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Conserved domains on  [gi|156119625|ref|NP_002206|]
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inter-alpha-trypsin inhibitor heavy chain H1 isoform a preproprotein [Homo sapiens]

Protein Classification

VWA domain-containing protein( domain architecture ID 10652060)

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
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 705-892 1.05e-92

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


:

Pssm-ID: 461981  Cd Length: 189  Bit Score: 290.64  E-value: 1.05e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625  705 NTGFSVNGQLIGNKARsPGQHD--GTYFGRLGIANPATDFQLEVTPQNITLNPGFGGPVFSWRDQAVLRQDGVVVTINKK 782
Cdd:pfam06668   1 GSGVTVNGQLIGAKKP-PGSHKklRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625  783 RNLVVSVDDGGTFEVVLHRVWKGSSVHQDFLGFYVLDSHRMSARTHGLLGQFFHPIGFEVSDIHPGSDPTKPDATMVVRN 862
Cdd:pfam06668  80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKG 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 156119625  863 RRLTVTRGLQKDYSKDPWHGAEVSCWFIHN 892
Cdd:pfam06668 160 HKLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
37-166 3.88e-68

Vault protein Inter-alpha-Trypsin domain;


:

Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 222.62  E-value: 3.88e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625    37 SSEKRQAVDTAVDGVFIRSLKVNCKVTSRFAHYVVTSQVVNTANEAREVAFDLEIPKTAFISDFAVTADGNAFIGDIKDK 116
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 156119625   117 VTAWKQYRKAAISGENAGLVRASGRTMEQFTIHLTVNPQSKVTFQLTYEE 166
Cdd:smart00609  81 EVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 289-470 2.54e-66

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: 219.01  E-value: 2.54e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 289 MNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQSWKGSLVQASEANLQAAQDFVRGFSLDEAT 368
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 369 NLNGGLLRGIEILNqvqeslpELSNHASILIMLTDGDptegVTDRSQILKNVRNAIRGRFPLYNLGFGHNVDFNFLEVMS 448
Cdd:cd01461   81 NMNDALEAALELLN-------SSPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 156119625 449 MENNGRAQRIYEDHDATQQLQG 470
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
 
Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 705-892 1.05e-92

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


Pssm-ID: 461981  Cd Length: 189  Bit Score: 290.64  E-value: 1.05e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625  705 NTGFSVNGQLIGNKARsPGQHD--GTYFGRLGIANPATDFQLEVTPQNITLNPGFGGPVFSWRDQAVLRQDGVVVTINKK 782
Cdd:pfam06668   1 GSGVTVNGQLIGAKKP-PGSHKklRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625  783 RNLVVSVDDGGTFEVVLHRVWKGSSVHQDFLGFYVLDSHRMSARTHGLLGQFFHPIGFEVSDIHPGSDPTKPDATMVVRN 862
Cdd:pfam06668  80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKG 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 156119625  863 RRLTVTRGLQKDYSKDPWHGAEVSCWFIHN 892
Cdd:pfam06668 160 HKLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
37-166 3.88e-68

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 222.62  E-value: 3.88e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625    37 SSEKRQAVDTAVDGVFIRSLKVNCKVTSRFAHYVVTSQVVNTANEAREVAFDLEIPKTAFISDFAVTADGNAFIGDIKDK 116
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 156119625   117 VTAWKQYRKAAISGENAGLVRASGRTMEQFTIHLTVNPQSKVTFQLTYEE 166
Cdd:smart00609  81 EVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 289-470 2.54e-66

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: 219.01  E-value: 2.54e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 289 MNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQSWKGSLVQASEANLQAAQDFVRGFSLDEAT 368
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 369 NLNGGLLRGIEILNqvqeslpELSNHASILIMLTDGDptegVTDRSQILKNVRNAIRGRFPLYNLGFGHNVDFNFLEVMS 448
Cdd:cd01461   81 NMNDALEAALELLN-------SSPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 156119625 449 MENNGRAQRIYEDHDATQQLQG 470
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 282-491 3.12e-34

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 132.92  E-value: 3.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 282 APQNLTNMNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQswkgsLVQASE--ANLQAAQDFV 359
Cdd:COG2304   83 KAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDAR-----VLLPPTpaTDRAKILAAI 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 360 RGFSLDEATNLNGGLLRGIEILNQVQEslpelSNHASILIMLTDGDPTEGVTDRSQILKNVRNAIRGRFPLYNLGFGHNV 439
Cdd:COG2304  158 DRLQAGGGTALGAGLELAYELARKHFI-----PGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDY 232

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 156119625 440 DFNFLEVMSMENNGRAQRIYEDHDATQQLQGFYSQVAKPLLVDVDLQYPQDA 491
Cdd:COG2304  233 NEDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPLPY 284
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 53-164 3.21e-31

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: 117.97  E-value: 3.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625   53 IRSLKVNCKVTSRFAHYVVTSQVVNTANEAREVAFDLEIPKTAFISDFAVTADGNAFIGDIKDKVTAWKQYRKAAISGEN 132
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 156119625  133 AGLVRASgrTMEQFTIHL-TVNPQSKVTFQLTY 164
Cdd:pfam08487  81 AGLLEQD--TPDVFTTSVgNIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 292-469 2.77e-24

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: 100.61  E-value: 2.77e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625   292 NVVFVIDISGSMRGQKVKQTKEALLKILGDM---QPGDYFDLVLFGTRVQSWKGSLvqaSEANLQAAQDFVRGFSLD--E 366
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLN---DSRSKDALLEALASLSYKlgG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625   367 ATNLNGGLLRGIEILNqvQESLPELSNHASILIMLTDGDPTEGVTDrsqILKNVRNAIRGRFPLYNLGFGHNVDFNFLEV 446
Cdd:smart00327  78 GTNLGAALQYALENLF--SKSAGSRRGAPKVVILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEELKK 152

                          170       180
                   ....*....|....*....|...
gi 156119625   447 MSMENNGRAQRIYEDHDATQQLQ 469
Cdd:smart00327 153 LASAPGGVYVFLPELLDLLIDLL 175
VWA pfam00092
von Willebrand factor type A domain;
292-474 3.99e-21

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 91.57  E-value: 3.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625  292 NVVFVIDISGSMRGQKVKQTKEALLKILGDMQ---PGDYFDLVLFGTRVQ-SWKGSLVQASEANLQAAQDFVrgFSLDEA 367
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVRtEFPLNDYSSKEELLSAVDNLR--YLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625  368 TNLNGGLLRGIEILNQVQESLPElsNHASILIMLTDGDPTEGvtdrsQILKNVRNAIRGRFPLYNLGFGhNVDFNFLEVM 447
Cdd:pfam00092  79 TNTGKALKYALENLFSSAAGARP--GAPKVVVLLTDGRSQDG-----DPEEVARELKSAGVTVFAVGVG-NADDEELRKI 150

                         170       180
                  ....*....|....*....|....*..
gi 156119625  448 SMENNgrAQRIYEDHDATqQLQGFYSQ 474
Cdd:pfam00092 151 ASEPG--EGHVFTVSDFE-ALEDLQDQ 174
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 283-435 3.62e-03

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: 40.37  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625  283 PQNLTNMNKN------VVFVIDISGSMRgQKVKQTKEALLKIL-GDMQPGDYFDLVLFGTR---VQSWKGSLVQaseanL 352
Cdd:TIGR03436  40 PQTIASFRREtdlpltVGLVIDTSGSMR-NDLDRARAAAIRFLkTVLRPNDRVFVVTFNTRlrlLQDFTSDPRL-----L 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625  353 QAAQDFVR--GFSLDEATNLNGGLLRGIEILNQVQ-ESLPELSNHAS------ILIMLTDGDPTEGVTDRSQIlknVRNA 423
Cdd:TIGR03436 114 EAALNRLKppLRTDYNSSGAFVRDGGGTALYDAITlAALEQLANALAgipgrkALIVISDGGDNRSRDTLERA---IDAA 190

                         170
                  ....*....|..
gi 156119625  424 IRGRFPLYNLGF 435
Cdd:TIGR03436 191 QRADVAIYSIDA 202
 
Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 705-892 1.05e-92

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


Pssm-ID: 461981  Cd Length: 189  Bit Score: 290.64  E-value: 1.05e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625  705 NTGFSVNGQLIGNKARsPGQHD--GTYFGRLGIANPATDFQLEVTPQNITLNPGFGGPVFSWRDQAVLRQDGVVVTINKK 782
Cdd:pfam06668   1 GSGVTVNGQLIGAKKP-PGSHKklRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625  783 RNLVVSVDDGGTFEVVLHRVWKGSSVHQDFLGFYVLDSHRMSARTHGLLGQFFHPIGFEVSDIHPGSDPTKPDATMVVRN 862
Cdd:pfam06668  80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKG 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 156119625  863 RRLTVTRGLQKDYSKDPWHGAEVSCWFIHN 892
Cdd:pfam06668 160 HKLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
37-166 3.88e-68

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 222.62  E-value: 3.88e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625    37 SSEKRQAVDTAVDGVFIRSLKVNCKVTSRFAHYVVTSQVVNTANEAREVAFDLEIPKTAFISDFAVTADGNAFIGDIKDK 116
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 156119625   117 VTAWKQYRKAAISGENAGLVRASGRTMEQFTIHLTVNPQSKVTFQLTYEE 166
Cdd:smart00609  81 EVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 289-470 2.54e-66

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: 219.01  E-value: 2.54e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 289 MNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQSWKGSLVQASEANLQAAQDFVRGFSLDEAT 368
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 369 NLNGGLLRGIEILNqvqeslpELSNHASILIMLTDGDptegVTDRSQILKNVRNAIRGRFPLYNLGFGHNVDFNFLEVMS 448
Cdd:cd01461   81 NMNDALEAALELLN-------SSPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 156119625 449 MENNGRAQRIYEDHDATQQLQG 470
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 282-491 3.12e-34

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 132.92  E-value: 3.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 282 APQNLTNMNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQswkgsLVQASE--ANLQAAQDFV 359
Cdd:COG2304   83 KAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDAR-----VLLPPTpaTDRAKILAAI 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 360 RGFSLDEATNLNGGLLRGIEILNQVQEslpelSNHASILIMLTDGDPTEGVTDRSQILKNVRNAIRGRFPLYNLGFGHNV 439
Cdd:COG2304  158 DRLQAGGGTALGAGLELAYELARKHFI-----PGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDY 232

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 156119625 440 DFNFLEVMSMENNGRAQRIYEDHDATQQLQGFYSQVAKPLLVDVDLQYPQDA 491
Cdd:COG2304  233 NEDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPLPY 284
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 53-164 3.21e-31

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: 117.97  E-value: 3.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625   53 IRSLKVNCKVTSRFAHYVVTSQVVNTANEAREVAFDLEIPKTAFISDFAVTADGNAFIGDIKDKVTAWKQYRKAAISGEN 132
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 156119625  133 AGLVRASgrTMEQFTIHL-TVNPQSKVTFQLTY 164
Cdd:pfam08487  81 AGLLEQD--TPDVFTTSVgNIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 292-469 2.77e-24

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: 100.61  E-value: 2.77e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625   292 NVVFVIDISGSMRGQKVKQTKEALLKILGDM---QPGDYFDLVLFGTRVQSWKGSLvqaSEANLQAAQDFVRGFSLD--E 366
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLN---DSRSKDALLEALASLSYKlgG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625   367 ATNLNGGLLRGIEILNqvQESLPELSNHASILIMLTDGDPTEGVTDrsqILKNVRNAIRGRFPLYNLGFGHNVDFNFLEV 446
Cdd:smart00327  78 GTNLGAALQYALENLF--SKSAGSRRGAPKVVILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEELKK 152

                          170       180
                   ....*....|....*....|...
gi 156119625   447 MSMENNGRAQRIYEDHDATQQLQ 469
Cdd:smart00327 153 LASAPGGVYVFLPELLDLLIDLL 175
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 292-476 4.37e-22

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: 96.93  E-value: 4.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 292 NVVFVIDISGSMRGQ-KVKQTKEALLKILGDMQPGDYFDLVLFGTRVQswkgsLVQASEANLQAAQDFVRGFSLDEATNL 370
Cdd:COG1240   94 DVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAE-----VLLPLTRDREALKRALDELPPGGGTPL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 371 NGGLLRGIEILNQVQESLPelsnhaSILIMLTDGDPTEGVTDRSQILKNVRNAirgRFPLYNLGFGHN-VDFNFLEVMSM 449
Cdd:COG1240  169 GDALALALELLKRADPARR------KVIVLLTDGRDNAGRIDPLEAAELAAAA---GIRIYTIGVGTEaVDEGLLREIAE 239

                        170       180
                 ....*....|....*....|....*..
gi 156119625 450 ENNGRAQRIyedhDATQQLQGFYSQVA 476
Cdd:COG1240  240 ATGGRYFRA----DDLSELAAIYREID 262
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 282-448 5.38e-22

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 96.67  E-value: 5.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 282 APQNLTNMNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQSwkgSLVQASEANLQAAQDFVRG 361
Cdd:COG2425  110 ASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE---DLPLTADDGLEDAIEFLSG 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 362 FSLDEATNLNGGLLRGIEILNQVQeslpelsNHASILIMLTDGDPTEgvtDRSQILKNVRNAiRGRFPLYNLGFGHNVDF 441
Cdd:COG2425  187 LFAGGGTDIAPALRAALELLEEPD-------YRNADIVLITDGEAGV---SPEELLREVRAK-ESGVRLFTVAIGDAGNP 255


                 ....*..
gi 156119625 442 NFLEVMS 448
Cdd:COG2425  256 GLLEALA 262
VWA pfam00092
von Willebrand factor type A domain;
292-474 3.99e-21

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 91.57  E-value: 3.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625  292 NVVFVIDISGSMRGQKVKQTKEALLKILGDMQ---PGDYFDLVLFGTRVQ-SWKGSLVQASEANLQAAQDFVrgFSLDEA 367
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVRtEFPLNDYSSKEELLSAVDNLR--YLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625  368 TNLNGGLLRGIEILNQVQESLPElsNHASILIMLTDGDPTEGvtdrsQILKNVRNAIRGRFPLYNLGFGhNVDFNFLEVM 447
Cdd:pfam00092  79 TNTGKALKYALENLFSSAAGARP--GAPKVVVLLTDGRSQDG-----DPEEVARELKSAGVTVFAVGVG-NADDEELRKI 150

                         170       180
                  ....*....|....*....|....*..
gi 156119625  448 SMENNgrAQRIYEDHDATqQLQGFYSQ 474
Cdd:pfam00092 151 ASEPG--EGHVFTVSDFE-ALEDLQDQ 174
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 292-453 2.10e-20

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: 89.16  E-value: 2.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 292 NVVFVIDISGSMRGQKVKQTKEALLKILGDMQ---PGDYFDLVLFGTRVQSWKGSLVQASEANLQAAQDFVRgFSLDEAT 368
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSaspPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALK-KGLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 369 NLNGGLLRGIEILNQvqeslPELSNHASILIMLTDGDPTEGVTDRSQILKNVRNAirgRFPLYNLGFGHNVDFNFLEVMS 448
Cdd:cd00198   81 NIGAALRLALELLKS-----AKRPNARRVIILLTDGEPNDGPELLAEAARELRKL---GITVYTIGIGDDANEDELKEIA 152


                 ....*
gi 156119625 449 MENNG 453
Cdd:cd00198  153 DKTTG 157
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 292-458 2.70e-16

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: 77.31  E-value: 2.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 292 NVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVqswkGSLVQASEANLQAA-QDFVRGFSLDEATNL 370
Cdd:cd01465    2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAA----ETVLPATPVRDKAAiLAAIDRLTAGGSTAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 371 NGGLLRGIEILnqVQESLPELSNHasiLIMLTDGDPTEGVTDRSQILKNVRNAIRGRFPLYNLGFGHNVDFNFLEVMSME 450
Cdd:cd01465   78 GAGIQLGYQEA--QKHFVPGGVNR---ILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAIADA 152


                 ....*...
gi 156119625 451 NNGRAQRI 458
Cdd:cd01465  153 GNGNTAYI 160
VWA_3 pfam13768
von Willebrand factor type A domain;
291-456 1.88e-13

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 68.96  E-value: 1.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625  291 KNVVFVIDISGSMRGQKVKQtKEALLKILGDMQPGDYFDLVLFGTRVQSWKGSLVQASEANLQAAQDFVRGFSLDE-ATN 369
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLgGSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625  370 LNGGLLRGIEilnqvQESLPELSNHasiLIMLTDGDPTEGVTDrsqILKNVRNAiRGRFPLYNLGFGHNVDFNFLEVMSM 449
Cdd:pfam13768  80 LLGALKEAVR-----APASPGYIRH---VLLLTDGSPMQGETR---VSDLISRA-PGKIRFFAYGLGASISAPMLQLLAE 147


                  ....*..
gi 156119625  450 ENNGRAQ 456
Cdd:pfam13768 148 ASNGTYE 154
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
292-445 4.94e-11

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 63.02  E-value: 4.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 292 NVVFVIDISGSMRGQKVKQTKEALLKILGDMQP------GDYFDLVLFGTRVQsWKGSLVQASEanLQAAQDFVRGfsld 365
Cdd:COG4245    7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQdpyaleTVEVSVITFDGEAK-VLLPLTDLED--FQPPDLSASG---- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 366 eATNLNGGLLRGIEIL-NQVQESLPE-LSNHASILIMLTDGDPTEgvTDRSQILKNVRNAIRGRFP-LYNLGFGHNVDFN 442
Cdd:COG4245   80 -GTPLGAALELLLDLIeRRVQKYTAEgKGDWRPVVFLITDGEPTD--SDWEAALQRLKDGEAAKKAnIFAIGVGPDADTE 156


                 ...
gi 156119625 443 FLE 445
Cdd:COG4245  157 VLK 159
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 293-453 1.18e-08

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: 55.09  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 293 VVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTrvQSWKGS-LVQASEANLQAAQDFVRGFSLDEATNLN 371
Cdd:cd01466    3 LVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFST--SAKRLSpLRRMTAKGKRSAKRVVDGLQAGGGTNVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 372 GGLLRGIEILNQVQEslpelSNHASILIMLTDGDPTEGVTdrsqilknVRNAIRGRFPLYNLGFGHNVDFNFLEVMSMEN 451
Cdd:cd01466   81 GGLKKALKVLGDRRQ-----KNPVASIMLLSDGQDNHGAV--------VLRADNAPIPIHTFGLGASHDPALLAFIAEIT 147


                 ..
gi 156119625 452 NG 453
Cdd:cd01466  148 GG 149
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 291-476 5.72e-08

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: 53.94  E-value: 5.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 291 KNVVFVIDISGSMRGQK---VKQTKEALLKILGDmqpGDYFDLVLFGTRVQS----WKGSLVQASEANLQAAQDFVRGFS 363
Cdd:cd01463   14 KDIVILLDVSGSMTGQRlhlAKQTVSSILDTLSD---NDFFNIITFSNEVNPvvpcFNDTLVQATTSNKKVLKEALDMLE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 364 LDEATNLNGGLLRGIEILNQVQESLpeLSNHASI---LIMLTdgdpTEGVTDR-SQILK--NVRNAIRGRFPLYNLGFG- 436
Cdd:cd01463   91 AKGIANYTKALEFAFSLLLKNLQSN--HSGSRSQcnqAIMLI----TDGVPENyKEIFDkyNWDKNSEIPVRVFTYLIGr 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 156119625 437 HNVDFNFLEVMSMENngraqriyedhdatqqlQGFYSQVA 476
Cdd:cd01463  165 EVTDRREIQWMACEN-----------------KGYYSHIQ 187
VWA_2 pfam13519
von Willebrand factor type A domain;
293-401 1.46e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 44.59  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625  293 VVFVIDISGSMRGQKVKQT-----KEALLKILGDMqPGDYFDLVLFGTRVQ---SWKGSLVQASEAnLQAAQDFVRGfsl 364
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTrleaaKDAVLALLKSL-PGDRVGLVTFGDGPEvliPLTKDRAKILRA-LRRLEPKGGG--- 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 156119625  365 deaTNLNGGLLRGIEILNQVQeslpelSNHASILIML 401
Cdd:pfam13519  76 ---TNLAAALQLARAALKHRR------KNQPRRIVLI 103
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 292-419 2.41e-04

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: 42.66  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 292 NVVFVIDISGSMRGQKVKQTKEALLKILgdmqpgDYFDLVLFGTRVqswkgSLVQAS-----EANLQAAQDF------VR 360
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLV------EKLDIGPDKTRV-----GLVQYSddvrvEFSLNDYKSKddllkaVK 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156119625 361 GFSLD--EATNLNGGLLRGIEILNQVQESlpeLSNHASILIMLTDGDPTEG--VTDRSQILKN 419
Cdd:cd01450   71 NLKYLggGGTNTGKALQYALEQLFSESNA---RENVPKVIIVLTDGRSDDGgdPKEAAAKLKD 130
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 293-411 1.62e-03

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: 40.34  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625 293 VVFVIDISGSMRG-QKVKQTKEALLKILGD---------MQP--GDYFDLVLFGTRvqswkgSLVQASeanlQAAQDFVR 360
Cdd:cd01451    3 VIFVVDASGSMAArHRMAAAKGAVLSLLRDayqrrdkvaLIAfrGTEAEVLLPPTR------SVELAK----RRLARLPT 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 156119625 361 GfsldEATNLNGGLLRGIEILNQVQESLPElsnhASILIMLTDG------DPTEGVT 411
Cdd:cd01451   73 G----GGTPLAAGLLAAYELAAEQARDPGQ----RPLIVVITDGranvgpDPTADRA 121
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 283-435 3.62e-03

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: 40.37  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625  283 PQNLTNMNKN------VVFVIDISGSMRgQKVKQTKEALLKIL-GDMQPGDYFDLVLFGTR---VQSWKGSLVQaseanL 352
Cdd:TIGR03436  40 PQTIASFRREtdlpltVGLVIDTSGSMR-NDLDRARAAAIRFLkTVLRPNDRVFVVTFNTRlrlLQDFTSDPRL-----L 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156119625  353 QAAQDFVR--GFSLDEATNLNGGLLRGIEILNQVQ-ESLPELSNHAS------ILIMLTDGDPTEGVTDRSQIlknVRNA 423
Cdd:TIGR03436 114 EAALNRLKppLRTDYNSSGAFVRDGGGTALYDAITlAALEQLANALAgipgrkALIVISDGGDNRSRDTLERA---IDAA 190

                         170
                  ....*....|..
gi 156119625  424 IRGRFPLYNLGF 435
Cdd:TIGR03436 191 QRADVAIYSIDA 202
 
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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