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Conserved domains on  [gi|767960624|ref|XP_011518015|]
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inter-alpha-trypsin inhibitor heavy chain H5 isoform X1 [Homo sapiens]

Protein Classification

vWA_interalpha_trypsin_inhibitor and ITI_HC_C domain-containing protein( domain architecture ID 10553341)

protein containing domains VIT, vWA_interalpha_trypsin_inhibitor, and ITI_HC_C

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 ...
 740-934 9.71e-85

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: 270.61  E-value: 9.71e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624  740 DSGVTVNGELIGAPAPPNGHKKQRTYLRTITILiNKPERSYLEITPSRVIL-DGGDRLVLPCNQSVVVGSWGLEVSVSAN 818
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIV-VKPLGVKIEVTPEKITLkDGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624  819 ANVTVTIQGSIAFVILIHLYKKPAPFQRHHLGFYIANSEGLSSNCHGLLGQFLNQ-DARLTEDPAGpsqnlthplllQVG 897
Cdd:pfam06668  80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEpEVEVTDVRPG-----------SDP 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767960624  898 EGPEAVLTVKGHQVPVVWKQRKIYNGE----EQIDCWFARN 934
Cdd:pfam06668 149 EKPDATMKVKGHKLPVTRGWQKDYRGDrkhgTNVPCWFVHN 189
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 292-498 2.51e-67

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: 222.48  E-value: 2.51e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 292 LPKNVVFVLDSSASMVGTKLRQdigfslavqnwvpkgyldiscvtlqTKDALFTILHDLRPQDRFSIIGFSNRIKVWKDH 371
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQ-------------------------TKEALLTALKDLPPGDYFNIIGFSDTVEEFSPS 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 372 LISVTPDSIRDGKVYIHHMSPTGGTDINGALQRAIRLLNKyvahsgiGDRSVSLIVFLTDGKptvgETHTLKILNNTREA 451
Cdd:cd01461   56 SVSATAENVAAAIEYVNRLQALGGTNMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREA 124

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767960624 452 ARGQVCIFTIGIGNDVDFRLLEKLSLENCGLTRRVHEEEDAGSQLIG 498
Cdd:cd01461  125 LSGRIRLFTFGIGSDVNTYLLERLAREGRGIARRIYETDDIESQLLR 171
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 51-159 6.10e-29

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: 111.81  E-value: 6.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624   51 MTEFSVKSTIISRYAFTTVSCRMLNRASEDQDIEFQMQIPAAAFITNFTMLIGDKVYQGEITEREKKSGDRVKEKRNKTT 130
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 767960624  131 EENGEK-GTEIFRAS-AVIPSKDKAAFFLSY 159
Cdd:pfam08487  81 AGLLEQdTPDVFTTSvGNIPPGEKVTVELTY 111
 
Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 740-934 9.71e-85

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: 270.61  E-value: 9.71e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624  740 DSGVTVNGELIGAPAPPNGHKKQRTYLRTITILiNKPERSYLEITPSRVIL-DGGDRLVLPCNQSVVVGSWGLEVSVSAN 818
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIV-VKPLGVKIEVTPEKITLkDGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624  819 ANVTVTIQGSIAFVILIHLYKKPAPFQRHHLGFYIANSEGLSSNCHGLLGQFLNQ-DARLTEDPAGpsqnlthplllQVG 897
Cdd:pfam06668  80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEpEVEVTDVRPG-----------SDP 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767960624  898 EGPEAVLTVKGHQVPVVWKQRKIYNGE----EQIDCWFARN 934
Cdd:pfam06668 149 EKPDATMKVKGHKLPVTRGWQKDYRGDrkhgTNVPCWFVHN 189
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 292-498 2.51e-67

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: 222.48  E-value: 2.51e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 292 LPKNVVFVLDSSASMVGTKLRQdigfslavqnwvpkgyldiscvtlqTKDALFTILHDLRPQDRFSIIGFSNRIKVWKDH 371
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQ-------------------------TKEALLTALKDLPPGDYFNIIGFSDTVEEFSPS 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 372 LISVTPDSIRDGKVYIHHMSPTGGTDINGALQRAIRLLNKyvahsgiGDRSVSLIVFLTDGKptvgETHTLKILNNTREA 451
Cdd:cd01461   56 SVSATAENVAAAIEYVNRLQALGGTNMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREA 124

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767960624 452 ARGQVCIFTIGIGNDVDFRLLEKLSLENCGLTRRVHEEEDAGSQLIG 498
Cdd:cd01461  125 LSGRIRLFTFGIGSDVNTYLLERLAREGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 277-517 5.91e-33

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 129.45  E-value: 5.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 277 NGYFVHYFAPKDLPP---LPKNVVFVLDSSASMVGTKLRQdigfslavqnwvpkgyldiscvtlqTKDALFTILHDLRPQ 353
Cdd:COG2304   72 TRLLLVGLQPPKAAAeerPPLNLVFVIDVSGSMSGDKLEL-------------------------AKEAAKLLVDQLRPG 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 354 DRFSIIGFSNRIKVwkdhLISVTP-DSIRDGKVYIHHMSPTGGTDINGALQRAIRLLNKYvahsGIGDRsVSLIVFLTDG 432
Cdd:COG2304  127 DRVSIVTFAGDARV----LLPPTPaTDRAKILAAIDRLQAGGGTALGAGLELAYELARKH----FIPGR-VNRVILLTDG 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 433 KPTVGETHTLKILNNTREAARGQVCIFTIGIGNDVDFRLLEKLSLENCGLTRRVHEEEDAGSQLIGFYDEIRTPLLSDIR 512
Cdd:COG2304  198 DANVGITDPEELLKLAEEAREEGITLTTLGVGSDYNEDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALAT 277


                 ....*
gi 767960624 513 IDYPP 517
Cdd:COG2304  278 EDFPL 282
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 51-159 6.10e-29

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: 111.81  E-value: 6.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624   51 MTEFSVKSTIISRYAFTTVSCRMLNRASEDQDIEFQMQIPAAAFITNFTMLIGDKVYQGEITEREKKSGDRVKEKRNKTT 130
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 767960624  131 EENGEK-GTEIFRAS-AVIPSKDKAAFFLSY 159
Cdd:pfam08487  81 AGLLEQdTPDVFTTSvGNIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 295-492 1.52e-22

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: 95.60  E-value: 1.52e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624   295 NVVFVLDSSASMVGTKLRQdigfslavqnwvpkgyldiscvtlqTKDALFTILHDLR---PQDRFSIIGFSNRIKVWKDH 371
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFEL-------------------------AKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPL 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624   372 LISVTPDSIRDgkvYIHHMSPT--GGTDINGALQRAIRLLNKYVAHSGIGDRSVslIVFLTDGKPTVGETHTLKILnntR 449
Cdd:smart00327  56 NDSRSKDALLE---ALASLSYKlgGGTNLGAALQYALENLFSKSAGSRRGAPKV--VILITDGESNDGPKDLLKAA---K 127

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 767960624   450 EAARGQVCIFTIGIGNDVDFRLLEKLSLENCGltRRVHEEEDA 492
Cdd:smart00327 128 ELKRSGVKVFVVGVGNDVDEEELKKLASAPGG--VYVFLPELL 168
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
55-161 8.24e-18

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 80.48  E-value: 8.24e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624    55 SVKSTIISRYAFTTVSCRMLNRASEDQDIEFQMQIPAAAFITNFTMLIGDKVYQGEITEREKK----SGDRVKEKRNKTT 130
Cdd:smart00609  21 KVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEVAqkqyEKAVSQGKTAGLV 100

                           90       100       110
                   ....*....|....*....|....*....|.
gi 767960624   131 EENGEKgTEIFRASAVIPSKDKAAFFLSYEE 161
Cdd:smart00609 101 RASGRS-MEQFTVSVNVAPGSKVTFELTYEE 130
VWA pfam00092
von Willebrand factor type A domain;
295-479 1.86e-15

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 75.00  E-value: 1.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624  295 NVVFVLDSSASMVGTKLRQdigfslavqnwvpkgyldiscvtlqTKDALFTILHDL---RPQDRFSIIGFSNRIKVW--- 368
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEK-------------------------VKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEfpl 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624  369 -----KDHLISvtpdSIRDGKVyihhmSPTGGTDINGALQRAIRLLNKYVAHSGIGDRSVslIVFLTDGKPTVGEthtlk 443
Cdd:pfam00092  56 ndyssKEELLS----AVDNLRY-----LGGGTTNTGKALKYALENLFSSAAGARPGAPKV--VVLLTDGRSQDGD----- 119

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767960624  444 ILNNTREAARGQVCIFTIGIGNDVDfRLLEKLSLEN 479
Cdd:pfam00092 120 PEEVARELKSAGVTVFAVGVGNADD-EELRKIASEP 154
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 292-471 8.60e-04

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


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 42.29  E-value: 8.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624  292 LPKNVVFVLDSSASMvgtklRQDIGFSlavqnwvpkgyldiscvtlqtKDALFTIL-HDLRPQDRFSIIGFSNR------ 364
Cdd:TIGR03436  52 LPLTVGLVIDTSGSM-----RNDLDRA---------------------RAAAIRFLkTVLRPNDRVFVVTFNTRlrllqd 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624  365 ----IKVWKDHLISVTPDSIRDGKVYIHHMSPTGGTdingALQRAIRL--LNKYVAH-SGIGDRSVsLIVFlTDGkptVG 437
Cdd:TIGR03436 106 ftsdPRLLEAALNRLKPPLRTDYNSSGAFVRDGGGT----ALYDAITLaaLEQLANAlAGIPGRKA-LIVI-SDG---GD 176

                         170       180       190
                  ....*....|....*....|....*....|....
gi 767960624  438 ETHTLKILNNTREAARGQVCIFTIGIGNDVDFRL 471
Cdd:TIGR03436 177 NRSRDTLERAIDAAQRADVAIYSIDARGLRAPDL 210
 
Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 740-934 9.71e-85

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: 270.61  E-value: 9.71e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624  740 DSGVTVNGELIGAPAPPNGHKKQRTYLRTITILiNKPERSYLEITPSRVIL-DGGDRLVLPCNQSVVVGSWGLEVSVSAN 818
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIV-VKPLGVKIEVTPEKITLkDGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624  819 ANVTVTIQGSIAFVILIHLYKKPAPFQRHHLGFYIANSEGLSSNCHGLLGQFLNQ-DARLTEDPAGpsqnlthplllQVG 897
Cdd:pfam06668  80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEpEVEVTDVRPG-----------SDP 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767960624  898 EGPEAVLTVKGHQVPVVWKQRKIYNGE----EQIDCWFARN 934
Cdd:pfam06668 149 EKPDATMKVKGHKLPVTRGWQKDYRGDrkhgTNVPCWFVHN 189
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 292-498 2.51e-67

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: 222.48  E-value: 2.51e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 292 LPKNVVFVLDSSASMVGTKLRQdigfslavqnwvpkgyldiscvtlqTKDALFTILHDLRPQDRFSIIGFSNRIKVWKDH 371
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQ-------------------------TKEALLTALKDLPPGDYFNIIGFSDTVEEFSPS 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 372 LISVTPDSIRDGKVYIHHMSPTGGTDINGALQRAIRLLNKyvahsgiGDRSVSLIVFLTDGKptvgETHTLKILNNTREA 451
Cdd:cd01461   56 SVSATAENVAAAIEYVNRLQALGGTNMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREA 124

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767960624 452 ARGQVCIFTIGIGNDVDFRLLEKLSLENCGLTRRVHEEEDAGSQLIG 498
Cdd:cd01461  125 LSGRIRLFTFGIGSDVNTYLLERLAREGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 277-517 5.91e-33

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 129.45  E-value: 5.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 277 NGYFVHYFAPKDLPP---LPKNVVFVLDSSASMVGTKLRQdigfslavqnwvpkgyldiscvtlqTKDALFTILHDLRPQ 353
Cdd:COG2304   72 TRLLLVGLQPPKAAAeerPPLNLVFVIDVSGSMSGDKLEL-------------------------AKEAAKLLVDQLRPG 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 354 DRFSIIGFSNRIKVwkdhLISVTP-DSIRDGKVYIHHMSPTGGTDINGALQRAIRLLNKYvahsGIGDRsVSLIVFLTDG 432
Cdd:COG2304  127 DRVSIVTFAGDARV----LLPPTPaTDRAKILAAIDRLQAGGGTALGAGLELAYELARKH----FIPGR-VNRVILLTDG 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 433 KPTVGETHTLKILNNTREAARGQVCIFTIGIGNDVDFRLLEKLSLENCGLTRRVHEEEDAGSQLIGFYDEIRTPLLSDIR 512
Cdd:COG2304  198 DANVGITDPEELLKLAEEAREEGITLTTLGVGSDYNEDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALAT 277


                 ....*
gi 767960624 513 IDYPP 517
Cdd:COG2304  278 EDFPL 282
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 51-159 6.10e-29

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: 111.81  E-value: 6.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624   51 MTEFSVKSTIISRYAFTTVSCRMLNRASEDQDIEFQMQIPAAAFITNFTMLIGDKVYQGEITEREKKSGDRVKEKRNKTT 130
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 767960624  131 EENGEK-GTEIFRAS-AVIPSKDKAAFFLSY 159
Cdd:pfam08487  81 AGLLEQdTPDVFTTSvGNIPPGEKVTVELTY 111
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 290-476 1.12e-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: 98.60  E-value: 1.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 290 PPLPKNVVFVLDSSASMVGTKLRqdigfslavqnwvpkgyldiscvtlQTKDALFTILHDLRPQDRFSIIGFSNRIKVwk 369
Cdd:COG2425  115 PLLEGPVVLCVDTSGSMAGSKEA-------------------------AAKAAALALLRALRPNRRFGVILFDTEVVE-- 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 370 dHLISVTPDSIRDGKVYIHHMSPTGGTDINGALQRAIRLLNKYVAHSGIgdrsvslIVFLTDGKPTVGETHTLKILNntr 449
Cdd:COG2425  168 -DLPLTADDGLEDAIEFLSGLFAGGGTDIAPALRAALELLEEPDYRNAD-------IVLITDGEAGVSPEELLREVR--- 236

                        170       180
                 ....*....|....*....|....*..
gi 767960624 450 eAARGQVCIFTIGIGNDVDFRLLEKLS 476
Cdd:COG2425  237 -AKESGVRLFTVAIGDAGNPGLLEALA 262
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 295-492 1.52e-22

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: 95.60  E-value: 1.52e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624   295 NVVFVLDSSASMVGTKLRQdigfslavqnwvpkgyldiscvtlqTKDALFTILHDLR---PQDRFSIIGFSNRIKVWKDH 371
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFEL-------------------------AKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPL 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624   372 LISVTPDSIRDgkvYIHHMSPT--GGTDINGALQRAIRLLNKYVAHSGIGDRSVslIVFLTDGKPTVGETHTLKILnntR 449
Cdd:smart00327  56 NDSRSKDALLE---ALASLSYKlgGGTNLGAALQYALENLFSKSAGSRRGAPKV--VILITDGESNDGPKDLLKAA---K 127

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 767960624   450 EAARGQVCIFTIGIGNDVDFRLLEKLSLENCGltRRVHEEEDA 492
Cdd:smart00327 128 ELKRSGVKVFVVGVGNDVDEEELKKLASAPGG--VYVFLPELL 168
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 290-476 5.08e-21

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: 93.85  E-value: 5.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 290 PPLPKNVVFVLDSSASMVG-TKLRQdigfslavqnwvpkgyldiscvtlqTKDALFTILHDLRPQDRFSIIGFSNRIKVw 368
Cdd:COG1240   89 PQRGRDVVLVVDASGSMAAeNRLEA-------------------------AKGALLDFLDDYRPRDRVGLVAFGGEAEV- 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 369 kdhLISVTPDsIRDGKVYIHHMSPTGGTDINGALQRAIRLLNKYvahsgiGDRSVSLIVFLTDGKPTVGETHTLKILnnt 448
Cdd:COG1240  143 ---LLPLTRD-REALKRALDELPPGGGTPLGDALALALELLKRA------DPARRKVIVLLTDGRDNAGRIDPLEAA--- 209

                        170       180
                 ....*....|....*....|....*....
gi 767960624 449 REAARGQVCIFTIGIGND-VDFRLLEKLS 476
Cdd:COG1240  210 ELAAAAGIRIYTIGVGTEaVDEGLLREIA 238
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 295-476 1.12e-18

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: 84.15  E-value: 1.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 295 NVVFVLDSSASMVGTKLRqdigfslavqnwvpkgyldiscvtlQTKDALFTILHDL---RPQDRFSIIGFSNRIKVWKDH 371
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLD-------------------------KAKEALKALVSSLsasPPGDRVGLVTFGSNARVVLPL 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 372 LISVTPDSIRDGKVYIHHmSPTGGTDINGALQRAIRLLNKYvahsgIGDRSVSLIVFLTDGKPTVGETHTLKILNNTREA 451
Cdd:cd00198   57 TTDTDKADLLEAIDALKK-GLGGGTNIGAALRLALELLKSA-----KRPNARRVIILLTDGEPNDGPELLAEAARELRKL 130

                        170       180
                 ....*....|....*....|....*
gi 767960624 452 argQVCIFTIGIGNDVDFRLLEKLS 476
Cdd:cd00198  131 ---GITVYTIGIGDDANEDELKEIA 152
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
55-161 8.24e-18

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 80.48  E-value: 8.24e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624    55 SVKSTIISRYAFTTVSCRMLNRASEDQDIEFQMQIPAAAFITNFTMLIGDKVYQGEITEREKK----SGDRVKEKRNKTT 130
Cdd:smart00609  21 KVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEVAqkqyEKAVSQGKTAGLV 100

                           90       100       110
                   ....*....|....*....|....*....|.
gi 767960624   131 EENGEKgTEIFRASAVIPSKDKAAFFLSYEE 161
Cdd:smart00609 101 RASGRS-MEQFTVSVNVAPGSKVTFELTYEE 130
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
290-476 4.47e-17

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 80.35  E-value: 4.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 290 PPLPknVVFVLDSSASMVGTKLRQdigfslavqnwvpkgyldiscvtlqTKDALFTILHDLRPQD------RFSIIGFSN 363
Cdd:COG4245    4 RRLP--VYLLLDTSGSMSGEPIEA-------------------------LNEGLQALIDELRQDPyaletvEVSVITFDG 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 364 RIKVwkdhlisVTPDSIRDgKVYIHHMSPTGGTDINGALQRAIRLLNKYVAHS---GIGDRSVsLIVFLTDGKPTVGETH 440
Cdd:COG4245   57 EAKV-------LLPLTDLE-DFQPPDLSASGGTPLGAALELLLDLIERRVQKYtaeGKGDWRP-VVFLITDGEPTDSDWE 127

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767960624 441 T-LKILNNTREAARGQvcIFTIGIGNDVDFRLLEKLS 476
Cdd:COG4245  128 AaLQRLKDGEAAKKAN--IFAIGVGPDADTEVLKQLT 162
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 295-475 5.97e-17

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: 79.24  E-value: 5.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 295 NVVFVLDSSASMVGTKLRQdigfslavqnwvpkgyldiscvtlqTKDALFTILHDLRPQDRFSIIGFSNRIKVwkdhLIS 374
Cdd:cd01465    2 NLVFVIDRSGSMDGPKLPL-------------------------VKSALKLLVDQLRPDDRLAIVTYDGAAET----VLP 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 375 VTP----DSIRDGkvyIHHMSPTGGTDINGALQRAIRLLNKyvahsGIGDRSVSLIVFLTDGKPTVGETHTLKILNNTRE 450
Cdd:cd01465   53 ATPvrdkAAILAA---IDRLTAGGSTAGGAGIQLGYQEAQK-----HFVPGGVNRILLATDGDFNVGETDPDELARLVAQ 124

                        170       180
                 ....*....|....*....|....*
gi 767960624 451 AARGQVCIFTIGIGNDVDFRLLEKL 475
Cdd:cd01465  125 KRESGITLSTLGFGDNYNEDLMEAI 149
VWA pfam00092
von Willebrand factor type A domain;
295-479 1.86e-15

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 75.00  E-value: 1.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624  295 NVVFVLDSSASMVGTKLRQdigfslavqnwvpkgyldiscvtlqTKDALFTILHDL---RPQDRFSIIGFSNRIKVW--- 368
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEK-------------------------VKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEfpl 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624  369 -----KDHLISvtpdSIRDGKVyihhmSPTGGTDINGALQRAIRLLNKYVAHSGIGDRSVslIVFLTDGKPTVGEthtlk 443
Cdd:pfam00092  56 ndyssKEELLS----AVDNLRY-----LGGGTTNTGKALKYALENLFSSAAGARPGAPKV--VVLLTDGRSQDGD----- 119

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767960624  444 ILNNTREAARGQVCIFTIGIGNDVDfRLLEKLSLEN 479
Cdd:pfam00092 120 PEEVARELKSAGVTVFAVGVGNADD-EELRKIASEP 154
VWA_3 pfam13768
von Willebrand factor type A domain;
294-476 9.21e-14

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 69.73  E-value: 9.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624  294 KNVVFVLDSSASMVGtklrqdigfslavqnwvpkgyldisCVTLQtKDALFTILHDLRPQDRFSIIGFSNRIKVWKDHLI 373
Cdd:pfam13768   1 GDVVIVVDVSSSMSG-------------------------EPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWR 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624  374 SVTPDSIRDGKVYIHHMSPT-GGTDINGALQRAIRLLnkyvAHSGIgdrsVSLIVFLTDGKPTVGETHTLKILnntrEAA 452
Cdd:pfam13768  55 VVSPRSLQEAFQFIKTLQPPlGGSDLLGALKEAVRAP----ASPGY----IRHVLLLTDGSPMQGETRVSDLI----SRA 122

                         170       180
                  ....*....|....*....|....
gi 767960624  453 RGQVCIFTIGIGNDVDFRLLEKLS 476
Cdd:pfam13768 123 PGKIRFFAYGLGASISAPMLQLLA 146
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 293-481 7.16e-10

VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex.


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 59.33  E-value: 7.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 293 PKNVVFVLDSSASMVGtkLRQDIGfslavqnwvpkgyldiscvtlqtKDALFTILHDLRPQDRFSIIGFSNRIK----VW 368
Cdd:cd01463   13 PKDIVILLDVSGSMTG--QRLHLA-----------------------KQTVSSILDTLSDNDFFNIITFSNEVNpvvpCF 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 369 KDHLISVTPDSIRDGKVYIHHMSPTGGTDINGALQRAIRLLNKYVAHSGIGDRSV--SLIVFLTDGKPtvgETHTlKILN 446
Cdd:cd01463   68 NDTLVQATTSNKKVLKEALDMLEAKGIANYTKALEFAFSLLLKNLQSNHSGSRSQcnQAIMLITDGVP---ENYK-EIFD 143

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767960624 447 --NTREAARGQVCIFTIGIGNDV-DFRLLEKLSLENCG 481
Cdd:cd01463  144 kyNWDKNSEIPVRVFTYLIGREVtDRREIQWMACENKG 181
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 296-476 2.30e-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: 54.32  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 296 VVFVLDSSASMVGTKLRQdigfslavqnwvpkgyldiscvtlqTKDALFTILHDLRPQDRFSIIGFSNRIKVWKDhLISV 375
Cdd:cd01466    3 LVAVLDVSGSMAGDKLQL-------------------------VKHALRFVISSLGDADRLSIVTFSTSAKRLSP-LRRM 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 376 TPDSIRDGKVYIHHMSPTGGTDINGALQRAIRLLNKyvahSGIGDRSVSLIVfLTDGKPTVGETHTlkilnntrEAARGQ 455
Cdd:cd01466   57 TAKGKRSAKRVVDGLQAGGGTNVVGGLKKALKVLGD----RRQKNPVASIML-LSDGQDNHGAVVL--------RADNAP 123

                        170       180
                 ....*....|....*....|.
gi 767960624 456 VCIFTIGIGNDVDFRLLEKLS 476
Cdd:cd01466  124 IPIHTFGLGASHDPALLAFIA 144
VWA_2 pfam13519
von Willebrand factor type A domain;
296-411 3.14e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 49.60  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624  296 VVFVLDSSASMVGTKLRQDIgFSLAvqnwvpkgyldiscvtlqtKDALFTILHDLrPQDRFSIIGFSNRIKVwkdhLISV 375
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTR-LEAA-------------------KDAVLALLKSL-PGDRVGLVTFGDGPEV----LIPL 55

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767960624  376 TpDSIRDGKVYIHHMSPT-GGTDINGALQRAIRLLNK 411
Cdd:pfam13519  56 T-KDRAKILRALRRLEPKgGGTNLAAALQLARAALKH 91
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 295-476 1.26e-05

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: 46.52  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 295 NVVFVLDSSASMVGTKLRQDIGFslaVQNWVPKgyldiscvtlqtkdalFTILHDlrpQDRFSIIGFSNRIKVW------ 368
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDF---IEKLVEK----------------LDIGPD---KTRVGLVQYSDDVRVEfslndy 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 369 --KDHLISvtpdSIRDgkvyIHHMSPtGGTDINGALQRAIRLLNKyvaHSGIGDRSVSLIVFLTDGKPTVGEthtlKILN 446
Cdd:cd01450   60 ksKDDLLK----AVKN----LKYLGG-GGTNTGKALQYALEQLFS---ESNARENVPKVIIVLTDGRSDDGG----DPKE 123

                        170       180       190
                 ....*....|....*....|....*....|
gi 767960624 447 NTREAARGQVCIFTIGIGnDVDFRLLEKLS 476
Cdd:cd01450  124 AAAKLKDEGIKVFVVGVG-PADEEELREIA 152
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 292-476 6.02e-05

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: 44.64  E-value: 6.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 292 LPknVVFVLDSSASMVGTKLRqdigfslavqnwvpkgyldiscvtlQTKDALFTILHDLRpQDRF-------SIIGFSNR 364
Cdd:cd01464    4 LP--IYLLLDTSGSMAGEPIE-------------------------ALNQGLQMLQSELR-QDPYalesveiSVITFDSA 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 365 IKVWKDhLISVTpdsirdgKVYIHHMSPTGGTDINGALQRAIRLLN----KYVAhSGIGDRSvSLIVFLTDGKPTVGETH 440
Cdd:cd01464   56 ARVIVP-LTPLE-------SFQPPRLTASGGTSMGAALELALDCIDrrvqRYRA-DQKGDWR-PWVFLLTDGEPTDDLTA 125

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767960624 441 TLKILnntREAARGQVCIFTIGIGNDVDFRLLEKLS 476
Cdd:cd01464  126 AIERI---KEARDSKGRIVACAVGPKADLDTLKQIT 158
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 352-463 5.43e-04

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 42.11  E-value: 5.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624 352 PQDRFSIIGFSNRIKVwkdhLISVTPDS--IRDGKVYIHHMSPTGGTDINGALQRAirllNKYVAHSGIGDR-SVSLIVF 428
Cdd:cd01474   38 PGLRFSFITFSTRATK----ILPLTDDSsaIIKGLEVLKKVTPSGQTYIHEGLENA----NEQIFNRNGGGReTVSVIIA 109

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767960624 429 LTDgkptvGETHTLKILNNTREAARGQ---VCIFTIGI 463
Cdd:cd01474  110 LTD-----GQLLLNGHKYPEHEAKLSRklgAIVYCVGV 142
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 292-471 8.60e-04

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


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 42.29  E-value: 8.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624  292 LPKNVVFVLDSSASMvgtklRQDIGFSlavqnwvpkgyldiscvtlqtKDALFTIL-HDLRPQDRFSIIGFSNR------ 364
Cdd:TIGR03436  52 LPLTVGLVIDTSGSM-----RNDLDRA---------------------RAAAIRFLkTVLRPNDRVFVVTFNTRlrllqd 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960624  365 ----IKVWKDHLISVTPDSIRDGKVYIHHMSPTGGTdingALQRAIRL--LNKYVAH-SGIGDRSVsLIVFlTDGkptVG 437
Cdd:TIGR03436 106 ftsdPRLLEAALNRLKPPLRTDYNSSGAFVRDGGGT----ALYDAITLaaLEQLANAlAGIPGRKA-LIVI-SDG---GD 176

                         170       180       190
                  ....*....|....*....|....*....|....
gi 767960624  438 ETHTLKILNNTREAARGQVCIFTIGIGNDVDFRL 471
Cdd:TIGR03436 177 NRSRDTLERAIDAAQRADVAIYSIDARGLRAPDL 210
 
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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