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Conserved domains on  [gi|49355778|ref|NP_001001851|]
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inter-alpha-trypsin inhibitor heavy chain H5 isoform 3 precursor [Homo sapiens]

Protein Classification

VWA domain-containing protein( domain architecture ID 10553333)

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- ...
 292-473 4.53e-73

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: 234.03  E-value: 4.53e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 292 LPKNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVWKDHLISVTPDSIRDGKVYIHHMSPTGGT 371
Cdd:cd01461   1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 372 DINGALQRAIRLLNKyvahsgiGDRSVSLIVFLTDGKptvgETHTLKILNNTREAARGQVCIFTIGIGNDVDFRLLEKLS 451
Cdd:cd01461  81 NMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                       170       180
                ....*....|....*....|..
gi 49355778 452 LENCGLTRRVHEEEDAGSQLIG 473
Cdd:cd01461 150 REGRGIARRIYETDDIESQLLR 171
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 51-159 1.39e-28

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: 110.27  E-value: 1.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778    51 MTEFSVKSTIISRYAFTTVSCRMLNRASEDQDIEFQMQIPAAAFITNFTMLIGDKVYQGEITEREKKSGDRVKEKRNKTT 130
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 49355778   131 EENGEK-GTEIFRAS-AVIPSKDKAAFFLSY 159
Cdd:pfam08487  81 AGLLEQdTPDVFTTSvGNIPPGEKVTVELTY 111
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 292-473 4.53e-73

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: 234.03  E-value: 4.53e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 292 LPKNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVWKDHLISVTPDSIRDGKVYIHHMSPTGGT 371
Cdd:cd01461   1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 372 DINGALQRAIRLLNKyvahsgiGDRSVSLIVFLTDGKptvgETHTLKILNNTREAARGQVCIFTIGIGNDVDFRLLEKLS 451
Cdd:cd01461  81 NMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                       170       180
                ....*....|....*....|..
gi 49355778 452 LENCGLTRRVHEEEDAGSQLIG 473
Cdd:cd01461 150 REGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 277-492 8.83e-38

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 142.55  E-value: 8.83e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 277 NGYFVHYFAPKDLPP---LPKNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVwkdhLISVTP- 352
Cdd:COG2304  72 TRLLLVGLQPPKAAAeerPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV----LLPPTPa 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 353 DSIRDGKVYIHHMSPTGGTDINGALQRAIRLLNKYvahsGIGDRsVSLIVFLTDGKPTVGETHTLKILNNTREAARGQVC 432
Cdd:COG2304 148 TDRAKILAAIDRLQAGGGTALGAGLELAYELARKH----FIPGR-VNRVILLTDGDANVGITDPEELLKLAEEAREEGIT 222

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 433 IFTIGIGNDVDFRLLEKLSLENCGLTRRVHEEEDAGSQLIGFYDEIRTPLLSDIRIDYPP 492
Cdd:COG2304 223 LTTLGVGSDYNEDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPL 282
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 51-159 1.39e-28

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: 110.27  E-value: 1.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778    51 MTEFSVKSTIISRYAFTTVSCRMLNRASEDQDIEFQMQIPAAAFITNFTMLIGDKVYQGEITEREKKSGDRVKEKRNKTT 130
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 49355778   131 EENGEK-GTEIFRAS-AVIPSKDKAAFFLSY 159
Cdd:pfam08487  81 AGLLEQdTPDVFTTSvGNIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 295-457 5.25e-27

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: 107.93  E-value: 5.25e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778    295 NVVFVLDSSASMVGTKLRQTKDALFTILHDLR---PQDRFSIIGFSNRIKVWKDHLISVTPDSIRDgkvYIHHMSPT--G 369
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSKDALLE---ALASLSYKlgG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778    370 GTDINGALQRAIRLLNKYVAHSGIGDRSVslIVFLTDGKPTVGETHTLKILnntREAARGQVCIFTIGIGNDVDFRLLEK 449
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGSRRGAPKV--VILITDGESNDGPKDLLKAA---KELKRSGVKVFVVGVGNDVDEEELKK 152


                   ....*...
gi 49355778    450 LSLENCGL 457
Cdd:smart00327 153 LASAPGGV 160
VWA pfam00092
von Willebrand factor type A domain;
295-454 4.69e-20

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 88.10  E-value: 4.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778   295 NVVFVLDSSASMVGTKLRQTKDALFTILHDL---RPQDRFSIIGFSNRIKVWKDHLISVTPDSIRDgkvYIHHM--SPTG 369
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLS---AVDNLryLGGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778   370 GTDINGALQRAIRLLNKYVAHSGIGDRSVslIVFLTDGKPTVGEthtlkILNNTREAARGQVCIFTIGIGNDVDfRLLEK 449
Cdd:pfam00092  78 TTNTGKALKYALENLFSSAAGARPGAPKV--VVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNADD-EELRK 149


                  ....*
gi 49355778   450 LSLEN 454
Cdd:pfam00092 150 IASEP 154
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
55-161 1.40e-17

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 79.32  E-value: 1.40e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778     55 SVKSTIISRYAFTTVSCRMLNRASEDQDIEFQMQIPAAAFITNFTMLIGDKVYQGEITEREKK----SGDRVKEKRNKTT 130
Cdd:smart00609  21 KVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEVAqkqyEKAVSQGKTAGLV 100

                           90       100       110
                   ....*....|....*....|....*....|.
gi 49355778    131 EENGEKgTEIFRASAVIPSKDKAAFFLSYEE 161
Cdd:smart00609 101 RASGRS-MEQFTVSVNVAPGSKVTFELTYEE 130
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 292-446 1.41e-05

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: 47.69  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778   292 LPKNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNR----------IKVWKDHLISVTPDSIRDGKVY 361
Cdd:TIGR03436  52 LPLTVGLVIDTSGSMRNDLDRARAAAIRFLKTVLRPNDRVFVVTFNTRlrllqdftsdPRLLEAALNRLKPPLRTDYNSS 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778   362 IHHMSPTGGTdingALQRAIRL--LNKYVAH-SGIGDRSVsLIVFlTDGkptVGETHTLKILNNTREAARGQVCIFTIGI 438
Cdd:TIGR03436 132 GAFVRDGGGT----ALYDAITLaaLEQLANAlAGIPGRKA-LIVI-SDG---GDNRSRDTLERAIDAAQRADVAIYSIDA 202


                  ....*...
gi 49355778   439 GNDVDFRL 446
Cdd:TIGR03436 203 RGLRAPDL 210
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 292-473 4.53e-73

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: 234.03  E-value: 4.53e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 292 LPKNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVWKDHLISVTPDSIRDGKVYIHHMSPTGGT 371
Cdd:cd01461   1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 372 DINGALQRAIRLLNKyvahsgiGDRSVSLIVFLTDGKptvgETHTLKILNNTREAARGQVCIFTIGIGNDVDFRLLEKLS 451
Cdd:cd01461  81 NMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                       170       180
                ....*....|....*....|..
gi 49355778 452 LENCGLTRRVHEEEDAGSQLIG 473
Cdd:cd01461 150 REGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 277-492 8.83e-38

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 142.55  E-value: 8.83e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 277 NGYFVHYFAPKDLPP---LPKNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVwkdhLISVTP- 352
Cdd:COG2304  72 TRLLLVGLQPPKAAAeerPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV----LLPPTPa 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 353 DSIRDGKVYIHHMSPTGGTDINGALQRAIRLLNKYvahsGIGDRsVSLIVFLTDGKPTVGETHTLKILNNTREAARGQVC 432
Cdd:COG2304 148 TDRAKILAAIDRLQAGGGTALGAGLELAYELARKH----FIPGR-VNRVILLTDGDANVGITDPEELLKLAEEAREEGIT 222

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 433 IFTIGIGNDVDFRLLEKLSLENCGLTRRVHEEEDAGSQLIGFYDEIRTPLLSDIRIDYPP 492
Cdd:COG2304 223 LTTLGVGSDYNEDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPL 282
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 51-159 1.39e-28

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: 110.27  E-value: 1.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778    51 MTEFSVKSTIISRYAFTTVSCRMLNRASEDQDIEFQMQIPAAAFITNFTMLIGDKVYQGEITEREKKSGDRVKEKRNKTT 130
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 49355778   131 EENGEK-GTEIFRAS-AVIPSKDKAAFFLSY 159
Cdd:pfam08487  81 AGLLEQdTPDVFTTSvGNIPPGEKVTVELTY 111
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 290-451 3.31e-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: 111.31  E-value: 3.31e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 290 PPLPKNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVwkdHLISVTPDSIRDGKVYIHHMSPTG 369
Cdd:COG2425 115 PLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE---DLPLTADDGLEDAIEFLSGLFAGG 191

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 370 GTDINGALQRAIRLLNKYVAHSGIgdrsvslIVFLTDGKPTVGETHTLKILNntreAARGQVCIFTIGIGNDVDFRLLEK 449
Cdd:COG2425 192 GTDIAPALRAALELLEEPDYRNAD-------IVLITDGEAGVSPEELLREVR----AKESGVRLFTVAIGDAGNPGLLEA 260


                ..
gi 49355778 450 LS 451
Cdd:COG2425 261 LA 262
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 295-457 5.25e-27

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: 107.93  E-value: 5.25e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778    295 NVVFVLDSSASMVGTKLRQTKDALFTILHDLR---PQDRFSIIGFSNRIKVWKDHLISVTPDSIRDgkvYIHHMSPT--G 369
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSKDALLE---ALASLSYKlgG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778    370 GTDINGALQRAIRLLNKYVAHSGIGDRSVslIVFLTDGKPTVGETHTLKILnntREAARGQVCIFTIGIGNDVDFRLLEK 449
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGSRRGAPKV--VILITDGESNDGPKDLLKAA---KELKRSGVKVFVVGVGNDVDEEELKK 152


                   ....*...
gi 49355778    450 LSLENCGL 457
Cdd:smart00327 153 LASAPGGV 160
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 290-451 1.26e-25

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: 106.56  E-value: 1.26e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 290 PPLPKNVVFVLDSSASMVG-TKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVwkdhLISVTPDsIRDGKVYIHHMSPT 368
Cdd:COG1240  89 PQRGRDVVLVVDASGSMAAeNRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEV----LLPLTRD-REALKRALDELPPG 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 369 GGTDINGALQRAIRLLNKYvahsgiGDRSVSLIVFLTDGKPTVGETHTLKILnntREAARGQVCIFTIGIGND-VDFRLL 447
Cdd:COG1240 164 GGTPLGDALALALELLKRA------DPARRKVIVLLTDGRDNAGRIDPLEAA---ELAAAAGIRIYTIGVGTEaVDEGLL 234


                ....
gi 49355778 448 EKLS 451
Cdd:COG1240 235 REIA 238
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 295-451 2.27e-23

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: 97.25  E-value: 2.27e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 295 NVVFVLDSSASMVGTKLRQTKDALFTILHDL---RPQDRFSIIGFSNRIKVWKDHLISVTPDSIRDGKVYIHHmSPTGGT 371
Cdd:cd00198   2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLsasPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK-GLGGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 372 DINGALQRAIRLLNKYvahsgIGDRSVSLIVFLTDGKPTVGETHTLKILNNTREAargQVCIFTIGIGNDVDFRLLEKLS 451
Cdd:cd00198  81 NIGAALRLALELLKSA-----KRPNARRVIILLTDGEPNDGPELLAEAARELRKL---GITVYTIGIGDDANEDELKEIA 152
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 295-450 7.25e-22

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: 93.11  E-value: 7.25e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 295 NVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVwkdhLISVTP----DSIRDGkvyIHHMSPTGG 370
Cdd:cd01465   2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAET----VLPATPvrdkAAILAA---IDRLTAGGS 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 371 TDINGALQRAIRLLNKyvahsGIGDRSVSLIVFLTDGKPTVGETHTLKILNNTREAARGQVCIFTIGIGNDVDFRLLEKL 450
Cdd:cd01465  75 TAGGAGIQLGYQEAQK-----HFVPGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAI 149
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
290-451 1.01e-21

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 93.45  E-value: 1.01e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 290 PPLPknVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQD------RFSIIGFSNRIKVwkdhlisVTPDSIRDgKVYIH 363
Cdd:COG4245   4 RRLP--VYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPyaletvEVSVITFDGEAKV-------LLPLTDLE-DFQPP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 364 HMSPTGGTDINGALQRAIRLLNKYVAHS---GIGDRSVsLIVFLTDGKPTVGETHT-LKILNNTREAARGQvcIFTIGIG 439
Cdd:COG4245  74 DLSASGGTPLGAALELLLDLIERRVQKYtaeGKGDWRP-VVFLITDGEPTDSDWEAaLQRLKDGEAAKKAN--IFAIGVG 150

                       170
                ....*....|..
gi 49355778 440 NDVDFRLLEKLS 451
Cdd:COG4245 151 PDADTEVLKQLT 162
VWA pfam00092
von Willebrand factor type A domain;
295-454 4.69e-20

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 88.10  E-value: 4.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778   295 NVVFVLDSSASMVGTKLRQTKDALFTILHDL---RPQDRFSIIGFSNRIKVWKDHLISVTPDSIRDgkvYIHHM--SPTG 369
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLS---AVDNLryLGGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778   370 GTDINGALQRAIRLLNKYVAHSGIGDRSVslIVFLTDGKPTVGEthtlkILNNTREAARGQVCIFTIGIGNDVDfRLLEK 449
Cdd:pfam00092  78 TTNTGKALKYALENLFSSAAGARPGAPKV--VVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNADD-EELRK 149


                  ....*
gi 49355778   450 LSLEN 454
Cdd:pfam00092 150 IASEP 154
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
55-161 1.40e-17

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 79.32  E-value: 1.40e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778     55 SVKSTIISRYAFTTVSCRMLNRASEDQDIEFQMQIPAAAFITNFTMLIGDKVYQGEITEREKK----SGDRVKEKRNKTT 130
Cdd:smart00609  21 KVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEVAqkqyEKAVSQGKTAGLV 100

                           90       100       110
                   ....*....|....*....|....*....|.
gi 49355778    131 EENGEKgTEIFRASAVIPSKDKAAFFLSYEE 161
Cdd:smart00609 101 RASGRS-MEQFTVSVNVAPGSKVTFELTYEE 130
VWA_3 pfam13768
von Willebrand factor type A domain;
294-451 1.03e-16

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 77.82  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778   294 KNVVFVLDSSASMVGTKLRQtKDALFTILHDLRPQDRFSIIGFSNRIKVWKDHLISVTPDSIRDGKVYIHHMSPT-GGTD 372
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPlGGSD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 49355778   373 INGALQRAIRLLnkyvAHSGIgdrsVSLIVFLTDGKPTVGETHTLKILnntrEAARGQVCIFTIGIGNDVDFRLLEKLS 451
Cdd:pfam13768  80 LLGALKEAVRAP----ASPGY----IRHVLLLTDGSPMQGETRVSDLI----SRAPGKIRFFAYGLGASISAPMLQLLA 146
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 293-456 2.04e-13

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: 69.35  E-value: 2.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 293 PKNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIK----VWKDHLISVTPDSIRDGKVYIHHMSPT 368
Cdd:cd01463  13 PKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNpvvpCFNDTLVQATTSNKKVLKEALDMLEAK 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 369 GGTDINGALQRAIRLLNKYVAHSGIGDRSV--SLIVFLTDGKPtvgETHTlKILN--NTREAARGQVCIFTIGIGNDV-D 443
Cdd:cd01463  93 GIANYTKALEFAFSLLLKNLQSNHSGSRSQcnQAIMLITDGVP---ENYK-EIFDkyNWDKNSEIPVRVFTYLIGREVtD 168

                       170
                ....*....|...
gi 49355778 444 FRLLEKLSLENCG 456
Cdd:cd01463 169 RREIQWMACENKG 181
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 296-451 3.26e-13

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: 67.80  E-value: 3.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 296 VVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVWKDhLISVTPDSIRDGKVYIHHMSPTGGTDING 375
Cdd:cd01466   3 LVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSP-LRRMTAKGKRSAKRVVDGLQAGGGTNVVG 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 49355778 376 ALQRAIRLLNKyvahSGIGDRSVSLIVfLTDGKPTVGETHTlkilnntrEAARGQVCIFTIGIGNDVDFRLLEKLS 451
Cdd:cd01466  82 GLKKALKVLGD----RRQKNPVASIML-LSDGQDNHGAVVL--------RADNAPIPIHTFGLGASHDPALLAFIA 144
VWA_2 pfam13519
von Willebrand factor type A domain;
296-386 2.34e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 58.07  E-value: 2.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778   296 VVFVLDSSASM-----VGTKLRQTKDALFTILHDLrPQDRFSIIGFSNRIKVwkdhLISVTpDSIRDGKVYIHHMSPT-G 369
Cdd:pfam13519   1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSL-PGDRVGLVTFGDGPEV----LIPLT-KDRAKILRALRRLEPKgG 74

                          90
                  ....*....|....*..
gi 49355778   370 GTDINGALQRAIRLLNK 386
Cdd:pfam13519  75 GTNLAAALQLARAALKH 91
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 295-451 6.09e-10

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: 58.46  E-value: 6.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 295 NVVFVLDSSASMVGTKLRQTKDALFTILHDLRP---QDRFSIIGFSNRIKVW--------KDHLISvtpdSIRDgkvyIH 363
Cdd:cd01450   2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIgpdKTRVGLVQYSDDVRVEfslndyksKDDLLK----AVKN----LK 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 364 HMSPtGGTDINGALQRAIRLLNKyvaHSGIGDRSVSLIVFLTDGKPTVGEthtlKILNNTREAARGQVCIFTIGIGnDVD 443
Cdd:cd01450  74 YLGG-GGTNTGKALQYALEQLFS---ESNARENVPKVIIVLTDGRSDDGG----DPKEAAAKLKDEGIKVFVVGVG-PAD 144


                ....*...
gi 49355778 444 FRLLEKLS 451
Cdd:cd01450 145 EEELREIA 152
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 292-451 8.23e-10

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: 58.51  E-value: 8.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 292 LPknVVFVLDSSASMVGTKLRQTKDALFTILHDLRpQDRF-------SIIGFSNRIKVWKDhLISVTpdsirdgKVYIHH 364
Cdd:cd01464   4 LP--IYLLLDTSGSMAGEPIEALNQGLQMLQSELR-QDPYalesveiSVITFDSAARVIVP-LTPLE-------SFQPPR 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 365 MSPTGGTDINGALQRAIRLLN----KYVAhSGIGDRSvSLIVFLTDGKPTVGETHTLKILnntREAARGQVCIFTIGIGN 440
Cdd:cd01464  73 LTASGGTSMGAALELALDCIDrrvqRYRA-DQKGDWR-PWVFLLTDGEPTDDLTAAIERI---KEARDSKGRIVACAVGP 147

                       170
                ....*....|.
gi 49355778 441 DVDFRLLEKLS 451
Cdd:cd01464 148 KADLDTLKQIT 158
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 296-412 4.35e-06

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: 47.66  E-value: 4.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 296 VVFVLDSSASM-VGTKLRQTKDALFTILHD-LRPQDRFSIIGFSNRIkvwKDHLISVTpDSIRDGKVYIHHMSPTGGTDI 373
Cdd:cd01451   3 VIFVVDASGSMaARHRMAAAKGAVLSLLRDaYQRRDKVALIAFRGTE---AEVLLPPT-RSVELAKRRLARLPTGGGTPL 78

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 49355778 374 NGALQRAIRLLNKYVAHSGIgdrsVSLIVFLTDGKPTVG 412
Cdd:cd01451  79 AAGLLAAYELAAEQARDPGQ----RPLIVVITDGRANVG 113
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 296-442 1.05e-05

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: 46.55  E-value: 1.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 296 VVFVLDSSASMVGT-KLRQTKDALFtILHD--LRPQDRFSIIGFSNRIKV--WKDHLISVTPDSIRDGKVY--IHHMSPT 368
Cdd:cd01454   3 VTLLLDLSGSMRSDrRIDVAKKAAV-LLAEalEACGVPHAILGFTTDAGGreRVRWIKIKDFDESLHERARkrLAALSPG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 369 GGTDINGALQRAIRLLNKYVAHSGIgdrsvsLIVFlTDGKPTVGETHTLKI------LNNTREAARGQVCIFTIGIGNDV 442
Cdd:cd01454  82 GNTRDGAAIRHAAERLLARPEKRKI------LLVI-SDGEPNDLDYYEGNVfatedaLRAVIEARKLGIEVFGITIDRDA 154
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 292-446 1.41e-05

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: 47.69  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778   292 LPKNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNR----------IKVWKDHLISVTPDSIRDGKVY 361
Cdd:TIGR03436  52 LPLTVGLVIDTSGSMRNDLDRARAAAIRFLKTVLRPNDRVFVVTFNTRlrllqdftsdPRLLEAALNRLKPPLRTDYNSS 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778   362 IHHMSPTGGTdingALQRAIRL--LNKYVAH-SGIGDRSVsLIVFlTDGkptVGETHTLKILNNTREAARGQVCIFTIGI 438
Cdd:TIGR03436 132 GAFVRDGGGT----ALYDAITLaaLEQLANAlAGIPGRKA-LIVI-SDG---GDNRSRDTLERAIDAAQRADVAIYSIDA 202


                  ....*...
gi 49355778   439 GNDVDFRL 446
Cdd:TIGR03436 203 RGLRAPDL 210
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 290-443 1.02e-04

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: 43.96  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 290 PPLPKNVVFVLDSSASMV------GTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVWKDhlISVT-PDSIRDGKVYI 362
Cdd:cd01456  17 PQLPPNVAIVLDNSGSMRevdgggETRLDNAKAALDETANALPDGTRLGLWTFSGDGDNPLD--VRVLvPKGCLTAPVNG 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 363 HHM--------------SPTGGTDINGALQRAirllnkyvAHSgIGDRSVSLIVFLTDGKPTVGETH--TLKILNNTREA 426
Cdd:cd01456  95 FPSaqrsaldaalnslqTPTGWTPLAAALAEA--------AAY-VDPGRVNVVVLITDGEDTCGPDPceVARELAKRRTP 165

                       170
                ....*....|....*..
gi 49355778 427 ARGqVCIFTIGIGNDVD 443
Cdd:cd01456 166 APP-IKVNVIDFGGDAD 181
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 294-442 1.24e-04

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: 42.99  E-value: 1.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 294 KNVVFVLDSSASMVGTKLRQTKDALFTILHDL--RPQD-RFSIIGFSNRIKVWKDHLISVTPDSIRDGkvyIHHMSPTGG 370
Cdd:cd01472   1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLdiGPDGvRVGVVQYSDDPRTEFYLNTYRSKDDVLEA---VKNLRYIGG 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49355778 371 -TDINGALQRAIRLLnkYVAHSGIGDRSVSLIVFLTDGKPTVGethtlkILNNTREAARGQVCIFTIGIGNDV 442
Cdd:cd01472  78 gTNTGKALKYVRENL--FTEASGSREGVPKVLVVITDGKSQDD------VEEPAVELKQAGIEVFAVGVKNAD 142
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 298-438 3.04e-04

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 42.50  E-value: 3.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 298 FVLDSSASmVGTKLRQTKDALFTILHDL-RPQDRFSIIGFSNRIKVwkdhLISVTPDS--IRDGKVYIHHMSPTGGTDIN 374
Cdd:cd01474   9 FVLDKSGS-VAANWIEIYDFVEQLVDRFnSPGLRFSFITFSTRATK----ILPLTDDSsaIIKGLEVLKKVTPSGQTYIH 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 49355778 375 GALQRAirllNKYVAHSGIGDR-SVSLIVFLTDgkptvGETHTLKILNNTREAARGQ---VCIFTIGI 438
Cdd:cd01474  84 EGLENA----NEQIFNRNGGGReTVSVIIALTD-----GQLLLNGHKYPEHEAKLSRklgAIVYCVGV 142
YeaD2 COG1721
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];
295-406 2.63e-03

Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];


Pssm-ID: 441327 [Multi-domain]  Cd Length: 287  Bit Score: 40.58  E-value: 2.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 295 NVVFVLDSSASM-----VGTKLRQTKDALFTILHD-LRPQDRFSIIGFSNRIKVWkdhlisVTPDSirdGKVYIHHM--- 365
Cdd:COG1721 149 TVVLLLDTSASMrfgsgGPSKLDLAVEAAASLAYLaLRQGDRVGLLTFGDRVRRY------LPPRR---GRRHLLRLlea 219

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 49355778 366 ----SPTGGTDINGALQRAIRLLnkyvahsgigdRSVSLIVFLTD 406
Cdd:COG1721 220 larlEPAGETDLAAALRRLARRL-----------PRRSLVVLISD 253
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 294-441 8.13e-03

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


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 37.71  E-value: 8.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 294 KNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDR-FSIIGFSNRIKVWkdhlISVTPDSIRDGKVYIHHMSPTGGTD 372
Cdd:cd01462   1 GPVILLVDQSGSMYGAPEEVAKAVALALLRIALAENRdTYLILFDSEFQTK----IVDKTDDLEEPVEFLSGVQLGGGTD 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355778 373 INGALQRAIRLLNKYvahsgigDRSVSLIVFLTDG-KPTVGEthtlKILNNTREAARGQVCIFTIGIGND 441
Cdd:cd01462  77 INKALRYALELIERR-------DPRKADIVLITDGyEGGVSD----ELLREVELKRSRVARFVALALGDH 135
 
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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