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Conserved domains on  [gi|126722991|ref|NP_062242|]
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inter-alpha-trypsin inhibitor heavy chain H4 precursor [Rattus norvegicus]

Protein Classification

VWA domain-containing protein( domain architecture ID 10652053)

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 3.15e-68

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: 224.79  E-value: 3.15e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 271 MAKNVLFVIDKSGSMAGKKIQQTREALIKILKDLSTQDQFNIIVFSGEANQWEQLLVQATEENLNRAVDYASKIPAQGGT 350
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 351 NINKAVLSAVELLDKSNqaellpsKSVSLIILLTDGEptvgETNPKIIQKNTQEAINGRYSLFCLGFGFDVNYPFLEKLA 430
Cdd:cd01461   81 NMNDALEAALELLNSSP-------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 126722991 431 LDNGGLARRIYEDSDSALQLQD 452
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
24-148 6.67e-66

Vault protein Inter-alpha-Trypsin domain;


:

Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 216.84  E-value: 6.67e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991    24 PITTTEKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRADTVQEATFQVELPRKAFITNFSMIIDGVTYPGVVKEKAEAQK 103
Cdd:smart00609   6 GLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEVAQK 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 126722991   104 QYTAAVGRGESAGLVKTTGRKTEQFEVSVNVAPGSKTTFELIYQE 148
Cdd:smart00609  86 QYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 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 3.15e-68

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: 224.79  E-value: 3.15e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 271 MAKNVLFVIDKSGSMAGKKIQQTREALIKILKDLSTQDQFNIIVFSGEANQWEQLLVQATEENLNRAVDYASKIPAQGGT 350
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 351 NINKAVLSAVELLDKSNqaellpsKSVSLIILLTDGEptvgETNPKIIQKNTQEAINGRYSLFCLGFGFDVNYPFLEKLA 430
Cdd:cd01461   81 NMNDALEAALELLNSSP-------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 126722991 431 LDNGGLARRIYEDSDSALQLQD 452
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
24-148 6.67e-66

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 216.84  E-value: 6.67e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991    24 PITTTEKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRADTVQEATFQVELPRKAFITNFSMIIDGVTYPGVVKEKAEAQK 103
Cdd:smart00609   6 GLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEVAQK 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 126722991   104 QYTAAVGRGESAGLVKTTGRKTEQFEVSVNVAPGSKTTFELIYQE 148
Cdd:smart00609  86 QYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 35-146 6.00e-41

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: 145.70  E-value: 6.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991   35 IYSLTVDSRVSSRFAHTVVTSRVVNRADTVQEATFQVELPRKAFITNFSMIIDGVTYPGVVKEKAEAQKQYTAAVGRGES 114
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 126722991  115 AGLVKTTGRktEQFEVSV-NVAPGSKTTFELIY 146
Cdd:pfam08487  81 AGLLEQDTP--DVFTTSVgNIPPGEKVTVELTY 111
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 255-471 4.06e-39

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 147.17  E-value: 4.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 255 ENGYFVHHFAPEDLPT---MAKNVLFVIDKSGSMAGKKIQQTREALIKILKDLSTQDQFNIIVFSGEAnqweQLLVQATE 331
Cdd:COG2304   71 QTRLLLVGLQPPKAAAeerPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDA----RVLLPPTP 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 332 -ENLNRAVDYASKIPAQGGTNINKAVLSAVELLDKSNQAEllpskSVSLIILLTDGEPTVGETNPKIIQKNTQEAINGRY 410
Cdd:COG2304  147 aTDRAKILAAIDRLQAGGGTALGAGLELAYELARKHFIPG-----RVNRVILLTDGDANVGITDPEELLKLAEEAREEGI 221

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126722991 411 SLFCLGFGFDVNYPFLEKLALDNGGLARRIyEDSDSALQ-LQDFYQEVANPLLSSVTFEYPS 471
Cdd:COG2304  222 TLTTLGVGSDYNEDLLERLADAGGGNYYYI-DDPEEAEKvFVREFSRIGYENRALATEDFPL 282
marine_srt_targ TIGR03788
marine proteobacterial sortase target protein; Members of this protein family are restricted ...
 40-592 9.38e-38

marine proteobacterial sortase target protein; Members of this protein family are restricted to the Proteobacteria. Each contains a C-terminal sortase-recognition motif, transmembrane domain, and basic residues cluster at the the C-terminus, and is encoded adjacent to a sortase gene. This protein is frequently the only sortase target in its genome, which is as unusual its occurrence in Gram-negative rather than Gram-positive genomes. Many bacteria with this system are marine. In addition to the LPXTG signal, members carry a vault protein inter-alpha-trypsin inhibitor domain (pfam08487) and a von Willebrand factor type A domain (pfam00092).


Pssm-ID: 274782 [Multi-domain]  Cd Length: 596  Bit Score: 150.23  E-value: 9.38e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991   40 VDSRVSSRFAHTVVTSRVVNRADTVQEATFQVELPRKAFITNFSMIIDGVTYPGVVKEKAEAQKQYTAAVGRGESAGLVk 119
Cdd:TIGR03788   5 ANITVTGLIARTEVTQTFRNPSQFWVEGRYVFPLPENAAVDSLTMHIGERVIVGQIMPKAAARAIYEQAKAEGKKAALV- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  120 ttgrktEQ-----FEVSV-NVAPGSKTTFELIYQELLQRRLGMYELLLK--VRPEQLVKHLQMDIYIFEPQG--IST--- 186
Cdd:TIGR03788  84 ------EQqrpnlFTNKVaNIGPGETVVVTIEYQQPVSYSSGTFSLRLPltVTPRYIPGSTVNTVTDVNNSGwaIPTtqv 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  187 ---LETESTFMTQ--------------ELANALTTSQNKTKAH-IQFKPTLSQQRK-SQNEQDTVLDGDFTVRYDVDRSS 247
Cdd:TIGR03788 158 pdaDKISAPRVLDpdddapssqasinvDLNAGLPLDSITSPSHpIQIEQQGQSGYTiSLAQGQVIADRDFVLTWRPAQGE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  248 tggtiQIENGYFVHHFAPEDL-------PT-------MAKNVLFVIDKSGSMAGKKIQQTREALIKILKDLSTQDQFNII 313
Cdd:TIGR03788 238 -----APSAALFREQIGGERYglamvmpPTeaavaqvLPRELVFVIDTSGSMAGESIEQAKSALLLALDQLRPGDRFNII 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  314 VFSGEANQWEQLLVQATEENLNRAVDYASKIPAQGGTNINKAvLSAVELLDKSnqaelLPSKSVSLIILLTDGepTVGET 393
Cdd:TIGR03788 313 QFDSDVTLLFPVPVPATAHNLARARQFVAGLQADGGTEMAGA-LSAALRDDGP-----ESSGALRQVVFLTDG--AVGNE 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  394 NPKIIQKNTQEainGRYSLFCLGFGFDVNYPFLEKLALDNGGLARRIYEDSDSALQLQDFYQEVANPLLSSVTFEYPSNA 473
Cdd:TIGR03788 385 DALFQLIRTKL---GDSRLFTVGIGSAPNSYFMRKAAQFGRGSFTFIGSTDEVQRKMSQLFAKLEQPALTDIALTFDNGN 461

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  474 VEDVTRYNFQHHFKGSEMVVAgkLRDQGPDVLLaKVSGQMHLQNitFQTEASIAQQEKEfQGpkyifhnfMERLWALLTI 553
Cdd:TIGR03788 462 AADVYPSPIPDLYRGEPLQIA--IKLQQAAGEL-QLTGRTGSQP--WSQQLDLDSAAPG-KG--------IDKLWARRKI 527

                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 126722991  554 QQQLEQRIsaSGAELEALEAQVLNLSLKYNFVTPLTHMV 592
Cdd:TIGR03788 528 DSLEDSLR--YGANEEKVKDQVTALALNHHLVSPFTSFV 564
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 274-452 1.69e-26

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: 106.77  E-value: 1.69e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991   274 NVLFVIDKSGSMAGKKIQQTREALIKILKDLS---TQDQFNIIVFSGEANQWEQLLVQATEENLNRAVDyASKIPAQGGT 350
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALA-SLSYKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991   351 NINKAVLSAVELLDKSNQAELLPSKSVslIILLTDGEPTVGETNpkiIQKNTQEAINGRYSLFCLGFGFDVNYPFLEKLA 430
Cdd:smart00327  80 NLGAALQYALENLFSKSAGSRRGAPKV--VILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEELKKLA 154

                          170       180
                   ....*....|....*....|..
gi 126722991   431 LDNGGlaRRIYEDSDSALQLQD 452
Cdd:smart00327 155 SAPGG--VYVFLPELLDLLIDL 174
VWA pfam00092
von Willebrand factor type A domain;
274-456 8.20e-25

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 101.97  E-value: 8.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  274 NVLFVIDKSGSMAGKKIQQTREALIKILKDLS---TQDQFNIIVFSGEANQWEQLLVQATEENLNRAVDYASKIPaQGGT 350
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLG-GGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  351 NINKAVLSAVELLDKSNQAEllPSKSVSLIILLTDGEPTVGEtnpkiIQKNTQEAINGRYSLFCLGFGFDVNYPfLEKLA 430
Cdd:pfam00092  80 NTGKALKYALENLFSSAAGA--RPGAPKVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNADDEE-LRKIA 151

                         170       180
                  ....*....|....*....|....*.
gi 126722991  431 LDNGglARRIYEDSDSAlQLQDFYQE 456
Cdd:pfam00092 152 SEPG--EGHVFTVSDFE-ALEDLQDQ 174
 
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 3.15e-68

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: 224.79  E-value: 3.15e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 271 MAKNVLFVIDKSGSMAGKKIQQTREALIKILKDLSTQDQFNIIVFSGEANQWEQLLVQATEENLNRAVDYASKIPAQGGT 350
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 351 NINKAVLSAVELLDKSNqaellpsKSVSLIILLTDGEptvgETNPKIIQKNTQEAINGRYSLFCLGFGFDVNYPFLEKLA 430
Cdd:cd01461   81 NMNDALEAALELLNSSP-------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 126722991 431 LDNGGLARRIYEDSDSALQLQD 452
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
24-148 6.67e-66

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 216.84  E-value: 6.67e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991    24 PITTTEKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRADTVQEATFQVELPRKAFITNFSMIIDGVTYPGVVKEKAEAQK 103
Cdd:smart00609   6 GLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEVAQK 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 126722991   104 QYTAAVGRGESAGLVKTTGRKTEQFEVSVNVAPGSKTTFELIYQE 148
Cdd:smart00609  86 QYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 35-146 6.00e-41

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: 145.70  E-value: 6.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991   35 IYSLTVDSRVSSRFAHTVVTSRVVNRADTVQEATFQVELPRKAFITNFSMIIDGVTYPGVVKEKAEAQKQYTAAVGRGES 114
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 126722991  115 AGLVKTTGRktEQFEVSV-NVAPGSKTTFELIY 146
Cdd:pfam08487  81 AGLLEQDTP--DVFTTSVgNIPPGEKVTVELTY 111
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 255-471 4.06e-39

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 147.17  E-value: 4.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 255 ENGYFVHHFAPEDLPT---MAKNVLFVIDKSGSMAGKKIQQTREALIKILKDLSTQDQFNIIVFSGEAnqweQLLVQATE 331
Cdd:COG2304   71 QTRLLLVGLQPPKAAAeerPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDA----RVLLPPTP 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 332 -ENLNRAVDYASKIPAQGGTNINKAVLSAVELLDKSNQAEllpskSVSLIILLTDGEPTVGETNPKIIQKNTQEAINGRY 410
Cdd:COG2304  147 aTDRAKILAAIDRLQAGGGTALGAGLELAYELARKHFIPG-----RVNRVILLTDGDANVGITDPEELLKLAEEAREEGI 221

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126722991 411 SLFCLGFGFDVNYPFLEKLALDNGGLARRIyEDSDSALQ-LQDFYQEVANPLLSSVTFEYPS 471
Cdd:COG2304  222 TLTTLGVGSDYNEDLLERLADAGGGNYYYI-DDPEEAEKvFVREFSRIGYENRALATEDFPL 282
marine_srt_targ TIGR03788
marine proteobacterial sortase target protein; Members of this protein family are restricted ...
 40-592 9.38e-38

marine proteobacterial sortase target protein; Members of this protein family are restricted to the Proteobacteria. Each contains a C-terminal sortase-recognition motif, transmembrane domain, and basic residues cluster at the the C-terminus, and is encoded adjacent to a sortase gene. This protein is frequently the only sortase target in its genome, which is as unusual its occurrence in Gram-negative rather than Gram-positive genomes. Many bacteria with this system are marine. In addition to the LPXTG signal, members carry a vault protein inter-alpha-trypsin inhibitor domain (pfam08487) and a von Willebrand factor type A domain (pfam00092).


Pssm-ID: 274782 [Multi-domain]  Cd Length: 596  Bit Score: 150.23  E-value: 9.38e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991   40 VDSRVSSRFAHTVVTSRVVNRADTVQEATFQVELPRKAFITNFSMIIDGVTYPGVVKEKAEAQKQYTAAVGRGESAGLVk 119
Cdd:TIGR03788   5 ANITVTGLIARTEVTQTFRNPSQFWVEGRYVFPLPENAAVDSLTMHIGERVIVGQIMPKAAARAIYEQAKAEGKKAALV- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  120 ttgrktEQ-----FEVSV-NVAPGSKTTFELIYQELLQRRLGMYELLLK--VRPEQLVKHLQMDIYIFEPQG--IST--- 186
Cdd:TIGR03788  84 ------EQqrpnlFTNKVaNIGPGETVVVTIEYQQPVSYSSGTFSLRLPltVTPRYIPGSTVNTVTDVNNSGwaIPTtqv 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  187 ---LETESTFMTQ--------------ELANALTTSQNKTKAH-IQFKPTLSQQRK-SQNEQDTVLDGDFTVRYDVDRSS 247
Cdd:TIGR03788 158 pdaDKISAPRVLDpdddapssqasinvDLNAGLPLDSITSPSHpIQIEQQGQSGYTiSLAQGQVIADRDFVLTWRPAQGE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  248 tggtiQIENGYFVHHFAPEDL-------PT-------MAKNVLFVIDKSGSMAGKKIQQTREALIKILKDLSTQDQFNII 313
Cdd:TIGR03788 238 -----APSAALFREQIGGERYglamvmpPTeaavaqvLPRELVFVIDTSGSMAGESIEQAKSALLLALDQLRPGDRFNII 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  314 VFSGEANQWEQLLVQATEENLNRAVDYASKIPAQGGTNINKAvLSAVELLDKSnqaelLPSKSVSLIILLTDGepTVGET 393
Cdd:TIGR03788 313 QFDSDVTLLFPVPVPATAHNLARARQFVAGLQADGGTEMAGA-LSAALRDDGP-----ESSGALRQVVFLTDG--AVGNE 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  394 NPKIIQKNTQEainGRYSLFCLGFGFDVNYPFLEKLALDNGGLARRIYEDSDSALQLQDFYQEVANPLLSSVTFEYPSNA 473
Cdd:TIGR03788 385 DALFQLIRTKL---GDSRLFTVGIGSAPNSYFMRKAAQFGRGSFTFIGSTDEVQRKMSQLFAKLEQPALTDIALTFDNGN 461

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  474 VEDVTRYNFQHHFKGSEMVVAgkLRDQGPDVLLaKVSGQMHLQNitFQTEASIAQQEKEfQGpkyifhnfMERLWALLTI 553
Cdd:TIGR03788 462 AADVYPSPIPDLYRGEPLQIA--IKLQQAAGEL-QLTGRTGSQP--WSQQLDLDSAAPG-KG--------IDKLWARRKI 527

                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 126722991  554 QQQLEQRIsaSGAELEALEAQVLNLSLKYNFVTPLTHMV 592
Cdd:TIGR03788 528 DSLEDSLR--YGANEEKVKDQVTALALNHHLVSPFTSFV 564
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 274-452 1.69e-26

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: 106.77  E-value: 1.69e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991   274 NVLFVIDKSGSMAGKKIQQTREALIKILKDLS---TQDQFNIIVFSGEANQWEQLLVQATEENLNRAVDyASKIPAQGGT 350
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALA-SLSYKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991   351 NINKAVLSAVELLDKSNQAELLPSKSVslIILLTDGEPTVGETNpkiIQKNTQEAINGRYSLFCLGFGFDVNYPFLEKLA 430
Cdd:smart00327  80 NLGAALQYALENLFSKSAGSRRGAPKV--VILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEELKKLA 154

                          170       180
                   ....*....|....*....|..
gi 126722991   431 LDNGGlaRRIYEDSDSALQLQD 452
Cdd:smart00327 155 SAPGG--VYVFLPELLDLLIDL 174
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 171-430 2.13e-26

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 109.38  E-value: 2.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 171 HLQMDIYIFEPQGISTLETESTFMTQELANALTTSQNKTKAHIQFKPTLSQQRKSQNEQDTVLDGDFTV-RYDVDRSSTG 249
Cdd:COG2425   16 LAPAPATALLLAGLLRAALALGLALALRAALLALLLLLLRAALALLTLLAGLVLLALDALLLAALLAALlDALLLAVLLL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 250 GTIQIENGYFVHHFAPEDLPTMAKNVLFVIDKSGSMAGKKIQQTREALIKILKDLSTQDQFNIIVFSGEAnqWEQLLVQA 329
Cdd:COG2425   96 ALLLLAALLLLAAPASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEV--VEDLPLTA 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 330 TeENLNRAVDYASKIPAQGGTNINKAVLSAVELLDKSNQAEllpsksvSLIILLTDGEPTVGETNpkiIQKNTQEAINGr 409
Cdd:COG2425  174 D-DGLEDAIEFLSGLFAGGGTDIAPALRAALELLEEPDYRN-------ADIVLITDGEAGVSPEE---LLREVRAKESG- 241

                        250       260
                 ....*....|....*....|.
gi 126722991 410 YSLFCLGFGFDVNYPFLEKLA 430
Cdd:COG2425  242 VRLFTVAIGDAGNPGLLEALA 262
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 269-458 8.24e-26

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: 107.72  E-value: 8.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 269 PTMAKNVLFVIDKSGSMAGK-KIQQTREALIKILKDLSTQDQFNIIVFSGEAnqweQLLVQATeENLNRAVDYASKIPAQ 347
Cdd:COG1240   89 PQRGRDVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFGGEA----EVLLPLT-RDREALKRALDELPPG 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 348 GGTNINKAVLSAVELLDKSNqaellPSKSVsLIILLTDGEPTVGETNPKIIqknTQEAINGRYSLFCLGFGFD-VNYPFL 426
Cdd:COG1240  164 GGTPLGDALALALELLKRAD-----PARRK-VIVLLTDGRDNAGRIDPLEA---AELAAAAGIRIYTIGVGTEaVDEGLL 234

                        170       180       190
                 ....*....|....*....|....*....|..
gi 126722991 427 EKLALDNGGLARRIyedsDSALQLQDFYQEVA 458
Cdd:COG1240  235 REIAEATGGRYFRA----DDLSELAAIYREID 262
VWA pfam00092
von Willebrand factor type A domain;
274-456 8.20e-25

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 101.97  E-value: 8.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  274 NVLFVIDKSGSMAGKKIQQTREALIKILKDLS---TQDQFNIIVFSGEANQWEQLLVQATEENLNRAVDYASKIPaQGGT 350
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLG-GGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  351 NINKAVLSAVELLDKSNQAEllPSKSVSLIILLTDGEPTVGEtnpkiIQKNTQEAINGRYSLFCLGFGFDVNYPfLEKLA 430
Cdd:pfam00092  80 NTGKALKYALENLFSSAAGA--RPGAPKVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNADDEE-LRKIA 151

                         170       180
                  ....*....|....*....|....*.
gi 126722991  431 LDNGglARRIYEDSDSAlQLQDFYQE 456
Cdd:pfam00092 152 SEPG--EGHVFTVSDFE-ALEDLQDQ 174
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 274-435 9.31e-25

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: 101.49  E-value: 9.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 274 NVLFVIDKSGSMAGKKIQQTREALIKILKDLS---TQDQFNIIVFSGEANQWEQLLVQATEENLNRAVDyASKIPAQGGT 350
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSaspPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAID-ALKKGLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 351 NINKAVLSAVELLDKSNQaellpSKSVSLIILLTDGEPTVGETNPKiiqKNTQEAINGRYSLFCLGFGFDVNYPFLEKLA 430
Cdd:cd00198   81 NIGAALRLALELLKSAKR-----PNARRVIILLTDGEPNDGPELLA---EAARELRKLGITVYTIGIGDDANEDELKEIA 152


                 ....*
gi 126722991 431 LDNGG 435
Cdd:cd00198  153 DKTTG 157
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 274-435 9.38e-25

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: 101.58  E-value: 9.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 274 NVLFVIDKSGSMAGKKIQQTREALIKILKDLSTQDQFNIIVFSGEAnqweQLLVQAT----EENLNRAVDyasKIPAQGG 349
Cdd:cd01465    2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAA----ETVLPATpvrdKAAILAAID---RLTAGGS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 350 TNINKAVLSAVELLDKSnqaelLPSKSVSLIILLTDGEPTVGETNPKIIQKNTQEAINGRYSLFCLGFGFDVNYPFLEKL 429
Cdd:cd01465   75 TAGGAGIQLGYQEAQKH-----FVPGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAI 149


                 ....*.
gi 126722991 430 ALDNGG 435
Cdd:cd01465  150 ADAGNG 155
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
274-464 7.97e-19

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 85.36  E-value: 7.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 274 NVLFVIDKSGSMAGKKIQQTREALIKILKDLSTQDQ------FNIIVFSGEAnQWEQLLVQAteENLnravdYASKIPAQ 347
Cdd:COG4245    7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYaletveVSVITFDGEA-KVLLPLTDL--EDF-----QPPDLSAS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 348 GGTNINKAVLSAVELLDKSNQAelLPSKSVS----LIILLTDGEPTVGETNPkIIQKNTQEAINGRYSLFCLGFGFDVNY 423
Cdd:COG4245   79 GGTPLGAALELLLDLIERRVQK--YTAEGKGdwrpVVFLITDGEPTDSDWEA-ALQRLKDGEAAKKANIFAIGVGPDADT 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 126722991 424 PFLEKLALDNGGLarriyeDSDSALQLQDFYQEVANPLLSS 464
Cdd:COG4245  156 EVLKQLTDPVRAL------DALDGLDFREFFKWLSASVSSV 190
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 270-435 9.50e-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: 67.80  E-value: 9.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 270 TMAKNVLFVIDKSGSMAGKK---IQQTREAlikILKDLSTQDQFNIIVFSGEANQ----WEQLLVQATEEN---LNRAVD 339
Cdd:cd01463   11 TSPKDIVILLDVSGSMTGQRlhlAKQTVSS---ILDTLSDNDFFNIITFSNEVNPvvpcFNDTLVQATTSNkkvLKEALD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 340 yasKIPAQGGTNINKAVLSAVELLDKSNQAELLPSKSV--SLIILLTDGEPtvgETNPKIIQK-NTQEAINGRYSLFCLG 416
Cdd:cd01463   88 ---MLEAKGIANYTKALEFAFSLLLKNLQSNHSGSRSQcnQAIMLITDGVP---ENYKEIFDKyNWDKNSEIPVRVFTYL 161

                        170       180
                 ....*....|....*....|
gi 126722991 417 FGFDV-NYPFLEKLALDNGG 435
Cdd:cd01463  162 IGREVtDRREIQWMACENKG 181
VWA_3 pfam13768
von Willebrand factor type A domain;
273-438 3.48e-12

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 65.11  E-value: 3.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  273 KNVLFVIDKSGSMAGKKIQQtREALIKILKDLSTQDQFNIIVFSGEANQWEQLLVQATEENLNRAVDYASKIPAQ-GGTN 351
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPlGGSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  352 INKAVLSAVELLDksnqaellPSKSVSLIILLTDGEPTVGETnpKIIQKNTQEAinGRYSLFCLGFGFDVNYPFLEKLAL 431
Cdd:pfam13768  80 LLGALKEAVRAPA--------SPGYIRHVLLLTDGSPMQGET--RVSDLISRAP--GKIRFFAYGLGASISAPMLQLLAE 147


                  ....*..
gi 126722991  432 DNGGLAR 438
Cdd:pfam13768 148 ASNGTYE 154
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 274-430 1.11e-11

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: 63.85  E-value: 1.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 274 NVLFVIDKSGSMAGKKIQQTREALIKILKDLS---TQDQFNIIVFSGEANQWEQLLVQATEENLNRAVDyASKIPAQGGT 350
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDigpDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVK-NLKYLGGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 351 NINKAVLSAVELLDKSNQAEllpSKSVSLIILLTDGEPTVGETNPKIIQKNTQEAINgrysLFCLGFGfDVNYPFLEKLA 430
Cdd:cd01450   81 NTGKALQYALEQLFSESNAR---ENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIK----VFVVGVG-PADEEELREIA 152
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 278-436 2.42e-11

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: 62.79  E-value: 2.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 278 VIDKSGSMAGKKIQQTREALIKILKDLSTQDQFNIIVFSGEANQWeQLLVQATEEN---LNRAVDyasKIPAQGGTNINK 354
Cdd:cd01466    6 VLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRL-SPLRRMTAKGkrsAKRVVD---GLQAGGGTNVVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 355 AVLSAVELLDKSNQAELLPSksvslIILLTDGEPTVGETNPKiiqkntqeAINGRYSLFCLGFGFDVNYPFLEKLALDNG 434
Cdd:cd01466   82 GLKKALKVLGDRRQKNPVAS-----IMLLSDGQDNHGAVVLR--------ADNAPIPIHTFGLGASHDPALLAFIAEITG 148


                 ..
gi 126722991 435 GL 436
Cdd:cd01466  149 GT 150
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 279-387 1.06e-09

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: 57.74  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 279 IDKSGSMAGKKIQQTREALIKILKDLSTQDQ-FNIIVFSGEanqWEQLLVQATEeNLNRAVDYASKIPAQGGTNINKAVL 357
Cdd:cd01462    7 VDQSGSMYGAPEEVAKAVALALLRIALAENRdTYLILFDSE---FQTKIVDKTD-DLEEPVEFLSGVQLGGGTDINKALR 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 126722991 358 SAVELLDksnqaELLPSKSVslIILLTDGE 387
Cdd:cd01462   83 YALELIE-----RRDPRKAD--IVLITDGY 105
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 275-391 7.15e-09

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: 56.13  E-value: 7.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 275 VLFVIDKSGSMAG-KKIQQTREALIKILKDLST-QDQFNIIVFSGEAnqwEQLLVQATeENLNRAVDYASKIPAQGGTNI 352
Cdd:cd01451    3 VIFVVDASGSMAArHRMAAAKGAVLSLLRDAYQrRDKVALIAFRGTE---AEVLLPPT-RSVELAKRRLARLPTGGGTPL 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 126722991 353 NKAVLSAVELLDKSNQAEllpsKSVSLIILLTDGEPTVG 391
Cdd:cd01451   79 AAGLLAAYELAAEQARDP----GQRPLIVVITDGRANVG 113
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 274-425 1.34e-08

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: 55.41  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 274 NVLFVIDKSGSMAGKKIQQ-TREALIK-ILKDLSTQ---DQFNIIVFSGEAnqWEQLLVQATEENLNRAVDYASKIPAQG 348
Cdd:cd01467    4 DIMIALDVSGSMLAQDFVKpSRLEAAKeVLSDFIDRrenDRIGLVVFAGAA--FTQAPLTLDRESLKELLEDIKIGLAGQ 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126722991 349 GTNINKAVLSAVELLDKSNQAEllpsksvSLIILLTDGEPTVGETNPkIIQKNTQEAINGRysLFCLGFGFDVNYPF 425
Cdd:cd01467   82 GTAIGDAIGLAIKRLKNSEAKE-------RVIVLLTDGENNAGEIDP-ATAAELAKNKGVR--IYTIGVGKSGSGPK 148
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 275-430 2.21e-08

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: 54.65  E-value: 2.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 275 VLFVIDKSGSMAGKKIQQTREALIKILKDLStQDQF-------NIIVFSGEANQwEQLLVQAteENLnravdYASKIPAQ 347
Cdd:cd01464    6 IYLLLDTSGSMAGEPIEALNQGLQMLQSELR-QDPYalesveiSVITFDSAARV-IVPLTPL--ESF-----QPPRLTAS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 348 GGTNINKAVLSAVELLDKSNQaellpsKSVS--------LIILLTDGEPTvGETNPKIIQKNTQEAINGRYSLFCLGFGF 419
Cdd:cd01464   77 GGTSMGAALELALDCIDRRVQ------RYRAdqkgdwrpWVFLLTDGEPT-DDLTAAIERIKEARDSKGRIVACAVGPKA 149

                        170
                 ....*....|.
gi 126722991 420 DVNYpfLEKLA 430
Cdd:cd01464  150 DLDT--LKQIT 158
VWA_2 pfam13519
von Willebrand factor type A domain;
275-365 3.67e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 49.21  E-value: 3.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  275 VLFVIDKSGSMAGKKIQQTR-----EALIKILKDLSTqDQFNIIVFSGEANqweqLLVQATEEN--LNRAVDYASkiPAQ 347
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRleaakDAVLALLKSLPG-DRVGLVTFGDGPE----VLIPLTKDRakILRALRRLE--PKG 73

                          90
                  ....*....|....*...
gi 126722991  348 GGTNINKAVLSAVELLDK 365
Cdd:pfam13519  74 GGTNLAAALQLARAALKH 91
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 277-387 4.29e-06

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: 48.28  E-value: 4.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 277 FVIDKSGSMAGK--KIQQTREALIKilKDLSTQDQFNIIVFSGEANQweQLLVQATEENLNRAVDYASKIPAQGGTNINK 354
Cdd:cd01474    9 FVLDKSGSVAANwiEIYDFVEQLVD--RFNSPGLRFSFITFSTRATK--ILPLTDDSSAIIKGLEVLKKVTPSGQTYIHE 84

                         90       100       110
                 ....*....|....*....|....*....|...
gi 126722991 355 AVLSAVELLDKSNQAELlpsKSVSLIILLTDGE 387
Cdd:cd01474   85 GLENANEQIFNRNGGGR---ETVSVIIALTDGQ 114
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 263-446 2.42e-05

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: 46.27  E-value: 2.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 263 FAPEDLPTMAK---NVLFVIDKSGSMAGK------KIQQTREALIKILKDLSTQDQFNIIVFSGEAN---QWEQLLV--- 327
Cdd:cd01456    8 FALEPVETEPQlppNVAIVLDNSGSMREVdgggetRLDNAKAALDETANALPDGTRLGLWTFSGDGDnplDVRVLVPkgc 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 328 ---------QATEENLNRAvdYASKIPAQGGTNINKAVLSAVELLDKsnqaellpsKSVSLIILLTDGEPTVGETNPKII 398
Cdd:cd01456   88 ltapvngfpSAQRSALDAA--LNSLQTPTGWTPLAAALAEAAAYVDP---------GRVNVVVLITDGEDTCGPDPCEVA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 126722991 399 QK-NTQEAINGRYSLFCLGFGFDVNYPFLEKLALDNGGLARRIYEDSDS 446
Cdd:cd01456  157 RElAKRRTPAPPIKVNVIDFGGDADRAELEAIAEATGGTYAYNQSDLAS 205
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 273-386 4.03e-05

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 45.08  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 273 KNVLFVIDKSGSMAGkKIQQTREALIKILKDLS---TQDQFNIIVFSGEANQWEQ--LLVQATEENLNRAVDyasKIPAQ 347
Cdd:cd01476    1 LDLLFVLDSSGSVRG-KFEKYKKYIERIVEGLEigpTATRVALITYSGRGRQRVRfnLPKHNDGEELLEKVD---NLRFI 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 126722991 348 GG-TNINKAVLSAVELLDKSNQAEllpSKSVSLIILLTDG 386
Cdd:cd01476   77 GGtTATGAAIEVALQQLDPSEGRR---EGIPKVVVVLTDG 113
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 275-389 5.72e-04

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: 41.54  E-value: 5.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991 275 VLFVIDKSGSM-AGKKIQQTREALIKILKDL-STQDQFNIIVFSGEA--NQWEQLLVQAT-EENLNRAVDY-ASKIPAQG 348
Cdd:cd01454    3 VTLLLDLSGSMrSDRRIDVAKKAAVLLAEALeACGVPHAILGFTTDAggRERVRWIKIKDfDESLHERARKrLAALSPGG 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 126722991 349 GTNINKAVLSAVELLDKSNQAEllpsksvSLIILLTDGEPT 389
Cdd:cd01454   83 NTRDGAAIRHAAERLLARPEKR-------KILLVISDGEPN 116
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 275-387 6.57e-03

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


Pssm-ID: 129946 [Multi-domain]  Cd Length: 863  Bit Score: 40.25  E-value: 6.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722991  275 VLFVIDKSGSMAGKK--IQQTREALIKILKDLSTQDQFNIIVFSGEAnQWEQLLVQATEENLNRAVDYASKIPAQGGTNI 352
Cdd:TIGR00868 307 VCLVLDKSGSMTVEDrlKRMNQAAKLFLLQTVEKGSWVGMVTFDSAA-YIKNELIQITSSAERDALTANLPTAASGGTSI 385

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 126722991  353 NKAVLSAVELLDKSNQaellpSKSVSLIILLTDGE 387
Cdd:TIGR00868 386 CSGLKAAFQVIKKSYQ-----STDGSEIVLLTDGE 415
 
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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