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Conserved domains on  [gi|74183702|dbj|BAE24467|]
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unnamed protein product [Mus musculus]

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 ...
 715-909 9.43e-81

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: 259.44  E-value: 9.43e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702   715 NSGVTVNGELIGAPAPPNGHKKQRTYFRTITILiNRPERSYLEITPSRVIL-DGGDRLVLPCNQSVVVGSRGLEVSVSAN 793
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIV-VKPLGVKIEVTPEKITLkDGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702   794 ANITVVIQGNIAFVILIHLYKNPAPFQRDHLGFYIANSRGLSDNCHGLLGQFLNqdaklvgapeEYGKNLSNQPFPRAEG 873
Cdd:pfam06668  80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLH----------EPEVEVTDVRPGSDPE 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 74183702   874 MPEAILKVKGRRVPVVWKQRKIYNGQA----QVDCWFDRN 909
Cdd:pfam06668 150 KPDATMKVKGHKLPVTRGWQKDYRGDRkhgtNVPCWFVHN 189
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 292-473 1.54e-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: 222.86  E-value: 1.54e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 292 LPKNVVFVLDISASMVGAKLQQTREALVTILNDLRPQDRFNIIGFSNRIKMWKDHLLPVTPDNIRNGKIYMYHLSPTGGT 371
Cdd:cd01461   1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 372 DINGALQAAIKLLNnyvaqndIEDRSVSLIIFLTDGKptfgETNTLKILSNTKEATRGQICIFTVGIGDDVDFKLLEKLS 451
Cdd:cd01461  81 NMNDALEAALELLN-------SSPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                       170       180
                ....*....|....*....|..
gi 74183702 452 LENCGLTRRVHEEDKAGAQLIG 473
Cdd:cd01461 150 REGRGIARRIYETDDIESQLLR 171
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 53-159 2.38e-27

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: 107.18  E-value: 2.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702    53 EFSVKSTIISRYAFTTVSCRMLNRASEDQEAEFQMQIPESAFITNFTMLIGDSVYRGEITQKD--KKSSESVKDKRNRTS 130
Cdd:pfam08487   3 SVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEeaKKEYEEAVARGKTAG 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 74183702   131 DDnEENGSDMFKASLV-IPSKDKAAFFLSY 159
Cdd:pfam08487  83 LL-EQDTPDVFTTSVGnIPPGEKVTVELTY 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 ...
 715-909 9.43e-81

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: 259.44  E-value: 9.43e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702   715 NSGVTVNGELIGAPAPPNGHKKQRTYFRTITILiNRPERSYLEITPSRVIL-DGGDRLVLPCNQSVVVGSRGLEVSVSAN 793
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIV-VKPLGVKIEVTPEKITLkDGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702   794 ANITVVIQGNIAFVILIHLYKNPAPFQRDHLGFYIANSRGLSDNCHGLLGQFLNqdaklvgapeEYGKNLSNQPFPRAEG 873
Cdd:pfam06668  80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLH----------EPEVEVTDVRPGSDPE 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 74183702   874 MPEAILKVKGRRVPVVWKQRKIYNGQA----QVDCWFDRN 909
Cdd:pfam06668 150 KPDATMKVKGHKLPVTRGWQKDYRGDRkhgtNVPCWFVHN 189
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 292-473 1.54e-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: 222.86  E-value: 1.54e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 292 LPKNVVFVLDISASMVGAKLQQTREALVTILNDLRPQDRFNIIGFSNRIKMWKDHLLPVTPDNIRNGKIYMYHLSPTGGT 371
Cdd:cd01461   1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 372 DINGALQAAIKLLNnyvaqndIEDRSVSLIIFLTDGKptfgETNTLKILSNTKEATRGQICIFTVGIGDDVDFKLLEKLS 451
Cdd:cd01461  81 NMNDALEAALELLN-------SSPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                       170       180
                ....*....|....*....|..
gi 74183702 452 LENCGLTRRVHEEDKAGAQLIG 473
Cdd:cd01461 150 REGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 277-493 9.44e-39

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 146.01  E-value: 9.44e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 277 NGYFVHYFAPKNLPP---LPKNVVFVLDISASMVGAKLQQTREALVTILNDLRPQDRFNIIGFSNRIKMwkdhLLPVTP- 352
Cdd:COG2304  72 TRLLLVGLQPPKAAAeerPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV----LLPPTPa 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 353 DNIRNGKIYMYHLSPTGGTDINGALQAAIKLLnnyvAQNDIEDRsVSLIIFLTDGKPTFGETNTLKILSNTKEATRGQIC 432
Cdd:COG2304 148 TDRAKILAAIDRLQAGGGTALGAGLELAYELA----RKHFIPGR-VNRVILLTDGDANVGITDPEELLKLAEEAREEGIT 222

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74183702 433 IFTVGIGDDVDFKLLEKLSLENCGLTRRVHEEDKAGAQLIGFYDEIRTPLLSDIRIDYPPD 493
Cdd:COG2304 223 LTTLGVGSDYNEDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPLP 283
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 53-159 2.38e-27

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: 107.18  E-value: 2.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702    53 EFSVKSTIISRYAFTTVSCRMLNRASEDQEAEFQMQIPESAFITNFTMLIGDSVYRGEITQKD--KKSSESVKDKRNRTS 130
Cdd:pfam08487   3 SVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEeaKKEYEEAVARGKTAG 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 74183702   131 DDnEENGSDMFKASLV-IPSKDKAAFFLSY 159
Cdd:pfam08487  83 LL-EQDTPDVFTTSVGnIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 295-457 2.52e-26

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 106.38  E-value: 2.52e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702    295 NVVFVLDISASMVGAKLQQTREALVTILNDLR---PQDRFNIIGFSNRIKMWKDHLLPVTPDNIRNgKIYMYHLSPTGGT 371
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSKDALLE-ALASLSYKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702    372 DINGALQAAIKLLNNYVAQNDIEDRSVslIIFLTDGKPTFGETNTLKILsntKEATRGQICIFTVGIGDDVDFKLLEKLS 451
Cdd:smart00327  80 NLGAALQYALENLFSKSAGSRRGAPKV--VILITDGESNDGPKDLLKAA---KELKRSGVKVFVVGVGNDVDEEELKKLA 154


                   ....*.
gi 74183702    452 LENCGL 457
Cdd:smart00327 155 SAPGGV 160
VWA pfam00092
von Willebrand factor type A domain;
295-454 1.22e-19

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 87.33  E-value: 1.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702   295 NVVFVLDISASMVGAKLQQTREALVTILNDL---RPQDRFNIIGFSNRIKMW--------KDHLLpvtpDNIRNGKIymy 363
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEfplndyssKEELL----SAVDNLRY--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702   364 hlSPTGGTDINGALQAAIKLLnnYVAQNDIEDRSVSLIIFLTDGKPTFGEtntlkILSNTKEATRGQICIFTVGIGDDVD 443
Cdd:pfam00092  74 --LGGGTTNTGKALKYALENL--FSSAAGARPGAPKVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNADD 144

                         170
                  ....*....|.
gi 74183702   444 fKLLEKLSLEN 454
Cdd:pfam00092 145 -EELRKIASEP 154
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
55-161 2.25e-18

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 82.02  E-value: 2.25e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702     55 SVKSTIISRYAFTTVSCRMLNRASEDQEAEFQMQIPESAFITNFTMLIGDSVYRGEItqKDKKSSESVKDK---RNRTSD 131
Cdd:smart00609  21 KVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEI--KEKEVAQKQYEKavsQGKTAG 98

                           90       100       110
                   ....*....|....*....|....*....|..
gi 74183702    132 DNEENGSDM--FKASLVIPSKDKAAFFLSYEE 161
Cdd:smart00609  99 LVRASGRSMeqFTVSVNVAPGSKVTFELTYEE 130
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 292-440 4.46e-05

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


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 46.53  E-value: 4.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702   292 LPKNVVFVLDISASMvGAKLQQTREALVTILND-LRPQDRFNIIGFSNRIKMWKD-------------HLLPVTPDNIRN 357
Cdd:TIGR03436  52 LPLTVGLVIDTSGSM-RNDLDRARAAAIRFLKTvLRPNDRVFVVTFNTRLRLLQDftsdprlleaalnRLKPPLRTDYNS 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702   358 GKIYMyhlSPTGGTDINGALQ-AAIKLLNNYVAQndIEDRSVslIIFLTDGkptFGETNTLKILSNTKEATRGQICIFTV 436
Cdd:TIGR03436 131 SGAFV---RDGGGTALYDAITlAALEQLANALAG--IPGRKA--LIVISDG---GDNRSRDTLERAIDAAQRADVAIYSI 200


                  ....
gi 74183702   437 GIGD 440
Cdd:TIGR03436 201 DARG 204
 
Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 715-909 9.43e-81

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: 259.44  E-value: 9.43e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702   715 NSGVTVNGELIGAPAPPNGHKKQRTYFRTITILiNRPERSYLEITPSRVIL-DGGDRLVLPCNQSVVVGSRGLEVSVSAN 793
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIV-VKPLGVKIEVTPEKITLkDGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702   794 ANITVVIQGNIAFVILIHLYKNPAPFQRDHLGFYIANSRGLSDNCHGLLGQFLNqdaklvgapeEYGKNLSNQPFPRAEG 873
Cdd:pfam06668  80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLH----------EPEVEVTDVRPGSDPE 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 74183702   874 MPEAILKVKGRRVPVVWKQRKIYNGQA----QVDCWFDRN 909
Cdd:pfam06668 150 KPDATMKVKGHKLPVTRGWQKDYRGDRkhgtNVPCWFVHN 189
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 292-473 1.54e-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: 222.86  E-value: 1.54e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 292 LPKNVVFVLDISASMVGAKLQQTREALVTILNDLRPQDRFNIIGFSNRIKMWKDHLLPVTPDNIRNGKIYMYHLSPTGGT 371
Cdd:cd01461   1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 372 DINGALQAAIKLLNnyvaqndIEDRSVSLIIFLTDGKptfgETNTLKILSNTKEATRGQICIFTVGIGDDVDFKLLEKLS 451
Cdd:cd01461  81 NMNDALEAALELLN-------SSPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                       170       180
                ....*....|....*....|..
gi 74183702 452 LENCGLTRRVHEEDKAGAQLIG 473
Cdd:cd01461 150 REGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 277-493 9.44e-39

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 146.01  E-value: 9.44e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 277 NGYFVHYFAPKNLPP---LPKNVVFVLDISASMVGAKLQQTREALVTILNDLRPQDRFNIIGFSNRIKMwkdhLLPVTP- 352
Cdd:COG2304  72 TRLLLVGLQPPKAAAeerPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV----LLPPTPa 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 353 DNIRNGKIYMYHLSPTGGTDINGALQAAIKLLnnyvAQNDIEDRsVSLIIFLTDGKPTFGETNTLKILSNTKEATRGQIC 432
Cdd:COG2304 148 TDRAKILAAIDRLQAGGGTALGAGLELAYELA----RKHFIPGR-VNRVILLTDGDANVGITDPEELLKLAEEAREEGIT 222

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74183702 433 IFTVGIGDDVDFKLLEKLSLENCGLTRRVHEEDKAGAQLIGFYDEIRTPLLSDIRIDYPPD 493
Cdd:COG2304 223 LTTLGVGSDYNEDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPLP 283
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 285-451 1.36e-28

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 115.93  E-value: 1.36e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 285 APKNLPPLPKNVVFVLDISASMVGAKLQQTREALVTILNDLRPQDRFNIIGFSNRIKMwkdHLLPVTPDNIRNGKIYMYH 364
Cdd:COG2425 110 ASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE---DLPLTADDGLEDAIEFLSG 186

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 365 LSPTGGTDINGALQAAIKLLNNYVAQNDIedrsvslIIFLTDGKPTFGETNTLKILsntkEATRGQICIFTVGIGDDVDF 444
Cdd:COG2425 187 LFAGGGTDIAPALRAALELLEEPDYRNAD-------IVLITDGEAGVSPEELLREV----RAKESGVRLFTVAIGDAGNP 255


                ....*..
gi 74183702 445 KLLEKLS 451
Cdd:COG2425 256 GLLEALA 262
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 53-159 2.38e-27

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: 107.18  E-value: 2.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702    53 EFSVKSTIISRYAFTTVSCRMLNRASEDQEAEFQMQIPESAFITNFTMLIGDSVYRGEITQKD--KKSSESVKDKRNRTS 130
Cdd:pfam08487   3 SVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEeaKKEYEEAVARGKTAG 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 74183702   131 DDnEENGSDMFKASLV-IPSKDKAAFFLSY 159
Cdd:pfam08487  83 LL-EQDTPDVFTTSVGnIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 295-457 2.52e-26

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 106.38  E-value: 2.52e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702    295 NVVFVLDISASMVGAKLQQTREALVTILNDLR---PQDRFNIIGFSNRIKMWKDHLLPVTPDNIRNgKIYMYHLSPTGGT 371
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSKDALLE-ALASLSYKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702    372 DINGALQAAIKLLNNYVAQNDIEDRSVslIIFLTDGKPTFGETNTLKILsntKEATRGQICIFTVGIGDDVDFKLLEKLS 451
Cdd:smart00327  80 NLGAALQYALENLFSKSAGSRRGAPKV--VILITDGESNDGPKDLLKAA---KELKRSGVKVFVVGVGNDVDEEELKKLA 154


                   ....*.
gi 74183702    452 LENCGL 457
Cdd:smart00327 155 SAPGGV 160
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 290-451 1.15e-24

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: 104.25  E-value: 1.15e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 290 PPLPKNVVFVLDISASMVG-AKLQQTREALVTILNDLRPQDRFNIIGFSNRIKMwkdhLLPVTPDnIRNGKIYMYHLSPT 368
Cdd:COG1240  89 PQRGRDVVLVVDASGSMAAeNRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEV----LLPLTRD-REALKRALDELPPG 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 369 GGTDINGALQAAIKLLnnyvAQNDIEDRSVslIIFLTDGKPTFGETNTLKILsntKEATRGQICIFTVGIGDD-VDFKLL 447
Cdd:COG1240 164 GGTPLGDALALALELL----KRADPARRKV--IVLLTDGRDNAGRIDPLEAA---ELAAAAGIRIYTIGVGTEaVDEGLL 234


                ....
gi 74183702 448 EKLS 451
Cdd:COG1240 235 REIA 238
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 295-450 5.95e-24

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: 99.65  E-value: 5.95e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 295 NVVFVLDISASMVGAKLQQTREALVTILNDLRPQDRFNIIGFSNRIKMwkdhLLPVTPDNIRnGKIY--MYHLSPTGGTD 372
Cdd:cd01465   2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAET----VLPATPVRDK-AAILaaIDRLTAGGSTA 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74183702 373 INGALQAAIKllnnyVAQNDIEDRSVSLIIFLTDGKPTFGETNTLKILSNTKEATRGQICIFTVGIGDDVDFKLLEKL 450
Cdd:cd01465  77 GGAGIQLGYQ-----EAQKHFVPGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAI 149
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 295-451 1.06e-23

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 98.41  E-value: 1.06e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 295 NVVFVLDISASMVGAKLQQTREALVTILNDL---RPQDRFNIIGFSNRIKMWKDHLLPVTPDNIRNgKIYMYHLSPTGGT 371
Cdd:cd00198   2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLsasPPGDRVGLVTFGSNARVVLPLTTDTDKADLLE-AIDALKKGLGGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 372 DINGALQAAIKLLNnyvaqNDIEDRSVSLIIFLTDGKPTFGETNTLKILsntKEATRGQICIFTVGIGDDVDFKLLEKLS 451
Cdd:cd00198  81 NIGAALRLALELLK-----SAKRPNARRVIILLTDGEPNDGPELLAEAA---RELRKLGITVYTIGIGDDANEDELKEIA 152
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
290-451 1.77e-20

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 90.37  E-value: 1.77e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 290 PPLPknVVFVLDISASMVGAKLQQTREALVTILNDLRPQD------RFNIIGFSNRIKMwkdhLLPVTPDNirngKIYMY 363
Cdd:COG4245   4 RRLP--VYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPyaletvEVSVITFDGEAKV----LLPLTDLE----DFQPP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 364 HLSPTGGTDINGALQAAIKLLNNYVAQNDIEDRSV--SLIIFLTDGKPTFGETNT-LKILSNTKEATRGQicIFTVGIGD 440
Cdd:COG4245  74 DLSASGGTPLGAALELLLDLIERRVQKYTAEGKGDwrPVVFLITDGEPTDSDWEAaLQRLKDGEAAKKAN--IFAIGVGP 151

                       170
                ....*....|.
gi 74183702 441 DVDFKLLEKLS 451
Cdd:COG4245 152 DADTEVLKQLT 162
VWA pfam00092
von Willebrand factor type A domain;
295-454 1.22e-19

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 87.33  E-value: 1.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702   295 NVVFVLDISASMVGAKLQQTREALVTILNDL---RPQDRFNIIGFSNRIKMW--------KDHLLpvtpDNIRNGKIymy 363
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEfplndyssKEELL----SAVDNLRY--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702   364 hlSPTGGTDINGALQAAIKLLnnYVAQNDIEDRSVSLIIFLTDGKPTFGEtntlkILSNTKEATRGQICIFTVGIGDDVD 443
Cdd:pfam00092  74 --LGGGTTNTGKALKYALENL--FSSAAGARPGAPKVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNADD 144

                         170
                  ....*....|.
gi 74183702   444 fKLLEKLSLEN 454
Cdd:pfam00092 145 -EELRKIASEP 154
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
55-161 2.25e-18

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 82.02  E-value: 2.25e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702     55 SVKSTIISRYAFTTVSCRMLNRASEDQEAEFQMQIPESAFITNFTMLIGDSVYRGEItqKDKKSSESVKDK---RNRTSD 131
Cdd:smart00609  21 KVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEI--KEKEVAQKQYEKavsQGKTAG 98

                           90       100       110
                   ....*....|....*....|....*....|..
gi 74183702    132 DNEENGSDM--FKASLVIPSKDKAAFFLSYEE 161
Cdd:smart00609  99 LVRASGRSMeqFTVSVNVAPGSKVTFELTYEE 130
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 296-451 6.87e-15

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: 72.81  E-value: 6.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 296 VVFVLDISASMVGAKLQQTREALVTILNDLRPQDRFNIIGFSNRIKMWKDhLLPVTPDNIRNGKIYMYHLSPTGGTDING 375
Cdd:cd01466   3 LVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSP-LRRMTAKGKRSAKRVVDGLQAGGGTNVVG 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74183702 376 ALQAAIKLLNNYVAQNdiedRSVSlIIFLTDGKPTFGEtntlkILSNTKEAtrgQICIFTVGIGDDVDFKLLEKLS 451
Cdd:cd01466  82 GLKKALKVLGDRRQKN----PVAS-IMLLSDGQDNHGA-----VVLRADNA---PIPIHTFGLGASHDPALLAFIA 144
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 293-456 2.19e-13

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


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 69.73  E-value: 2.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 293 PKNVVFVLDISASMVGAKLQQTREALVTILNDLRPQDRFNIIGFSNRIKM----WKDHLLPVTPDNIRNGKIYMYHLSPT 368
Cdd:cd01463  13 PKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPvvpcFNDTLVQATTSNKKVLKEALDMLEAK 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 369 GGTDINGALQAAIKLLNNYVAQNDIEDRSV--SLIIFLTDGkptfGETNTLKILS--NTKEATRGQICIFTVGIGDDV-D 443
Cdd:cd01463  93 GIANYTKALEFAFSLLLKNLQSNHSGSRSQcnQAIMLITDG----VPENYKEIFDkyNWDKNSEIPVRVFTYLIGREVtD 168

                       170
                ....*....|...
gi 74183702 444 FKLLEKLSLENCG 456
Cdd:cd01463 169 RREIQWMACENKG 181
VWA_3 pfam13768
von Willebrand factor type A domain;
294-451 2.93e-13

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 68.19  E-value: 2.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702   294 KNVVFVLDISASMVGAKLQQtREALVTILNDLRPQDRFNIIGFSNRIKMWKDHLLPVTPDNIRNGKIYMYHLSPT-GGTD 372
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPlGGSD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74183702   373 INGALQAAIKLLNnyvaqndiEDRSVSLIIFLTDGKPTFGETNTLKILSntkeATRGQICIFTVGIGDDVDFKLLEKLS 451
Cdd:pfam13768  80 LLGALKEAVRAPA--------SPGYIRHVLLLTDGSPMQGETRVSDLIS----RAPGKIRFFAYGLGASISAPMLQLLA 146
VWA_2 pfam13519
von Willebrand factor type A domain;
296-386 1.01e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 53.84  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702   296 VVFVLDISASMVGAKLQQTR-EALVTILNDL---RPQDRFNIIGFSNRIKmwkdHLLPVTPDN------IRNGKIYmyhl 365
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRlEAAKDAVLALlksLPGDRVGLVTFGDGPE----VLIPLTKDRakilraLRRLEPK---- 72

                          90       100
                  ....*....|....*....|.
gi 74183702   366 spTGGTDINGALQAAIKLLNN 386
Cdd:pfam13519  73 --GGGTNLAAALQLARAALKH 91
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 292-451 6.12e-08

VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 53.50  E-value: 6.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 292 LPknVVFVLDISASMVGAKLQQTREALVTILNDLRpQDRF-------NIIGFSNRIKMwkdhLLPVTP-DNirngkIYMY 363
Cdd:cd01464   4 LP--IYLLLDTSGSMAGEPIEALNQGLQMLQSELR-QDPYalesveiSVITFDSAARV----IVPLTPlES-----FQPP 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 364 HLSPTGGTDINGALQAAIKLLNNYVAQNDIEDRSV--SLIIFLTDGKPTFGETNTLKILSNTKEATRGqicIFTVGIGDD 441
Cdd:cd01464  72 RLTASGGTSMGAALELALDCIDRRVQRYRADQKGDwrPWVFLLTDGEPTDDLTAAIERIKEARDSKGR---IVACAVGPK 148

                       170
                ....*....|
gi 74183702 442 VDFKLLEKLS 451
Cdd:cd01464 149 ADLDTLKQIT 158
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 295-451 1.67e-07

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: 51.91  E-value: 1.67e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 295 NVVFVLDISASMVGAKLQQTREALVTILNDLRP---QDRFNIIGFSNRIKMW--------KDHLLpVTPDNIRngkiYMY 363
Cdd:cd01450   2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIgpdKTRVGLVQYSDDVRVEfslndyksKDDLL-KAVKNLK----YLG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 364 HlsptGGTDINGALQAAiklLNNYVAQNDIEDRSVSLIIFLTDGKPTfGETNTLKILSNTKEAtrgQICIFTVGIGdDVD 443
Cdd:cd01450  77 G----GGTNTGKALQYA---LEQLFSESNARENVPKVIIVLTDGRSD-DGGDPKEAAAKLKDE---GIKVFVVGVG-PAD 144


                ....*...
gi 74183702 444 FKLLEKLS 451
Cdd:cd01450 145 EEELREIA 152
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 287-450 4.49e-06

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


Pssm-ID: 238733 [Multi-domain]  Cd Length: 206  Bit Score: 48.58  E-value: 4.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 287 KNLPPLPKNVVFVLDISASMVGA------KLQQTREALVTILNDLRPQDRFNIIGFSNRIKMWKDH--LLPVTPDNIRNG 358
Cdd:cd01456  14 ETEPQLPPNVAIVLDNSGSMREVdgggetRLDNAKAALDETANALPDGTRLGLWTFSGDGDNPLDVrvLVPKGCLTAPVN 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 359 KIYMYHLS-----------PTGGTDINGALQAAIKllnnyvaqnDIEDRSVSLIIFLTDGKPTfGETNTLKIL--SNTKE 425
Cdd:cd01456  94 GFPSAQRSaldaalnslqtPTGWTPLAAALAEAAA---------YVDPGRVNVVVLITDGEDT-CGPDPCEVAreLAKRR 163

                       170       180
                ....*....|....*....|....*
gi 74183702 426 ATRGQICIFTVGIGDDVDFKLLEKL 450
Cdd:cd01456 164 TPAPPIKVNVIDFGGDADRAELEAI 188
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 292-440 4.46e-05

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


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 46.53  E-value: 4.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702   292 LPKNVVFVLDISASMvGAKLQQTREALVTILND-LRPQDRFNIIGFSNRIKMWKD-------------HLLPVTPDNIRN 357
Cdd:TIGR03436  52 LPLTVGLVIDTSGSM-RNDLDRARAAAIRFLKTvLRPNDRVFVVTFNTRLRLLQDftsdprlleaalnRLKPPLRTDYNS 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702   358 GKIYMyhlSPTGGTDINGALQ-AAIKLLNNYVAQndIEDRSVslIIFLTDGkptFGETNTLKILSNTKEATRGQICIFTV 436
Cdd:TIGR03436 131 SGAFV---RDGGGTALYDAITlAALEQLANALAG--IPGRKA--LIVISDG---GDNRSRDTLERAIDAAQRADVAIYSI 200


                  ....
gi 74183702   437 GIGD 440
Cdd:TIGR03436 201 DARG 204
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 295-442 2.99e-04

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 42.70  E-value: 2.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 295 NVVFVLDISASM------VGAKLQQTREALVTILNDlRPQDRFNIIGFSNRIKMwkdhLLPVTPDNIRNGKIY--MYHLS 366
Cdd:cd01467   4 DIMIALDVSGSMlaqdfvKPSRLEAAKEVLSDFIDR-RENDRIGLVVFAGAAFT----QAPLTLDRESLKELLedIKIGL 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74183702 367 PTGGTDINGALQAAIKLLNNYVAQNDIedrsvslIIFLTDGKPTFGETNTLKILSNTKEatRGqICIFTVGIGDDV 442
Cdd:cd01467  79 AGQGTAIGDAIGLAIKRLKNSEAKERV-------IVLLTDGENNAGEIDPATAAELAKN--KG-VRIYTIGVGKSG 144
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 296-412 7.98e-04

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: 41.49  E-value: 7.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 296 VVFVLDISASMVGA-KLQQTREALVTILND-LRPQDRFNIIGFSNRIkmwKDHLLPVTpDNIRNGKIYMYHLSPTGGTDI 373
Cdd:cd01451   3 VIFVVDASGSMAARhRMAAAKGAVLSLLRDaYQRRDKVALIAFRGTE---AEVLLPPT-RSVELAKRRLARLPTGGGTPL 78

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 74183702 374 NGALQAAIKLLNNYVAQNDIedrsVSLIIFLTDGKPTFG 412
Cdd:cd01451  79 AAGLLAAYELAAEQARDPGQ----RPLIVVITDGRANVG 113
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 296-451 1.83e-03

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


Pssm-ID: 238731 [Multi-domain]  Cd Length: 174  Bit Score: 40.39  E-value: 1.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 296 VVFVLDISASMVGA-KLQQTREALVTILNDL-RPQDRFNIIGFSNRIKM--WKDHLLPVTPDNI---RNGKIYMyHLSPT 368
Cdd:cd01454   3 VTLLLDLSGSMRSDrRIDVAKKAAVLLAEALeACGVPHAILGFTTDAGGreRVRWIKIKDFDESlheRARKRLA-ALSPG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 369 GGTDINGALQAAIKLLNnyvAQNdiEDRsvSLIIFLTDGKPTFGETNTLKI------LSNTKEATRGQICIFTVGIGDDV 442
Cdd:cd01454  82 GNTRDGAAIRHAAERLL---ARP--EKR--KILLVISDGEPNDLDYYEGNVfatedaLRAVIEARKLGIEVFGITIDRDA 154


                ....*....
gi 74183702 443 DFKLLEKLS 451
Cdd:cd01454 155 TTVDKEYLK 163
YeaD2 COG1721
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];
295-406 1.85e-03

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


Pssm-ID: 441327 [Multi-domain]  Cd Length: 287  Bit Score: 41.35  E-value: 1.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183702 295 NVVFVLDISASM-----VGAKLQQTREALVTILND-LRPQDRFNIIGFSNRIKMW------KDHLLPVtpdnIRngkiYM 362
Cdd:COG1721 149 TVVLLLDTSASMrfgsgGPSKLDLAVEAAASLAYLaLRQGDRVGLLTFGDRVRRYlpprrgRRHLLRL----LE----AL 220

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 74183702 363 YHLSPTGGTDINGALQAAIKLLnnyvaqndiedRSVSLIIFLTD 406
Cdd:COG1721 221 ARLEPAGETDLAAALRRLARRL-----------PRRSLVVLISD 253
 
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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