdd:cd01456  88 lTAPVNgfpsaQRSALDAALNSLqtptGWTPLAAALAEAAAYVD---------PGRVNVVVLITDGEDTCGPDPCEVARE 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 31542984 401 NV-REAVSGRYSLFCLGFGFDVSYAFLEKLALDNGGLARRIHEDSDS 446
Cdd:cd01456 159 LAkRRTPAPPIKVNVIDFGGDADRAELEAIAEATGGTYAYNQSDLAS 205
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 274-425 5.53e-07

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: 50.79  E-value: 5.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 274 NVVFVIDKSGSMSGRKIQQ------TREALIKILDDlSPRDQFNLIVFSTEATqwrpSLVPASAENV---NKARSFAAGI 344
Cdd:cd01467   4 DIMIALDVSGSMLAQDFVKpsrleaAKEVLSDFIDR-RENDRIGLVVFAGAAF----TQAPLTLDREslkELLEDIKIGL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 345 qALGGTNINDAMLMAVQLLDSSNQEERLpegsvslIILLTDGDPTVGETNPRSIQN-----NVReavsgrysLFCLGFGF 419
Cdd:cd01467  79 -AGQGTAIGDAIGLAIKRLKNSEAKERV-------IVLLTDGENNAGEIDPATAAElaknkGVR--------IYTIGVGK 142


                ....*.
gi 31542984 420 DVSYAF 425
Cdd:cd01467 143 SGSGPK 148
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 275-389 7.29e-07

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: 50.42  E-value: 7.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 275 VVFVIDKSGSMSGRKIQQTREALIKILDDLSpRDQFNL-------IVFSTEATQWRPsLVPasAENVNKARSFAAGIQAL 347
Cdd:cd01464   6 IYLLLDTSGSMAGEPIEALNQGLQMLQSELR-QDPYALesveisvITFDSAARVIVP-LTP--LESFQPPRLTASGGTSM 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 31542984 348 gGTNINdamlmavQLLDSSNQEERLPEGSVS-----LIILLTDGDPT 389
Cdd:cd01464  82 -GAALE-------LALDCIDRRVQRYRADQKgdwrpWVFLLTDGEPT 120
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 275-422 4.68e-06

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: 47.71  E-value: 4.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 275 VVFVIDKSGSMSG-RKIQQTREALIKILDDL-SPRDQFNLIVFSTEAT-QWRPSLVPASAENVN---KARSFAAGIQALG 348
Cdd:cd01454   3 VTLLLDLSGSMRSdRRIDVAKKAAVLLAEALeACGVPHAILGFTTDAGgRERVRWIKIKDFDESlheRARKRLAALSPGG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 349 GTNINDAMLMAVQLLDSSNQEERlpegsvsLIILLTDGDP------TVGETNPRSIQNNVREAVSGRYSLFCLGFGFDVS 422
Cdd:cd01454  83 NTRDGAAIRHAAERLLARPEKRK-------ILLVISDGEPndldyyEGNVFATEDALRAVIEARKLGIEVFGITIDRDAT 155
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 262-437 7.04e-06

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


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 48.84  E-value: 7.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   262 YFAPEglTTMPKNVVFVIDKSGSMSgRKIQQTREALIKILDD-LSPRDQFNLIVFSTEA----------TQWRPSLVPAS 330
Cdd:TIGR03436  45 SFRRE--TDLPLTVGLVIDTSGSMR-NDLDRARAAAIRFLKTvLRPNDRVFVVTFNTRLrllqdftsdpRLLEAALNRLK 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   331 AENVNKARSFAAGIQALGGTNINDAMLMAVqlLDSSNQEERLPEGSVSLIIlLTDG-----DPTVGETNPRSIQNNVreA 405
Cdd:TIGR03436 122 PPLRTDYNSSGAFVRDGGGTALYDAITLAA--LEQLANALAGIPGRKALIV-ISDGgdnrsRDTLERAIDAAQRADV--A 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 31542984   406 VsgrYSL-------FCLGFGFDVSYA---FLEKLALDNGGLA 437
Cdd:TIGR03436 197 I---YSIdarglraPDLGAGAKAGLGgpeALERLAEETGGRA 235
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 273-386 4.02e-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: 4.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 273 KNVVFVIDKSGSMSGrKIQQTREALIKILDDL--SPR-DQFNLIVFSTEATQwrpsLVPASAENVNKARSFAAGIQAL-- 347
Cdd:cd01476   1 LDLLFVLDSSGSVRG-KFEKYKKYIERIVEGLeiGPTaTRVALITYSGRGRQ----RVRFNLPKHNDGEELLEKVDNLrf 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 31542984 348 --GGTNINDAMLMAVQLLDSSnqeERLPEGSVSLIILLTDG 386
Cdd:cd01476  76 igGTTATGAAIEVALQQLDPS---EGRREGIPKVVVVLTDG 113
vWA-TerF-like pfam10138
vWA found in TerF C terminus; vWA domain fused to TerD domain typified by the TerF protein. ...
 275-448 6.28e-05

vWA found in TerF C terminus; vWA domain fused to TerD domain typified by the TerF protein. Some times found as solos.


Pssm-ID: 401947 [Multi-domain]  Cd Length: 200  Bit Score: 44.97  E-value: 6.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   275 VVFVIDKSGSMSG----RKIQQTREALIKI---LDDlsprD-QFNLIVFSTEATQWRPSLVPASAENVNKARSFAAGIQA 346
Cdd:pfam10138   4 VGLVLDASGSMSGlyrrGTVQRVVERMLPVaaqLDD----DgELDVWLFGTRAARLPDVTLADLPGWVERLHLGRDRYRK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   347 LGGTNiNDAMLMAVQLLDSSNQEERLPegsvSLIILLTDGDPtvgeTNPRSIQNNVREAVsgRYSLFC--LGFGfDVSYA 424
Cdd:pfam10138  80 LGGQN-NEPPVMEAVIDYYRKNPADLP----TLVLFITDGGV----TDNAAIERLLREAS--REPIFWqfVGIG-RSGYG 147

                         170       180       190
                  ....*....|....*....|....*....|..
gi 31542984   425 FLEKL------ALDNGGL--ARRIHEDSDSAL 448
Cdd:pfam10138 148 FLEKLdtlrgrVVDNAGFfaLDDIDRVSDAEL 179
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 274-388 1.56e-04

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: 43.53  E-value: 1.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 274 NVVFVIDKSGSMSG----RKIQQTREALIKILDdLSPRD-QFNLIVFSTEA-TQWRPSLVPASaeNVNKARSFAAGIQAL 347
Cdd:cd01471   2 DLYLLVDGSGSIGYsnwvTHVVPFLHTFVQNLN-ISPDEiNLYLVTFSTNAkELIRLSSPNST--NKDLALNAIRALLSL 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 31542984 348 ----GGTNINDAMLMAVQLLDSSnQEERlpEGSVSLIILLTDGDP 388
Cdd:cd01471  79 yypnGSTNTTSALLVVEKHLFDT-RGNR--ENAPQLVIIMTDGIP 120
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 764-928 1.43e-03

Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal region of inter-alpha-trypsin inhibitor heavy chains. Inter-alpha-trypsin inhibitors are glycoproteins with a high inhibitory activity against trypsin, built up from different combinations of four polypeptides: bikunin and the three heavy chains that belong to this family (HC1, HC2, HC3). The heavy chains do not have any protease inhibitory properties but have the capacity to interact in vitro and in vivo with hyaluronic acid, which promotes the stability of the extra-cellular matrix. All family members contain the pfam00092 domain.


Pssm-ID: 461981  Cd Length: 189  Bit Score: 40.65  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   764 EQGVEVTGQYEREKAG----------FSWIEVTFKNPLVWVHASPEHVVVTRNRRSSAYKWKETLFSVMPGLKMTMDKTG 833
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPpgshkklrtyFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   834 LLLLSDPDKVTIgllfwdgrgegLRLLLR-----------------DTDRFSSHVGGTLGQFYQEV---LWGSPAASDDG 893
Cdd:pfam06668  81 NVTVTIGDGISF-----------VVLLHRvwkkhpyqvdhlgfyilNSKGLSPSVHGLLGQFLHEPeveVTDVRPGSDPE 149

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 31542984   894 RR--TLRVQGNDHSATRERRLDY-QEGPPGVEISCWSV 928
Cdd:pfam06668 150 KPdaTMKVKGHKLPVTRGWQKDYrGDRKHGTNVPCWFV 187
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 277-386 2.69e-03

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 39.80  E-value: 2.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 277 FVIDKSGSMSGR--KIQQTREALIKILddLSPRDQFNLIVFSTEATQWRPslVPASAENVNKARSFAAGIQALGGTNIND 354
Cdd:cd01474   9 FVLDKSGSVAANwiEIYDFVEQLVDRF--NSPGLRFSFITFSTRATKILP--LTDDSSAIIKGLEVLKKVTPSGQTYIHE 84

                        90       100       110
                ....*....|....*....|....*....|..
gi 31542984 355 AMLMAVQLLDSSNQEERLpegSVSLIILLTDG 386
Cdd:cd01474  85 GLENANEQIFNRNGGGRE---TVSVIIALTDG 113
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 275-387 3.43e-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: 41.41  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984   275 VVFVIDKSGSMSG-----RKIQQTREALIKILDDLSprdQFNLIVFSTEATQwRPSLVPASAENVNKARSFAAGIQALGG 349
Cdd:TIGR00868 307 VCLVLDKSGSMTVedrlkRMNQAAKLFLLQTVEKGS---WVGMVTFDSAAYI-KNELIQITSSAERDALTANLPTAASGG 382

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 31542984   350 TNINDAMLMAVQLLDSSNQEErlpegSVSLIILLTDGD 387
Cdd:TIGR00868 383 TSICSGLKAAFQVIKKSYQST-----DGSEIVLLTDGE 415
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 273-386 3.98e-03

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


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 39.13  E-value: 3.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 273 KNVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQfnlivfsteatQWRPSLVPASAE--------NVNKARSFAAGI 344
Cdd:cd01472   1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPD-----------GVRVGVVQYSDDprtefylnTYRSKDDVLEAV 69

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 31542984 345 QAL----GGTNINDAMLMAVQLLDSSnqEERLPEGSVSLIILLTDG 386
Cdd:cd01472  70 KNLryigGGTNTGKALKYVRENLFTE--ASGSREGVPKVLVVITDG 113
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 274-406 8.28e-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: 38.42  E-value: 8.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542984 274 NVVFVIDKSGSMSGRKIQQTREALIKILD-----DLSPRdqFNLIVFSTEATQWRpSLVPASAENVNKA----RSFAAGI 344
Cdd:cd01470   2 NIYIALDASDSIGEEDFDEAKNAIKTLIEkissyEVSPR--YEIISYASDPKEIV-SIRDFNSNDADDVikrlEDFNYDD 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31542984 345 QALG-GTNINDAMLM---AVQLLDSSNQEERLPEGSVslIILLTDGDPTVGeTNPRSIQNNVREAV 406
Cdd:cd01470  79 HGDKtGTNTAAALKKvyeRMALEKVRNKEAFNETRHV--IILFTDGKSNMG-GSPLPTVDKIKNLV 141
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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