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Conserved domains on  [gi|341940373|sp|P21180|]
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RecName: Full=Complement C2; AltName: Full=C3/C5 convertase; Contains: RecName: Full=Complement C2b fragment; Contains: RecName: Full=Complement C2a fragment; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 260-457 1.03e-81

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.


The actual alignment was detected with superfamily member cd01470:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 198  Bit Score: 258.76  E-value: 1.03e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 260 LNLYLLLDASQSVTEKDFDIFKKSAELMVERIFSFEVNVSVAIITFASQPKTIMSILSERSQDVTEVITSLDSASYKDHE 339
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 340 NATGTNTYEVLIRVYSMMQSQMDRLGMetsAWKEIRHTIILLTDGKSNMGDSPKKAVTRIRELLSIEQ----NRDDYLDI 415
Cdd:cd01470   81 DKTGTNTAAALKKVYERMALEKVRNKE---AFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNksdnPREDYLDV 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 341940373 416 YAIGVGKlDVDWKELNELGSKKDGERHAFILQDAKALQQIFE 457
Cdd:cd01470  158 YVFGVGD-DVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 480-750 1.02e-39

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 146.27  E-value: 1.02e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 480 SDQERTPWQVT-FKPKSKETCQGSLISDQWVLTAAHCFHDIQMEDhhlWRVNVGD----PTSQHGKEFLVEDVIIAPGFN 554
Cdd:cd00190    7 AKIGSFPWQVSlQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGShdlsSNEGGGQVIKVKKVIVHPNYN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 555 vhakrkqgiSEFYADDIALLKLSRKVKMSTHARPICLPCTvGANMAlrrsPGSTC------KDHETELLSQ--QKVpahf 626
Cdd:cd00190   84 ---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSS-GYNLP----AGTTCtvsgwgRTSEGGPLPDvlQEV---- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 627 valngnrlNINLRTgpeWTRCIQAVSQNknifpsltnvsEVVTDQFLCSGMEEEDDNPCKGESGGAVFLGRRYRFFQVGL 706
Cdd:cd00190  146 --------NVPIVS---NAECKRAYSYG-----------GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGI 203

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 341940373 707 VSWGLFdpChGSSNKnlrkkpprgvlPRDFHIsLFRLQPWLRQH 750
Cdd:cd00190  204 VSWGSG--C-ARPNY-----------PGVYTR-VSSYLDWIQKT 232
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 94-149 8.38e-14

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


:

Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 66.33  E-value: 8.38e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940373  94 CLAPSSFENGIYFPRLVSYPVGSNVSFECEQDFTLRGSPVRYCRPNGLWDGETAVC 149
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 156-210 7.34e-10

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


:

Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 55.23  E-value: 7.34e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940373   156 CPNPG-ISVGTAR-TGLNFDLGDKVRYRCSSsNMVLTGSAERECQSNGVWSGSEPIC 210
Cdd:smart00032   1 CPPPPdIENGTVTsSSGTYSYGDTVTYSCDP-GYTLIGSSTITCLENGTWSPPPPTC 56
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 260-457 1.03e-81

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 258.76  E-value: 1.03e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 260 LNLYLLLDASQSVTEKDFDIFKKSAELMVERIFSFEVNVSVAIITFASQPKTIMSILSERSQDVTEVITSLDSASYKDHE 339
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 340 NATGTNTYEVLIRVYSMMQSQMDRLGMetsAWKEIRHTIILLTDGKSNMGDSPKKAVTRIRELLSIEQ----NRDDYLDI 415
Cdd:cd01470   81 DKTGTNTAAALKKVYERMALEKVRNKE---AFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNksdnPREDYLDV 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 341940373 416 YAIGVGKlDVDWKELNELGSKKDGERHAFILQDAKALQQIFE 457
Cdd:cd01470  158 YVFGVGD-DVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 480-750 1.02e-39

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 146.27  E-value: 1.02e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 480 SDQERTPWQVT-FKPKSKETCQGSLISDQWVLTAAHCFHDIQMEDhhlWRVNVGD----PTSQHGKEFLVEDVIIAPGFN 554
Cdd:cd00190    7 AKIGSFPWQVSlQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGShdlsSNEGGGQVIKVKKVIVHPNYN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 555 vhakrkqgiSEFYADDIALLKLSRKVKMSTHARPICLPCTvGANMAlrrsPGSTC------KDHETELLSQ--QKVpahf 626
Cdd:cd00190   84 ---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSS-GYNLP----AGTTCtvsgwgRTSEGGPLPDvlQEV---- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 627 valngnrlNINLRTgpeWTRCIQAVSQNknifpsltnvsEVVTDQFLCSGMEEEDDNPCKGESGGAVFLGRRYRFFQVGL 706
Cdd:cd00190  146 --------NVPIVS---NAECKRAYSYG-----------GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGI 203

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 341940373 707 VSWGLFdpChGSSNKnlrkkpprgvlPRDFHIsLFRLQPWLRQH 750
Cdd:cd00190  204 VSWGSG--C-ARPNY-----------PGVYTR-VSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 480-721 1.38e-37

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 140.12  E-value: 1.38e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373   480 SDQERTPWQVT-FKPKSKETCQGSLISDQWVLTAAHCFHDIqmeDHHLWRVNVGD---PTSQHGKEFLVEDVIIAPGFNv 555
Cdd:smart00020   8 ANIGSFPWQVSlQYGGGRHFCGGSLISPRWVLTAAHCVRGS---DPSNIRVRLGShdlSSGEEGQVIKVSKVIIHPNYN- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373   556 hakrkqgiSEFYADDIALLKLSRKVKMSTHARPICLPCTvganmALRRSPGSTCKD---HETELlsqqKVPAHFVALNGN 632
Cdd:smart00020  84 --------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCTVsgwGRTSE----GAGSLPDTLQEV 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373   633 RLNINlrtgpEWTRCIQAVSQNknifpsltnvsEVVTDQFLCSGMEEEDDNPCKGESGGAVFLGRRyRFFQVGLVSWGlf 712
Cdd:smart00020 147 NVPIV-----SNATCRRAYSGG-----------GAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG-RWVLVGIVSWG-- 207


                   ....*....
gi 341940373   713 DPChGSSNK 721
Cdd:smart00020 208 SGC-ARPGK 215
VWA pfam00092
von Willebrand factor type A domain;
261-458 6.92e-33

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 125.08  E-value: 6.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373  261 NLYLLLDASQSVTEKDFDIFKKSAELMVERIFSFEVNVSVAIITFASQPKTIMSILSERSQDvtEVITSLDSASYKDHEN 340
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKE--ELLSAVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373  341 A-TGTNTYEVLIRVYSMMQsqmdrlgmetSAWKEIRHTIILLTDGKSNMGDsPKKAVTRIrellsieqnRDDYLDIYAIG 419
Cdd:pfam00092  79 TnTGKALKYALENLFSSAA----------GARPGAPKVVVLLTDGRSQDGD-PEEVAREL---------KSAGVTVFAVG 138

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 341940373  420 VGklDVDWKELNELGSKKDgERHAFILQDAKALQQIFEH 458
Cdd:pfam00092 139 VG--NADDEELRKIASEPG-EGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 261-455 1.27e-27

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 109.85  E-value: 1.27e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373   261 NLYLLLDASQSVTEKDFDIFKKSAELMVERIFSFEVNVSVAIITFASQPKTIMSILSERSQDvtEVITSLDSASYKDHEn 340
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKD--ALLEALASLSYKLGG- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373   341 atGTNTYEVLIRVYSMMQSQMDRlgmetsAWKEIRHTIILLTDGKSNmgDSPKKAVTRIRELlsieqnRDDYLDIYAIGV 420
Cdd:smart00327  78 --GTNLGAALQYALENLFSKSAG------SRRGAPKVVILITDGESN--DGPKDLLKAAKEL------KRSGVKVFVVGV 141

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 341940373   421 GKlDVDWKELNELgSKKDGERHAFILQDAKALQQI 455
Cdd:smart00327 142 GN-DVDEEELKKL-ASAPGGVYVFLPELLDLLIDL 174
Trypsin pfam00089
Trypsin;
486-747 7.10e-27

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 109.07  E-value: 7.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373  486 PWQVTFK-PKSKETCQGSLISDQWVLTAAHCFHdiqmeDHHLWRVNVGDPTSQHG----KEFLVEDVIIAPGFNvhakrk 560
Cdd:pfam00089  13 PWQVSLQlSSGKHFCGGSLISENWVLTAAHCVS-----GASDVKVVLGAHNIVLReggeQKFDVEKIIVHPNYN------ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373  561 qgiSEFYADDIALLKLSRKVKMSTHARPICLPCTvganmALRRSPGSTCkdhetellsqqkvpahFVA----LNGNRLNI 636
Cdd:pfam00089  82 ---PDTLDNDIALLKLESPVTLGDTVRPICLPDA-----SSDLPVGTTC----------------TVSgwgnTKTLGPSD 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373  637 NLRTGPewtrcIQAVSQNKNIfpslTNVSEVVTDQFLCSGMEEEDdnPCKGESGGAVFLGRRYrffQVGLVSWGlfDPCh 716
Cdd:pfam00089 138 TLQEVT-----VPVVSRETCR----SAYGGTVTDTMICAGAGGKD--ACQGDSGGPLVCSDGE---LIGIVSWG--YGC- 200

                         250       260       270
                  ....*....|....*....|....*....|.
gi 341940373  717 gssnkNLRKKPprgvlprDFHISLFRLQPWL 747
Cdd:pfam00089 201 -----ASGNYP-------GVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 478-719 7.69e-21

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 92.79  E-value: 7.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 478 NASDQERtPWQVTFKPKS---KETCQGSLISDQWVLTAAHCFHDIQMEDHHLwRVNVGDPTSQHGKEFLVEDVIIAPGFN 554
Cdd:COG5640   36 PATVGEY-PWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRV-VIGSTDLSTSGGTVVKVARIVVHPDYD 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 555 VHAkrkqgisefYADDIALLKLSRKVkmsTHARPICLpctvgANMALRRSPGSTckdhetellsqqkvpahFVAL----- 629
Cdd:COG5640  114 PAT---------PGNDIALLKLATPV---PGVAPAPL-----ATSADAAAPGTP-----------------ATVAgwgrt 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 630 --NGNRLNINLRTGPewtrcIQAVSQNknifpSLTNVSEVVTDQFLCSGMEEEDDNPCKGESGGAVFLGRRYRFFQVGLV 707
Cdd:COG5640  160 seGPGSQSGTLRKAD-----VPVVSDA-----TCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVV 229

                        250
                 ....*....|..
gi 341940373 708 SWGLfDPCHGSS 719
Cdd:COG5640  230 SWGG-GPCAAGY 240
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 94-149 8.38e-14

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 66.33  E-value: 8.38e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940373  94 CLAPSSFENGIYFPRLVSYPVGSNVSFECEQDFTLRGSPVRYCRPNGLWDGETAVC 149
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 211-457 9.33e-13

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: 69.20  E-value: 9.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 211 RQPYSYDFPEDVASALDTSLTNLLGATNPTQNLLTKSLGRKIIIQRSGHLNLYLLLDASQSVTEKD-FDIFKKSAELMVE 289
Cdd:COG1240   44 LAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLD 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 290 RifsFEVNVSVAIITFASQPKTIMSIlserSQDVTEVITSLDSASYKDhenatGTNTYEVLIRVYSMMQSQMDrlgmets 369
Cdd:COG1240  124 D---YRPRDRVGLVAFGGEAEVLLPL----TRDREALKRALDELPPGG-----GTPLGDALALALELLKRADP------- 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 370 awkEIRHTIILLTDGKSNMGD-SPKKAVTRIRELLsieqnrddyLDIYAIGVGKLDVDWKELNELGSKKDGErhAFILQD 448
Cdd:COG1240  185 ---ARRKVIVLLTDGRDNAGRiDPLEAAELAAAAG---------IRIYTIGVGTEAVDEGLLREIAEATGGR--YFRADD 250


                 ....*....
gi 341940373 449 AKALQQIFE 457
Cdd:COG1240  251 LSELAAIYR 259
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 94-149 6.46e-12

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 61.00  E-value: 6.46e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940373    94 CLAPSSFENGIYFPRLVSYPVGSNVSFECEQDFTLRGSPVRYCRPNGLWDGETAVC 149
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
94-149 9.59e-11

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 57.51  E-value: 9.59e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940373   94 CLAPSSFENGIYFPRLVSYPVGSNVSFECEQDFTLRGSPVRYCRPNGLWDGETAVC 149
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 156-210 7.34e-10

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 55.23  E-value: 7.34e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940373   156 CPNPG-ISVGTAR-TGLNFDLGDKVRYRCSSsNMVLTGSAERECQSNGVWSGSEPIC 210
Cdd:smart00032   1 CPPPPdIENGTVTsSSGTYSYGDTVTYSCDP-GYTLIGSSTITCLENGTWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 156-211 8.68e-10

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 55.16  E-value: 8.68e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 341940373 156 CPNPGISV-GTARTGL-NFDLGDKVRYRCSSsNMVLTGSAERECQSNGVWSGSEPICR 211
Cdd:cd00033    1 CPPPPVPEnGTVTGSKgSYSYGSTVTYSCNE-GYTLVGSSTITCTENGGWSPPPPTCE 57
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 23-210 2.20e-08

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 55.81  E-value: 2.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373  23 NQNVNITGGNFtlshgwapGSLLIYSCplgrypspawrkcqSNGQWLTPRSSSHHTLRSS-RMV----KAVCKPVRCLAP 97
Cdd:PHA02927  94 NGQLDIGGVDF--------GSSITYSC--------------NSGYQLIGESKSYCELGSTgSMVwnpeAPICESVKCQSP 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373  98 SSFENGIYFPRLVSYPVGSNVSFECEQDFTLRGSPVRYCRpNGLWDgETAVCDngASHCPNPGISVGTARTGL--NFDLG 175
Cdd:PHA02927 152 PSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGFkrSYSYN 227

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 341940373 176 DKVRYRCSSSnMVLTGSAERECQSNGVWSGSEPIC 210
Cdd:PHA02927 228 DNVDFKCKYG-YKLSGSSSSTCSPGNTWQPELPKC 261
Sushi pfam00084
Sushi repeat (SCR repeat);
156-210 5.62e-05

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 41.33  E-value: 5.62e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 341940373  156 CPNP----GISVGTARTGLNFdlGDKVRYRCSSSNmVLTGSAERECQSNGVWSGSEPIC 210
Cdd:pfam00084   1 CPPPpdipNGKVSATKNEYNY--GASVSYECDPGY-RLVGSPTITCQEDGTWSPPFPEC 56
PHA02831 PHA02831
EEV host range protein; Provisional
 88-142 9.22e-03

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 38.82  E-value: 9.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940373  88 VCKPVRCLAPSsFENGIY--FPRLVSYpvGSNVSFECEQDFTLRGSPVRYCRPNGLW 142
Cdd:PHA02831 135 VCKLIRCKYPA-LQNGFLnvFEKKFYY--GDIVNFKCKKGFILLGSSVSTCDINSIW 188
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 260-457 1.03e-81

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 258.76  E-value: 1.03e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 260 LNLYLLLDASQSVTEKDFDIFKKSAELMVERIFSFEVNVSVAIITFASQPKTIMSILSERSQDVTEVITSLDSASYKDHE 339
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 340 NATGTNTYEVLIRVYSMMQSQMDRLGMetsAWKEIRHTIILLTDGKSNMGDSPKKAVTRIRELLSIEQ----NRDDYLDI 415
Cdd:cd01470   81 DKTGTNTAAALKKVYERMALEKVRNKE---AFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNksdnPREDYLDV 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 341940373 416 YAIGVGKlDVDWKELNELGSKKDGERHAFILQDAKALQQIFE 457
Cdd:cd01470  158 YVFGVGD-DVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 480-750 1.02e-39

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 146.27  E-value: 1.02e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 480 SDQERTPWQVT-FKPKSKETCQGSLISDQWVLTAAHCFHDIQMEDhhlWRVNVGD----PTSQHGKEFLVEDVIIAPGFN 554
Cdd:cd00190    7 AKIGSFPWQVSlQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGShdlsSNEGGGQVIKVKKVIVHPNYN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 555 vhakrkqgiSEFYADDIALLKLSRKVKMSTHARPICLPCTvGANMAlrrsPGSTC------KDHETELLSQ--QKVpahf 626
Cdd:cd00190   84 ---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSS-GYNLP----AGTTCtvsgwgRTSEGGPLPDvlQEV---- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 627 valngnrlNINLRTgpeWTRCIQAVSQNknifpsltnvsEVVTDQFLCSGMEEEDDNPCKGESGGAVFLGRRYRFFQVGL 706
Cdd:cd00190  146 --------NVPIVS---NAECKRAYSYG-----------GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGI 203

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 341940373 707 VSWGLFdpChGSSNKnlrkkpprgvlPRDFHIsLFRLQPWLRQH 750
Cdd:cd00190  204 VSWGSG--C-ARPNY-----------PGVYTR-VSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 480-721 1.38e-37

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 140.12  E-value: 1.38e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373   480 SDQERTPWQVT-FKPKSKETCQGSLISDQWVLTAAHCFHDIqmeDHHLWRVNVGD---PTSQHGKEFLVEDVIIAPGFNv 555
Cdd:smart00020   8 ANIGSFPWQVSlQYGGGRHFCGGSLISPRWVLTAAHCVRGS---DPSNIRVRLGShdlSSGEEGQVIKVSKVIIHPNYN- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373   556 hakrkqgiSEFYADDIALLKLSRKVKMSTHARPICLPCTvganmALRRSPGSTCKD---HETELlsqqKVPAHFVALNGN 632
Cdd:smart00020  84 --------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCTVsgwGRTSE----GAGSLPDTLQEV 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373   633 RLNINlrtgpEWTRCIQAVSQNknifpsltnvsEVVTDQFLCSGMEEEDDNPCKGESGGAVFLGRRyRFFQVGLVSWGlf 712
Cdd:smart00020 147 NVPIV-----SNATCRRAYSGG-----------GAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG-RWVLVGIVSWG-- 207


                   ....*....
gi 341940373   713 DPChGSSNK 721
Cdd:smart00020 208 SGC-ARPGK 215
VWA pfam00092
von Willebrand factor type A domain;
261-458 6.92e-33

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 125.08  E-value: 6.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373  261 NLYLLLDASQSVTEKDFDIFKKSAELMVERIFSFEVNVSVAIITFASQPKTIMSILSERSQDvtEVITSLDSASYKDHEN 340
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKE--ELLSAVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373  341 A-TGTNTYEVLIRVYSMMQsqmdrlgmetSAWKEIRHTIILLTDGKSNMGDsPKKAVTRIrellsieqnRDDYLDIYAIG 419
Cdd:pfam00092  79 TnTGKALKYALENLFSSAA----------GARPGAPKVVVLLTDGRSQDGD-PEEVAREL---------KSAGVTVFAVG 138

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 341940373  420 VGklDVDWKELNELGSKKDgERHAFILQDAKALQQIFEH 458
Cdd:pfam00092 139 VG--NADDEELRKIASEPG-EGHVFTVSDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 260-444 8.55e-32

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: 121.24  E-value: 8.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 260 LNLYLLLDASQSVTEKDFDIFKKSAELMVERIFSFEVNVSVAIITFASQPKTIMSILSerSQDVTEVITSLDSASYKDHe 339
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLND--YKSKDDLLKAVKNLKYLGG- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 340 naTGTNTYEVLIRVYSMMQSqmdrlgmETSAWKEIRHTIILLTDGKSNMGDSPKKAVTRIrellsieqnRDDYLDIYAIG 419
Cdd:cd01450   78 --GGTNTGKALQYALEQLFS-------ESNARENVPKVIIVLTDGRSDDGGDPKEAAAKL---------KDEGIKVFVVG 139

                        170       180
                 ....*....|....*....|....*
gi 341940373 420 VGklDVDWKELNELGSKKdGERHAF 444
Cdd:cd01450  140 VG--PADEEELREIASCP-SERHVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 261-455 1.27e-27

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 109.85  E-value: 1.27e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373   261 NLYLLLDASQSVTEKDFDIFKKSAELMVERIFSFEVNVSVAIITFASQPKTIMSILSERSQDvtEVITSLDSASYKDHEn 340
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKD--ALLEALASLSYKLGG- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373   341 atGTNTYEVLIRVYSMMQSQMDRlgmetsAWKEIRHTIILLTDGKSNmgDSPKKAVTRIRELlsieqnRDDYLDIYAIGV 420
Cdd:smart00327  78 --GTNLGAALQYALENLFSKSAG------SRRGAPKVVILITDGESN--DGPKDLLKAAKEL------KRSGVKVFVVGV 141

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 341940373   421 GKlDVDWKELNELgSKKDGERHAFILQDAKALQQI 455
Cdd:smart00327 142 GN-DVDEEELKKL-ASAPGGVYVFLPELLDLLIDL 174
Trypsin pfam00089
Trypsin;
486-747 7.10e-27

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 109.07  E-value: 7.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373  486 PWQVTFK-PKSKETCQGSLISDQWVLTAAHCFHdiqmeDHHLWRVNVGDPTSQHG----KEFLVEDVIIAPGFNvhakrk 560
Cdd:pfam00089  13 PWQVSLQlSSGKHFCGGSLISENWVLTAAHCVS-----GASDVKVVLGAHNIVLReggeQKFDVEKIIVHPNYN------ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373  561 qgiSEFYADDIALLKLSRKVKMSTHARPICLPCTvganmALRRSPGSTCkdhetellsqqkvpahFVA----LNGNRLNI 636
Cdd:pfam00089  82 ---PDTLDNDIALLKLESPVTLGDTVRPICLPDA-----SSDLPVGTTC----------------TVSgwgnTKTLGPSD 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373  637 NLRTGPewtrcIQAVSQNKNIfpslTNVSEVVTDQFLCSGMEEEDdnPCKGESGGAVFLGRRYrffQVGLVSWGlfDPCh 716
Cdd:pfam00089 138 TLQEVT-----VPVVSRETCR----SAYGGTVTDTMICAGAGGKD--ACQGDSGGPLVCSDGE---LIGIVSWG--YGC- 200

                         250       260       270
                  ....*....|....*....|....*....|.
gi 341940373  717 gssnkNLRKKPprgvlprDFHISLFRLQPWL 747
Cdd:pfam00089 201 -----ASGNYP-------GVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 478-719 7.69e-21

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 92.79  E-value: 7.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 478 NASDQERtPWQVTFKPKS---KETCQGSLISDQWVLTAAHCFHDIQMEDHHLwRVNVGDPTSQHGKEFLVEDVIIAPGFN 554
Cdd:COG5640   36 PATVGEY-PWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRV-VIGSTDLSTSGGTVVKVARIVVHPDYD 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 555 VHAkrkqgisefYADDIALLKLSRKVkmsTHARPICLpctvgANMALRRSPGSTckdhetellsqqkvpahFVAL----- 629
Cdd:COG5640  114 PAT---------PGNDIALLKLATPV---PGVAPAPL-----ATSADAAAPGTP-----------------ATVAgwgrt 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 630 --NGNRLNINLRTGPewtrcIQAVSQNknifpSLTNVSEVVTDQFLCSGMEEEDDNPCKGESGGAVFLGRRYRFFQVGLV 707
Cdd:COG5640  160 seGPGSQSGTLRKAD-----VPVVSDA-----TCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVV 229

                        250
                 ....*....|..
gi 341940373 708 SWGLfDPCHGSS 719
Cdd:COG5640  230 SWGG-GPCAAGY 240
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 260-441 4.05e-19

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: 84.92  E-value: 4.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 260 LNLYLLLDASQSVTEKDFDIFKKSAELMVERIFSFEVNVSVAIITFASQPKTIMSILSERS-QDVTEVITSLdsasykDH 338
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDkADLLEAIDAL------KK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 339 ENATGTNTYEVLIRVYSMMQSQMDRLGmetsawkeiRHTIILLTDGKSNmgDSPKKAVTRIRELlsieqnRDDYLDIYAI 418
Cdd:cd00198   75 GLGGGTNIGAALRLALELLKSAKRPNA---------RRVIILLTDGEPN--DGPELLAEAAREL------RKLGITVYTI 137

                        170       180
                 ....*....|....*....|...
gi 341940373 419 GVGkLDVDWKELNELGSKKDGER 441
Cdd:cd00198  138 GIG-DDANEDELKEIADKTTGGA 159
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 94-149 8.38e-14

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 66.33  E-value: 8.38e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940373  94 CLAPSSFENGIYFPRLVSYPVGSNVSFECEQDFTLRGSPVRYCRPNGLWDGETAVC 149
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 211-457 9.33e-13

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: 69.20  E-value: 9.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 211 RQPYSYDFPEDVASALDTSLTNLLGATNPTQNLLTKSLGRKIIIQRSGHLNLYLLLDASQSVTEKD-FDIFKKSAELMVE 289
Cdd:COG1240   44 LAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLD 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 290 RifsFEVNVSVAIITFASQPKTIMSIlserSQDVTEVITSLDSASYKDhenatGTNTYEVLIRVYSMMQSQMDrlgmets 369
Cdd:COG1240  124 D---YRPRDRVGLVAFGGEAEVLLPL----TRDREALKRALDELPPGG-----GTPLGDALALALELLKRADP------- 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 370 awkEIRHTIILLTDGKSNMGD-SPKKAVTRIRELLsieqnrddyLDIYAIGVGKLDVDWKELNELGSKKDGErhAFILQD 448
Cdd:COG1240  185 ---ARRKVIVLLTDGRDNAGRiDPLEAAELAAAAG---------IRIYTIGVGTEAVDEGLLREIAEATGGR--YFRADD 250


                 ....*....
gi 341940373 449 AKALQQIFE 457
Cdd:COG1240  251 LSELAAIYR 259
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 238-491 1.05e-12

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 69.36  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 238 NPTQNLLTKSL-GRKIIIQRSGHLNLYLLLDASQSVTEKDFDIFKKSAELMVERIfsfEVNVSVAIITFASQPKTIMSil 316
Cdd:COG2304   69 NPQTRLLLVGLqPPKAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQL---RPGDRVSIVTFAGDARVLLP-- 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 317 SERSQDVTEVITSLDSASykdhenATG-TNTYEVLIRVYSMMQSQMDRLGmetsawkeIRHtIILLTDGKSNMGdspkka 395
Cdd:COG2304  144 PTPATDRAKILAAIDRLQ------AGGgTALGAGLELAYELARKHFIPGR--------VNR-VILLTDGDANVG------ 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 396 VTRIRELLS-IEQNRDDYLDIYAIGVGkldVDWKE--LNELGSKKDGeRHAFIlQDAKALQQIFEhmldvsKLTDTIcGV 472
Cdd:COG2304  203 ITDPEELLKlAEEAREEGITLTTLGVG---SDYNEdlLERLADAGGG-NYYYI-DDPEEAEKVFV------REFSRI-GY 270

                        250
                 ....*....|....*....
gi 341940373 473 GNMSANASDQERTPWQVTF 491
Cdd:COG2304  271 ENRALATEDFPLPYGTLKL 289
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 94-149 6.46e-12

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 61.00  E-value: 6.46e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940373    94 CLAPSSFENGIYFPRLVSYPVGSNVSFECEQDFTLRGSPVRYCRPNGLWDGETAVC 149
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 260-449 3.23e-11

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: 62.68  E-value: 3.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 260 LNLYLLLDASQSVTEKDFDIFKKSAELMVERIfsfEVNVSVAIITFASQPKTIMSilSERSQDVTEVITSLDSAsykdhE 339
Cdd:cd01465    1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQL---RPDDRLAIVTYDGAAETVLP--ATPVRDKAAILAAIDRL-----T 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 340 NATGTNTYEVLIRVYSMMQSQMDRLGMetsawkeirHTIILLTDGKSNMGDspkkavTRIRELL-SIEQNRDDYLDIYAI 418
Cdd:cd01465   71 AGGSTAGGAGIQLGYQEAQKHFVPGGV---------NRILLATDGDFNVGE------TDPDELArLVAQKRESGITLSTL 135

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 341940373 419 GVGKldvDWKE--LNELGSKKDGeRHAFI--LQDA 449
Cdd:cd01465  136 GFGD---NYNEdlMEAIADAGNG-NTAYIdnLAEA 166
Sushi pfam00084
Sushi repeat (SCR repeat);
94-149 9.59e-11

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 57.51  E-value: 9.59e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940373   94 CLAPSSFENGIYFPRLVSYPVGSNVSFECEQDFTLRGSPVRYCRPNGLWDGETAVC 149
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 156-210 7.34e-10

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 55.23  E-value: 7.34e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940373   156 CPNPG-ISVGTAR-TGLNFDLGDKVRYRCSSsNMVLTGSAERECQSNGVWSGSEPIC 210
Cdd:smart00032   1 CPPPPdIENGTVTsSSGTYSYGDTVTYSCDP-GYTLIGSSTITCLENGTWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 156-211 8.68e-10

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 55.16  E-value: 8.68e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 341940373 156 CPNPGISV-GTARTGL-NFDLGDKVRYRCSSsNMVLTGSAERECQSNGVWSGSEPICR 211
Cdd:cd00033    1 CPPPPVPEnGTVTGSKgSYSYGSTVTYSCNE-GYTLVGSSTITCTENGGWSPPPPTCE 57
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 23-210 2.20e-08

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 55.81  E-value: 2.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373  23 NQNVNITGGNFtlshgwapGSLLIYSCplgrypspawrkcqSNGQWLTPRSSSHHTLRSS-RMV----KAVCKPVRCLAP 97
Cdd:PHA02927  94 NGQLDIGGVDF--------GSSITYSC--------------NSGYQLIGESKSYCELGSTgSMVwnpeAPICESVKCQSP 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373  98 SSFENGIYFPRLVSYPVGSNVSFECEQDFTLRGSPVRYCRpNGLWDgETAVCDngASHCPNPGISVGTARTGL--NFDLG 175
Cdd:PHA02927 152 PSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGFkrSYSYN 227

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 341940373 176 DKVRYRCSSSnMVLTGSAERECQSNGVWSGSEPIC 210
Cdd:PHA02927 228 DNVDFKCKYG-YKLSGSSSSTCSPGNTWQPELPKC 261
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 258-463 5.60e-08

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: 53.28  E-value: 5.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 258 GHLNLYLLLDASQSVTEKDFDIFkKSAELMVERIFSfeVNVSVAIITFASQPKTIMSILSERSQ------DVTEVITSLD 331
Cdd:cd01474    3 GHFDLYFVLDKSGSVAANWIEIY-DFVEQLVDRFNS--PGLRFSFITFSTRATKILPLTDDSSAiikgleVLKKVTPSGQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 332 SASYKDHENATGTNTYEvlirvysmmqsqmDRLGMETSAwkeirhTIILLTDGK--SNMGDSPKKAVTRIRELLSIeqnr 409
Cdd:cd01474   80 TYIHEGLENANEQIFNR-------------NGGGRETVS------VIIALTDGQllLNGHKYPEHEAKLSRKLGAI---- 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 341940373 410 ddyldIYAIGVgkLDVDWKELNELGSKKDgerHAFILQDA-KALQQIFEHMLDVS 463
Cdd:cd01474  137 -----VYCVGV--TDFLKSQLINIADSKE---YVFPVTSGfQALSGIIESVVKKA 181
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 260-445 8.23e-08

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 52.40  E-value: 8.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 260 LNLYLLLDASQSVTekdfDIFKKSAELMVERIFSFEVN---VSVAIITFASQPKTIMSILSERSQDVTEVITSLDSAsyK 336
Cdd:cd01476    1 LDLLFVLDSSGSVR----GKFEKYKKYIERIVEGLEIGptaTRVALITYSGRGRQRVRFNLPKHNDGEELLEKVDNL--R 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 337 DHENATGTNtyeVLIRVysmmqsQMDRLGMETSAWKEIRHTIILLTDGKSNmgDSPKKAVTRIRELLSIeqnrddylDIY 416
Cdd:cd01476   75 FIGGTTATG---AAIEV------ALQQLDPSEGRREGIPKVVVVLTDGRSH--DDPEKQARILRAVPNI--------ETF 135

                        170       180       190
                 ....*....|....*....|....*....|
gi 341940373 417 AIGVG-KLDVDWKELNELGSKkdgERHAFI 445
Cdd:cd01476  136 AVGTGdPGTVDTEELHSITGN---EDHIFT 162
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
259-457 1.18e-07

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 52.62  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 259 HLNLYLLLDASQSVTEKDFDIFKKSAELMVERIFSFEV---NVSVAIITFASQPKTIMSilsersqdvtevITSLDSASY 335
Cdd:COG4245    5 RLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYaleTVEVSVITFDGEAKVLLP------------LTDLEDFQP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 336 KDHENATGTNTYEVLIRVYSMMQSQMDRL-GMETSAWKEIrhtIILLTDGKSNmGDSPKKAVTRIRELlsiEQNRDDYld 414
Cdd:COG4245   73 PDLSASGGTPLGAALELLLDLIERRVQKYtAEGKGDWRPV---VFLITDGEPT-DSDWEAALQRLKDG---EAAKKAN-- 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 341940373 415 IYAIGVGKlDVDWKELNELGskkDGERhAFILQDAKALQQIFE 457
Cdd:COG4245  144 IFAIGVGP-DADTEVLKQLT---DPVR-ALDALDGLDFREFFK 181
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 261-448 3.59e-07

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 50.69  E-value: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 261 NLYLLLDASQSVTEKDFDIFKKSAELMVERifsFEV---NVSVAIITFASQPKTIMSILSERSQDvtEVITSLDSASYKd 337
Cdd:cd01472    2 DIVFLVDGSESIGLSNFNLVKDFVKRVVER---LDIgpdGVRVGVVQYSDDPRTEFYLNTYRSKD--DVLEAVKNLRYI- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 338 henATGTNTYEVLIRVYSMMQSQMDRLGmetsawKEIRHTIILLTDGKSnMGDSPKKAVTRIRelLSIEqnrddyldIYA 417
Cdd:cd01472   76 ---GGGTNTGKALKYVRENLFTEASGSR------EGVPKVLVVITDGKS-QDDVEEPAVELKQ--AGIE--------VFA 135

                        170       180       190
                 ....*....|....*....|....*....|.
gi 341940373 418 IGVGKLDVDwkELNELGSkKDGERHAFILQD 448
Cdd:cd01472  136 VGVKNADEE--ELKQIAS-DPKELYVFNVAD 163
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 258-480 8.93e-07

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 50.46  E-value: 8.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 258 GHLNLYLLLDASQSVTEKDFDIFKKSAELMVERIFSFEVNVSVAIITFASQPKTIMSILS-ERSQDVTEVITSLDSASyk 336
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRfKSKADLKRAVRRMEYLE-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 337 dhenaTGTNTYEVLirVYSMMQSQMDRLGMETSAwKEIRHTIILLTDGKS--NMGDSPKKAvtrirellsieqnRDDYLD 414
Cdd:cd01475   79 -----TGTMTGLAI--QYAMNNAFSEAEGARPGS-ERVPRVGIVVTDGRPqdDVSEVAAKA-------------RALGIE 137

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341940373 415 IYAIGVGKLDVDwkELNELGSKKDGErHAFILQDAKALQQIfehmldVSKLTDTICGVGNMSANAS 480
Cdd:cd01475  138 MFAVGVGRADEE--ELREIASEPLAD-HVFYVEDFSTIEEL------TKKFQGKICVVPDLCATLS 194
PHA02817 PHA02817
EEV Host range protein; Provisional
 85-253 1.09e-06

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 50.32  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373  85 VKAVCKPVRCLAPSSFENGIYFPRLVSYPVGSNVSFECEQD-----FTLRGSPVRYCRPNGLWDGETAVCDngASHCPNP 159
Cdd:PHA02817  15 VYSLCDLNKCCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCK--IIRCRFP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 160 GISVGTAR---TGLNFDLGDKVRYRCSSSnMVLTGSAERECQSNGVWSGSEPIC-RQPYSY------------DFPEDVA 223
Cdd:PHA02817  93 ALQNGFVNgipDSKKFYYESEVSFSCKPG-FVLIGTKYSVCGINSSWIPKVPICsRDNITYnkiyinkvniddNFFNQIN 171

                        170       180       190
                 ....*....|....*....|....*....|..
gi 341940373 224 SALDTSLTNLLGATNPTQN--LLTKSLGRKII 253
Cdd:PHA02817 172 NSNTYYFDKILQINNVNRYtlIFFVVVSIKIL 203
PHA02639 PHA02639
EEV host range protein; Provisional
 90-211 5.48e-06

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 48.89  E-value: 5.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373  90 KPVRCLAPSSFENGIYFPRLVSYPVGSNVSFECEQDFTLRGSPVRYC---RPNGLWDGETAVCDNGASHCPNPGISVGTA 166
Cdd:PHA02639  18 KSIYCDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCikdKNNAIWSNKAPFCMLKECNDPPSIINGKIY 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 341940373 167 RTGLNFDLGDKVRYRCSSSNMV---LTGSAERECQSNGVWSGSEPICR 211
Cdd:PHA02639  98 NKREMYKVGDEIYYVCNEHKGVqysLVGNEKITCIQDKSWKPDPPICK 145
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 265-455 5.95e-06

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 47.35  E-value: 5.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 265 LLDASQSVTEKDFDIFKKSAELMVERIFSFEVNVSVAIITFASQPKTIMSIlsERSQDVTEVITSLDSASYkdhenatgt 344
Cdd:cd01469    6 VLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTL--NEYRTKEEPLSLVKHISQ--------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 345 ntYEVLIRVYSMMQSQMDRLGMETS-AWKEIRHTIILLTDGKSNmGDSPKKAVtrirellsIEQNRDDYLDIYAIGVGKL 423
Cdd:cd01469   75 --LLGLTNTATAIQYVVTELFSESNgARKDATKVLVVITDGESH-DDPLLKDV--------IPQAEREGIIRYAIGVGGH 143

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 341940373 424 ---DVDWKELNELGSKKDgERHAFILQDAKALQQI 455
Cdd:cd01469  144 fqrENSREELKTIASKPP-EEHFFNVTDFAALKDI 177
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 264-448 1.68e-05

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 45.74  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 264 LLLDASQSVTEKDFDIFKKSAELMVErifSFEV---NVSVAIITFASQPKTIMSILSERS-QDVTEVITSLdsaSYKdhe 339
Cdd:cd01482    5 FLVDGSWSIGRSNFNLVRSFLSSVVE---AFEIgpdGVQVGLVQYSDDPRTEFDLNAYTSkEDVLAAIKNL---PYK--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 340 natGTNTYEVLIRVYSMMQSQMDRLGMEtsawKEIRHTIILLTDGKSNmgDSPKKAVTRIRElLSIEqnrddyldIYAIG 419
Cdd:cd01482   76 ---GGNTRTGKALTHVREKNFTPDAGAR----PGVPKVVILITDGKSQ--DDVELPARVLRN-LGVN--------VFAVG 137

                        170       180
                 ....*....|....*....|....*....
gi 341940373 420 VGklDVDWKELNELGSKKDgERHAFILQD 448
Cdd:cd01482  138 VK--DADESELKMIASKPS-ETHVFNVAD 163
Sushi pfam00084
Sushi repeat (SCR repeat);
156-210 5.62e-05

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 41.33  E-value: 5.62e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 341940373  156 CPNP----GISVGTARTGLNFdlGDKVRYRCSSSNmVLTGSAERECQSNGVWSGSEPIC 210
Cdd:pfam00084   1 CPPPpdipNGKVSATKNEYNY--GASVSYECDPGY-RLVGSPTITCQEDGTWSPPFPEC 56
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 258-402 8.27e-05

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 44.30  E-value: 8.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 258 GHLNLYLLLDASQSVTEKDFDIFKKSAELMVERIFSFEV------NVSVAIITFASQPkTIMSILSERSQDVTEVITSLD 331
Cdd:cd01480    1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYrkdpagSWRVGVVQYSDQQ-EVEAGFLRDIRNYTSLKEAVD 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940373 332 SASYKdhenATGTNTYEVLIRVYSMMQsqmdrlgmETSAWKEIRHtIILLTDGKSNMGD--SPKKAVTRIREL 402
Cdd:cd01480   80 NLEYI----GGGTFTDCALKYATEQLL--------EGSHQKENKF-LLVITDGHSDGSPdgGIEKAVNEADHL 139
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 499-580 1.28e-04

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 43.51  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373 499 CQGSLISDQWVLTAAHCFHDIQM-EDHHLWRVNVGDPTSQHGkEFLVEDVIIAPGFnvhakrkqGISEFYADDIALLKLS 577
Cdd:COG3591   14 CTGTLIGPNLVLTAGHCVYDGAGgGWATNIVFVPGYNGGPYG-TATATRFRVPPGW--------VASGDAGYDYALLRLD 84


                 ...
gi 341940373 578 RKV 580
Cdd:COG3591   85 EPL 87
VWA_2 pfam13519
von Willebrand factor type A domain;
262-381 1.99e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 41.12  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940373  262 LYLLLDASQSVTEKDFDIFKKSAEL-MVERIFSFEVNVSVAIITFASQPKTIMSiLSERSQDVTEVITSLDSASykdhen 340
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRLEAAKdAVLALLKSLPGDRVGLVTFGDGPEVLIP-LTKDRAKILRALRRLEPKG------ 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 341940373  341 aTGTNTYEVLIRVYSMMQSQmdrlgmetsaWKEIRHTIILL 381
Cdd:pfam13519  74 -GGTNLAAALQLARAALKHR----------RKNQPRRIVLI 103
PHA02831 PHA02831
EEV host range protein; Provisional
 88-142 9.22e-03

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 38.82  E-value: 9.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940373  88 VCKPVRCLAPSsFENGIY--FPRLVSYpvGSNVSFECEQDFTLRGSPVRYCRPNGLW 142
Cdd:PHA02831 135 VCKLIRCKYPA-LQNGFLnvFEKKFYY--GDIVNFKCKKGFILLGSSVSTCDINSIW 188
 
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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