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Conserved domains on  [gi|1622907606|ref|XP_014986192|]
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inter-alpha-trypsin inhibitor heavy chain H4 isoform X9 [Macaca mulatta]

Protein Classification

inter-alpha-trypsin inhibitor heavy chain H; VIT and vWA domain-containing protein( domain architecture ID 10652053)

inter-alpha-trypsin inhibitor heavy chain H may act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes| VIT (vault protein inter-alpha-trypsin) and vWA (von Willebrand factor type A) domain-containing protein

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 1.31e-77

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: 250.21  E-value: 1.31e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 271 MPKNVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEATQWRPSLVPASAENVNEARSFAAGIQALGGT 350
Cdd:cd01461     1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 351 NINEAMLVAVQLLDSSNqeerlpdGSVSLIILLTDGDptvgETNPRSIQKNVREAVSGRYSLFCLGFGFDVSYAFLEKLA 430
Cdd:cd01461    81 NMNDALEAALELLNSSP-------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                         170       180
                  ....*....|....*....|..
gi 1622907606 431 LDNGGLARRIHEDSDSALQLQD 452
Cdd:cd01461   150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
21-148 1.48e-66

Vault protein Inter-alpha-Trypsin domain;


:

Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 218.38  E-value: 1.48e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606   21 AIHQTTTAQKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRASTVQEATFQMELPKKAFITNFSMIIDGVTYPGIIKEKAK 100
Cdd:smart00609   3 GKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEV 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1622907606  101 AQAQYSAAVAKGKSAGLVKATGRNMEQFQVSVSVAPNAKITFELVYEE 148
Cdd:smart00609  83 AQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
 
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 1.31e-77

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: 250.21  E-value: 1.31e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 271 MPKNVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEATQWRPSLVPASAENVNEARSFAAGIQALGGT 350
Cdd:cd01461     1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 351 NINEAMLVAVQLLDSSNqeerlpdGSVSLIILLTDGDptvgETNPRSIQKNVREAVSGRYSLFCLGFGFDVSYAFLEKLA 430
Cdd:cd01461    81 NMNDALEAALELLNSSP-------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                         170       180
                  ....*....|....*....|..
gi 1622907606 431 LDNGGLARRIHEDSDSALQLQD 452
Cdd:cd01461   150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
21-148 1.48e-66

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 218.38  E-value: 1.48e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606   21 AIHQTTTAQKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRASTVQEATFQMELPKKAFITNFSMIIDGVTYPGIIKEKAK 100
Cdd:smart00609   3 GKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEV 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1622907606  101 AQAQYSAAVAKGKSAGLVKATGRNMEQFQVSVSVAPNAKITFELVYEE 148
Cdd:smart00609  83 AQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 244-471 6.95e-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: 169.51  E-value: 6.95e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 244 DRAVSGGTIQIENGYFVHYFAPEGLTT---MPKNVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEAT 320
Cdd:COG2304    60 TGRLAQSPWNPQTRLLLVGLQPPKAAAeerPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDAR 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 321 QWRPslvPASAENVNEARSFAAGIQALGGTNINEAMLVAVQLLDSSNQEERlpdgsVSLIILLTDGDPTVGETNPRSIQK 400
Cdd:COG2304   140 VLLP---PTPATDRAKILAAIDRLQAGGGTALGAGLELAYELARKHFIPGR-----VNRVILLTDGDANVGITDPEELLK 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622907606 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 4.05e-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: 4.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606  35 IYSLTVDSRVSSRFAHTVVTSRVVNRASTVQEATFQMELPKKAFITNFSMIIDGVTYPGIIKEKAKAQAQYSAAVAKGKS 114
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622907606 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 2.77e-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: 114.86  E-value: 2.77e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606  274 NVVFVIDKSGSMSGRKIQQTREALIKILDDLS---PRDQFNLIVFSTEATQWRPSLVPASAENVNEArsfaagIQAL--- 347
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSKDALLEA------LASLsyk 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606  348 --GGTNINEAMLVAVQLLDSSNQEERlpDGSVSLIILLTDGDPTVGETNprsIQKNVREAVSGRYSLFCLGFGFDVSYAF 425
Cdd:smart00327  75 lgGGTNLGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEE 149

                          170       180
                   ....*....|....*....|....*..
gi 1622907606  426 LEKLALDNGGlaRRIHEDSDSALQLQD 452
Cdd:smart00327 150 LKKLASAPGG--VYVFLPELLDLLIDL 174
VWA pfam00092
von Willebrand factor type A domain;
274-456 3.04e-28

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 111.98  E-value: 3.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 274 NVVFVIDKSGSMSGRKIQQTREALIKILDDLS---PRDQFNLIVFSTEATQWRPslvPASAENVNEARSFAAGIQALGG- 349
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVRTEFP---LNDYSSKEELLSAVDNLRYLGGg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 350 -TNINEAMLVAVQLLDSSNQEERlpDGSVSLIILLTDGDPTVGetnprSIQKNVREAVSGRYSLFCLGFGFDVSYAfLEK 428
Cdd:pfam00092  78 tTNTGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDG-----DPEEVARELKSAGVTVFAVGVGNADDEE-LRK 149

                         170       180
                  ....*....|....*....|....*...
gi 1622907606 429 LALDNGglARRIHEDSDSAlQLQDFYQE 456
Cdd:pfam00092 150 IASEPG--EGHVFTVSDFE-ALEDLQDQ 174
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 262-319 4.35e-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: 43.45  E-value: 4.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622907606 262 YFAPEglTTMPKNVVFVIDKSGSMSgRKIQQTREALIKILDD-LSPRDQFNLIVFSTEA 319
Cdd:TIGR03436  45 SFRRE--TDLPLTVGLVIDTSGSMR-NDLDRARAAAIRFLKTvLRPNDRVFVVTFNTRL 100
 
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 1.31e-77

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: 250.21  E-value: 1.31e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 271 MPKNVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEATQWRPSLVPASAENVNEARSFAAGIQALGGT 350
Cdd:cd01461     1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 351 NINEAMLVAVQLLDSSNqeerlpdGSVSLIILLTDGDptvgETNPRSIQKNVREAVSGRYSLFCLGFGFDVSYAFLEKLA 430
Cdd:cd01461    81 NMNDALEAALELLNSSP-------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                         170       180
                  ....*....|....*....|..
gi 1622907606 431 LDNGGLARRIHEDSDSALQLQD 452
Cdd:cd01461   150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
21-148 1.48e-66

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 218.38  E-value: 1.48e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606   21 AIHQTTTAQKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRASTVQEATFQMELPKKAFITNFSMIIDGVTYPGIIKEKAK 100
Cdd:smart00609   3 GKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEV 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1622907606  101 AQAQYSAAVAKGKSAGLVKATGRNMEQFQVSVSVAPNAKITFELVYEE 148
Cdd:smart00609  83 AQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 244-471 6.95e-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: 169.51  E-value: 6.95e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 244 DRAVSGGTIQIENGYFVHYFAPEGLTT---MPKNVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEAT 320
Cdd:COG2304    60 TGRLAQSPWNPQTRLLLVGLQPPKAAAeerPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDAR 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 321 QWRPslvPASAENVNEARSFAAGIQALGGTNINEAMLVAVQLLDSSNQEERlpdgsVSLIILLTDGDPTVGETNPRSIQK 400
Cdd:COG2304   140 VLLP---PTPATDRAKILAAIDRLQAGGGTALGAGLELAYELARKHFIPGR-----VNRVILLTDGDANVGITDPEELLK 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622907606 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 4.05e-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: 4.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606  35 IYSLTVDSRVSSRFAHTVVTSRVVNRASTVQEATFQMELPKKAFITNFSMIIDGVTYPGIIKEKAKAQAQYSAAVAKGKS 114
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622907606 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 2.77e-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: 114.86  E-value: 2.77e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606  274 NVVFVIDKSGSMSGRKIQQTREALIKILDDLS---PRDQFNLIVFSTEATQWRPSLVPASAENVNEArsfaagIQAL--- 347
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSKDALLEA------LASLsyk 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606  348 --GGTNINEAMLVAVQLLDSSNQEERlpDGSVSLIILLTDGDPTVGETNprsIQKNVREAVSGRYSLFCLGFGFDVSYAF 425
Cdd:smart00327  75 lgGGTNLGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEE 149

                          170       180
                   ....*....|....*....|....*..
gi 1622907606  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 1.80e-28

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: 115.42  E-value: 1.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 272 PKNVVFVIDKSGSMSGR-KIQQTREALIKILDDLSPRDQFNLIVFSTEATQwrpsLVPASAeNVNEARSFAAGIQALGGT 350
Cdd:COG1240    92 GRDVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEV----LLPLTR-DREALKRALDELPPGGGT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 351 NINEAMLVAVQLLDSSNQEERlpdgsvSLIILLTDGDPTVGETNPRSIqknVREAVSGRYSLFCLGFGFD-VSYAFLEKL 429
Cdd:COG1240   167 PLGDALALALELLKRADPARR------KVIVLLTDGRDNAGRIDPLEA---AELAAAAGIRIYTIGVGTEaVDEGLLREI 237

                         170       180
                  ....*....|....*....|....*....
gi 1622907606 430 ALDNGGLARRIhedsDSALQLQDFYQEVA 458
Cdd:COG1240   238 AEATGGRYFRA----DDLSELAAIYREID 262
VWA pfam00092
von Willebrand factor type A domain;
274-456 3.04e-28

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 111.98  E-value: 3.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 274 NVVFVIDKSGSMSGRKIQQTREALIKILDDLS---PRDQFNLIVFSTEATQWRPslvPASAENVNEARSFAAGIQALGG- 349
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVRTEFP---LNDYSSKEELLSAVDNLRYLGGg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 350 -TNINEAMLVAVQLLDSSNQEERlpDGSVSLIILLTDGDPTVGetnprSIQKNVREAVSGRYSLFCLGFGFDVSYAfLEK 428
Cdd:pfam00092  78 tTNTGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDG-----DPEEVARELKSAGVTVFAVGVGNADDEE-LRK 149

                         170       180
                  ....*....|....*....|....*...
gi 1622907606 429 LALDNGglARRIHEDSDSAlQLQDFYQE 456
Cdd:pfam00092 150 IASEPG--EGHVFTVSDFE-ALEDLQDQ 174
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 264-430 1.01e-27

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 113.24  E-value: 1.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 264 APEGLTTMPKNVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEATQwrPSLVPASAeNVNEARSFAAG 343
Cdd:COG2425   110 ASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE--DLPLTADD-GLEDAIEFLSG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 344 IQALGGTNINEAMLVAVQLLDSSNQEERlpdgsvsLIILLTDGDPTVGETnprSIQKNVREAVSGrYSLFCLGFGFDVSY 423
Cdd:COG2425   187 LFAGGGTDIAPALRAALELLEEPDYRNA-------DIVLITDGEAGVSPE---ELLREVRAKESG-VRLFTVAIGDAGNP 255


                  ....*..
gi 1622907606 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 1622907606 274 NVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEATqwrpSLVPASAenVNEARSFAAGIQAL---GGT 350
Cdd:cd01465     2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAE----TVLPATP--VRDKAAILAAIDRLtagGST 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 351 NINEAMLVAVQLLdssnQEERLPDGsVSLIILLTDGDPTVGETNPRSIQKNVREAVSGRYSLFCLGFGFDVSYAFLEKLA 430
Cdd:cd01465    76 AGGAGIQLGYQEA----QKHFVPGG-VNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAIA 150


                  ....*
gi 1622907606 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 5.80e-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: 107.65  E-value: 5.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 274 NVVFVIDKSGSMSGRKIQQTREALIKILDDLS---PRDQFNLIVFSTEATQWRPSLVPASAENVNEARSfAAGIQALGGT 350
Cdd:cd00198     2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSaspPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAID-ALKKGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 351 NINEAMLVAVQLLDSSNQeerlpDGSVSLIILLTDGDPTVGETNPRSIQKNVREAvsgRYSLFCLGFGFDVSYAFLEKLA 430
Cdd:cd00198    81 NIGAALRLALELLKSAKR-----PNARRVIILLTDGEPNDGPELLAEAARELRKL---GITVYTIGIGDDANEDELKEIA 152


                  ....*
gi 1622907606 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 3.01e-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: 88.22  E-value: 3.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 275 VVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEATQWRPsLVPASAENVNEARSFAAGIQALGGTNINE 354
Cdd:cd01466     3 LVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSP-LRRMTAKGKRSAKRVVDGLQAGGGTNVVG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 355 AMLVAVQLLdssnqEERLPDGSVSLIILLTDGDPTVGETNPRSIQknvreavsGRYSLFCLGFGFDVSYAFLEKLALDNG 434
Cdd:cd01466    82 GLKKALKVL-----GDRRQKNPVASIMLLSDGQDNHGAVVLRADN--------APIPIHTFGLGASHDPALLAFIAEITG 148


                  ..
gi 1622907606 435 GL 436
Cdd:cd01466   149 GT 150
VWA_3 pfam13768
von Willebrand factor type A domain;
273-438 1.67e-16

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 77.44  E-value: 1.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 273 KNVVFVIDKSGSMSGRKIQQtREALIKILDDLSPRDQFNLIVFSTEATQWRPSLVPASAENVNEARSFAAGIQA-LGGTN 351
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPpLGGSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 352 INEAMLVAVQLLDssnqeerlPDGSVSLIILLTDGDPTVGETnprSIQKNVREAVsGRYSLFCLGFGFDVSYAFLEKLAL 431
Cdd:pfam13768  80 LLGALKEAVRAPA--------SPGYIRHVLLLTDGSPMQGET---RVSDLISRAP-GKIRFFAYGLGASISAPMLQLLAE 147


                  ....*..
gi 1622907606 432 DNGGLAR 438
Cdd:pfam13768 148 ASNGTYE 154
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
274-459 1.83e-16

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 78.81  E-value: 1.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 274 NVVFVIDKSGSMSGRKIQQTREALIKILDDLSP------RDQFNLIVFSTEATQWRPsLVPASAENVNEarsfaagIQAL 347
Cdd:COG4245     7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQdpyaleTVEVSVITFDGEAKVLLP-LTDLEDFQPPD-------LSAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 348 GGTNINEAMLVAVQLLDSSNQEERlPDGSVS---LIILLTDGDPTVGETNpRSIQKNVREAVSGRYSLFCLGFGFDVSYA 424
Cdd:COG4245    79 GGTPLGAALELLLDLIERRVQKYT-AEGKGDwrpVVFLITDGEPTDSDWE-AALQRLKDGEAAKKANIFAIGVGPDADTE 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622907606 425 FLEKLALDNGGLarriheDSDSALQLQDFYQEVAN 459
Cdd:COG4245   157 VLKQLTDPVRAL------DALDGLDFREFFKWLSA 185
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 274-430 3.81e-12

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: 65.39  E-value: 3.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 274 NVVFVIDKSGSMSGRKIQQTREALIKILDDLSP---RDQFNLIVFSTEATQWRPSLVPASAENVNEArsfaagIQAL--- 347
Cdd:cd01450     2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIgpdKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKA------VKNLkyl 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 348 --GGTNINEAMLVAVQLLDSSNQEERlpdGSVSLIILLTDGDPTVGeTNPRSIQKNVREAvsgRYSLFCLGFGfDVSYAF 425
Cdd:cd01450    76 ggGGTNTGKALQYALEQLFSESNARE---NVPKVIIVLTDGRSDDG-GDPKEAAAKLKDE---GIKVFVVGVG-PADEEE 147


                  ....*
gi 1622907606 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 2.12e-11

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: 63.95  E-value: 2.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 270 TMPKNVVFVIDKSGSMSGRK---IQQTREAlikILDDLSPRDQFNLIVFSTEATQWRP----SLVPASAENVNEARSFAA 342
Cdd:cd01463    11 TSPKDIVILLDVSGSMTGQRlhlAKQTVSS---ILDTLSDNDFFNIITFSNEVNPVVPcfndTLVQATTSNKKVLKEALD 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622907606 343 GIQALGGTNINEAMLVAVQLLdsSNQEERLPDGSVS----LIILLTDGDP 388
Cdd:cd01463    88 MLEAKGIANYTKALEFAFSLL--LKNLQSNHSGSRSqcnqAIMLITDGVP 135
VWA_2 pfam13519
von Willebrand factor type A domain;
275-364 3.17e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 54.99  E-value: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 275 VVFVIDKSGSMSGRKIQQTR-EALIKILDDLS---PRDQFNLIVFSTEATQwrpsLVPASaENVNEARSFAAGIQAL-GG 349
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRlEAAKDAVLALLkslPGDRVGLVTFGDGPEV----LIPLT-KDRAKILRALRRLEPKgGG 75

                          90
                  ....*....|....*
gi 1622907606 350 TNINEAMLVAVQLLD 364
Cdd:pfam13519  76 TNLAAALQLARAALK 90
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 263-446 7.70e-09

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: 56.67  E-value: 7.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 263 FAPEGLTTMPK---NVVFVIDKSGSMS------GRKIQQTREALIKILDDLSPRDQFNLIVFSTEA---TQWRPSLVPAS 330
Cdd:cd01456     8 FALEPVETEPQlppNVAIVLDNSGSMRevdgggETRLDNAKAALDETANALPDGTRLGLWTFSGDGdnpLDVRVLVPKGC 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 331 -AENVN-----EARSFAAGIQAL----GGTNINEAMLVAVQLLDssnqeerlpDGSVSLIILLTDGDPTVGETNP---RS 397
Cdd:cd01456    88 lTAPVNgfpsaQRSALDAALNSLqtptGWTPLAAALAEAAAYVD---------PGRVNVVVLITDGEDTCGPDPCevaRE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1622907606 398 IQKnvREAVSGRYSLFCLGFGFDVSYAFLEKLALDNGGLARRIHEDSDS 446
Cdd:cd01456   159 LAK--RRTPAPPIKVNVIDFGGDADRAELEAIAEATGGTYAYNQSDLAS 205
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 273-386 1.09e-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: 55.05  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 273 KNVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQ-FNLIVFSTEatqWRPSLVPASAeNVNEARSFAAGIQALGGTN 351
Cdd:cd01462     1 GPVILLVDQSGSMYGAPEEVAKAVALALLRIALAENRdTYLILFDSE---FQTKIVDKTD-DLEEPVEFLSGVQLGGGTD 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1622907606 352 INEAMLVAVQLLdssnqEERLPDGSVslIILLTDG 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 7.74e-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: 53.05  E-value: 7.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 275 VVFVIDKSGSMSGR-KIQQTREALIKILDD-LSPRDQFNLIVF-STEATqwrpSLVPASaENVNEARSFAAGIQALGGTN 351
Cdd:cd01451     3 VIFVVDASGSMAARhRMAAAKGAVLSLLRDaYQRRDKVALIAFrGTEAE----VLLPPT-RSVELAKRRLARLPTGGGTP 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1622907606 352 INEAMLVAVQLLdssNQEERLPDGsVSLIILLTDGDPTVG 391
Cdd:cd01451    78 LAAGLLAAYELA---AEQARDPGQ-RPLIVVITDGRANVG 113
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 275-422 1.12e-07

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


Pssm-ID: 238731 [Multi-domain]  Cd Length: 174  Bit Score: 52.71  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 275 VVFVIDKSGSMSG-RKIQQTREALIKILDDL-SPRDQFNLIVFSTEAT-QWRPSLvpASAENVNEARSFAAG--IQAL-- 347
Cdd:cd01454     3 VTLLLDLSGSMRSdRRIDVAKKAAVLLAEALeACGVPHAILGFTTDAGgRERVRW--IKIKDFDESLHERARkrLAALsp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 348 -GGTNINEAMLVAVQLLDSSNQEERlpdgsvsLIILLTDGDP------TVGETNPRSIQKNVREAVSGRYSLFCLGFGFD 420
Cdd:cd01454    81 gGNTRDGAAIRHAAERLLARPEKRK-------ILLVISDGEPndldyyEGNVFATEDALRAVIEARKLGIEVFGITIDRD 153


                  ..
gi 1622907606 421 VS 422
Cdd:cd01454   154 AT 155
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 274-425 1.81e-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: 51.95  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 274 NVVFVIDKSGSMSGRKIQQ------TREALIKILDDlSPRDQFNLIVFSTEA------TQWRPSLvpasAENVNEARSFA 341
Cdd:cd01467     4 DIMIALDVSGSMLAQDFVKpsrleaAKEVLSDFIDR-RENDRIGLVVFAGAAftqaplTLDRESL----KELLEDIKIGL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 342 AGiqalGGTNINEAMLVAVQLLDSSNQEERLpdgsvslIILLTDGDPTVGETNPRSI-----QKNVReavsgrysLFCLG 416
Cdd:cd01467    79 AG----QGTAIGDAIGLAIKRLKNSEAKERV-------IVLLTDGENNAGEIDPATAaelakNKGVR--------IYTIG 139


                  ....*....
gi 1622907606 417 FGFDVSYAF 425
Cdd:cd01467   140 VGKSGSGPK 148
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 275-389 3.45e-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: 51.19  E-value: 3.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 275 VVFVIDKSGSMSGRKIQQTREALIKILDDLSpRDQFNL-------IVFSTEATQWRPsLVPasAENVNEARSFAAGIQAL 347
Cdd:cd01464     6 IYLLLDTSGSMAGEPIEALNQGLQMLQSELR-QDPYALesveisvITFDSAARVIVP-LTP--LESFQPPRLTASGGTSM 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1622907606 348 gGTNINeamlvavQLLDSSNQEERLPDGSVS-----LIILLTDGDPT 389
Cdd:cd01464    82 -GAALE-------LALDCIDRRVQRYRADQKgdwrpWVFLLTDGEPT 120
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 273-386 1.12e-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: 46.62  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 273 KNVVFVIDKSGSMSGrKIQQTREALIKILDDL--SPR-DQFNLIVFSTEATQwrpsLVPASAENVNEARSFAAGIQAL-- 347
Cdd:cd01476     1 LDLLFVLDSSGSVRG-KFEKYKKYIERIVEGLeiGPTaTRVALITYSGRGRQ----RVRFNLPKHNDGEELLEKVDNLrf 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1622907606 348 --GGTNINEAMLVAVQLLDSSnqeERLPDGSVSLIILLTDG 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 4.71e-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: 45.36  E-value: 4.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 275 VVFVIDKSGSMSG----RKIQQTREALIKI---LDDlsprD-QFNLIVFSTEATQWRPSLVPASAENVNEARSFAAGIQA 346
Cdd:pfam10138   4 VGLVLDASGSMSGlyrrGTVQRVVERMLPVaaqLDD----DgELDVWLFGTRAARLPDVTLADLPGWVERLHLGRDRYRK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 347 LGGTNiNEAMLVAVQLLDSSNQEERLPdgsvSLIILLTDGDPtvgeTNPRSIQKNVREAVsgRYSLFC--LGFGfDVSYA 424
Cdd:pfam10138  80 LGGQN-NEPPVMEAVIDYYRKNPADLP----TLVLFITDGGV----TDNAAIERLLREAS--REPIFWqfVGIG-RSGYG 147

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622907606 425 FLEKL------ALDNGGL--ARRIHEDSDSAL 448
Cdd:pfam10138 148 FLEKLdtlrgrVVDNAGFfaLDDIDRVSDAEL 179
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 262-319 4.35e-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: 43.45  E-value: 4.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622907606 262 YFAPEglTTMPKNVVFVIDKSGSMSgRKIQQTREALIKILDD-LSPRDQFNLIVFSTEA 319
Cdd:TIGR03436  45 SFRRE--TDLPLTVGLVIDTSGSMR-NDLDRARAAAIRFLKTvLRPNDRVFVVTFNTRL 100
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 275-387 7.07e-04

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: 43.33  E-value: 7.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 275 VVFVIDKSGSMSG-----RKIQQTREALIKILDDLSprdQFNLIVFSTEATQwRPSLVPASAENVNEARSFAAGIQALGG 349
Cdd:TIGR00868 307 VCLVLDKSGSMTVedrlkRMNQAAKLFLLQTVEKGS---WVGMVTFDSAAYI-KNELIQITSSAERDALTANLPTAASGG 382

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622907606 350 TNINEAMLVAVQLLDSSNQEErlpDGSVslIILLTDGD 387
Cdd:TIGR00868 383 TSICSGLKAAFQVIKKSYQST---DGSE--IVLLTDGE 415
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 274-388 1.35e-03

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: 40.83  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622907606 274 NVVFVIDKSGSMSG----RKIQQTREALIKILDdLSPRD-QFNLIVFSTEA-TQWR----PSLVPASAENVneARSFAAG 343
Cdd:cd01471     2 DLYLLVDGSGSIGYsnwvTHVVPFLHTFVQNLN-ISPDEiNLYLVTFSTNAkELIRlsspNSTNKDLALNA--IRALLSL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1622907606 344 IQALGGTNINEAMLVAVQLLDSSnQEERlpDGSVSLIILLTDGDP 388
Cdd:cd01471    79 YYPNGSTNTTSALLVVEKHLFDT-RGNR--ENAPQLVIIMTDGIP 120
 
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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