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Conserved domains on  [gi|47575877|ref|NP_757376|]
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complement C2 precursor [Rattus norvegicus]

Protein Classification

serine protease( domain architecture ID 13332055)

trypsin-like serine protease such as human plasminogen, the precursor of the widely distributed protease plasmin, or granzyme B, a human enzyme necessary for target cell lysis in cell-mediated immune responses

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 ...
 259-456 1.10e-83

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: 264.15  E-value: 1.10e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 259 LNLYLLLDASQSVSEKDFNIFKESAFLMVDRIFSFEIKVSVAIITFASRPKIIMSVLNERSQNVMEVMDSLDSVCYKDHE 338
Cdd:cd01470   1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 339 NATGTNTYEALNSVYLMMNNQMDRLGMetsAWQEIRHAIILLTDGKSNMGGSPKPAVDNIREILGISR----NRNDYLDI 414
Cdd:cd01470  81 DKTGTNTAAALKKVYERMALEKVRNKE---AFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNksdnPREDYLDV 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 47575877 415 YAIGVGKlDVDWKELNELGSKKDGERHAFILQDAKAVQQVFE 456
Cdd:cd01470 158 YVFGVGD-DVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 479-748 2.25e-37

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: 139.72  E-value: 2.25e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 479 SDQERTPWQVT-FKPKSKETCQGSLISDQWVLTAAHCFHDAQMEDrhlWRVIVGD----PTSHHGKEFHVEEVLVAPGFN 553
Cdd:cd00190   7 AKIGSFPWQVSlQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGShdlsSNEGGGQVIKVKKVIVHPNYN 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 554 vhakqsqgiSEFYADDIALLKLSQRVKMSSHARPICLPCTvGANMAlrrsPGSTC------KDHETELLSQ--QKVpahf 625
Cdd:cd00190  84 ---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSS-GYNLP----AGTTCtvsgwgRTSEGGPLPDvlQEV---- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 626 valngnrmNINLRTgpeRTSCIEAVSQNkgsfpgltnvsEVVTDQFLCSG-MEGDDSPCKGESGGAVFLERRYRFFQVGL 704
Cdd:cd00190 146 --------NVPIVS---NAECKRAYSYG-----------GTITDNMLCAGgLEGGKDACQGDSGGPLVCNDNGRGVLVGI 203

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 47575877 705 VSWGLFdpChGSSNKnlrrkpphgvvPRDFHIsLFRLQPWLRQH 748
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 8.19e-16

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: 72.11  E-value: 8.19e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 47575877  94 CPAPTSFENGIYIPRLGSYPVGGNLSFECEHGFTLRGSPVRYCRPNGVWDGETAVC 149
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
 22-210 5.12e-10

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 60.82  E-value: 5.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   22 CPQNVNIVGGNFTLSrGWAPGSVLIYSCPLGRY---PSPAWRECQSNGQ--WQtPRASslptlrssrlakaVCKPVRCPA 96
Cdd:PHA02927  86 CPSPRDIDNGQLDIG-GVDFGSSITYSCNSGYQligESKSYCELGSTGSmvWN-PEAP-------------ICESVKCQS 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   97 PTSFENGIYIPRLGSYPVGGNLSFECEHGFTLRGSPVRYCRpNGVWDgETAVCDngASHCPNPGISVGTMRTG--SSFDL 174
Cdd:PHA02927 151 PPSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGfkRSYSY 226

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 47575877  175 GDKVSYRCSStNLVLTGSVERECLSNGVWSGSEPIC 210
Cdd:PHA02927 227 NDNVDFKCKY-GYKLSGSSSSTCSPGNTWQPELPKC 261
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 259-456 1.10e-83

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: 264.15  E-value: 1.10e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 259 LNLYLLLDASQSVSEKDFNIFKESAFLMVDRIFSFEIKVSVAIITFASRPKIIMSVLNERSQNVMEVMDSLDSVCYKDHE 338
Cdd:cd01470   1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 339 NATGTNTYEALNSVYLMMNNQMDRLGMetsAWQEIRHAIILLTDGKSNMGGSPKPAVDNIREILGISR----NRNDYLDI 414
Cdd:cd01470  81 DKTGTNTAAALKKVYERMALEKVRNKE---AFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNksdnPREDYLDV 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 47575877 415 YAIGVGKlDVDWKELNELGSKKDGERHAFILQDAKAVQQVFE 456
Cdd:cd01470 158 YVFGVGD-DVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 479-748 2.25e-37

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: 139.72  E-value: 2.25e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 479 SDQERTPWQVT-FKPKSKETCQGSLISDQWVLTAAHCFHDAQMEDrhlWRVIVGD----PTSHHGKEFHVEEVLVAPGFN 553
Cdd:cd00190   7 AKIGSFPWQVSlQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGShdlsSNEGGGQVIKVKKVIVHPNYN 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 554 vhakqsqgiSEFYADDIALLKLSQRVKMSSHARPICLPCTvGANMAlrrsPGSTC------KDHETELLSQ--QKVpahf 625
Cdd:cd00190  84 ---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSS-GYNLP----AGTTCtvsgwgRTSEGGPLPDvlQEV---- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 626 valngnrmNINLRTgpeRTSCIEAVSQNkgsfpgltnvsEVVTDQFLCSG-MEGDDSPCKGESGGAVFLERRYRFFQVGL 704
Cdd:cd00190 146 --------NVPIVS---NAECKRAYSYG-----------GTITDNMLCAGgLEGGKDACQGDSGGPLVCNDNGRGVLVGI 203

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 47575877 705 VSWGLFdpChGSSNKnlrrkpphgvvPRDFHIsLFRLQPWLRQH 748
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 ...
 479-719 8.94e-36

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: 135.11  E-value: 8.94e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877    479 SDQERTPWQVT-FKPKSKETCQGSLISDQWVLTAAHCFHDAqmeDRHLWRVIVGD---PTSHHGKEFHVEEVLVAPGFNv 554
Cdd:smart00020   8 ANIGSFPWQVSlQYGGGRHFCGGSLISPRWVLTAAHCVRGS---DPSNIRVRLGShdlSSGEEGQVIKVSKVIIHPNYN- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877    555 hakqsqgiSEFYADDIALLKLSQRVKMSSHARPICLPCTvganmALRRSPGSTCKD---HETELlsqqKVPAHFVALngn 631
Cdd:smart00020  84 --------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCTVsgwGRTSE----GAGSLPDTL--- 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877    632 rMNINLRTGPERTsCIEAVSQNkgsfpgltnvsEVVTDQFLCSG-MEGDDSPCKGESGGAVFLERRyRFFQVGLVSWGlf 710
Cdd:smart00020 144 -QEVNVPIVSNAT-CRRAYSGG-----------GAITDNMLCAGgLEGGKDACQGDSGGPLVCNDG-RWVLVGIVSWG-- 207


                   ....*....
gi 47575877    711 DPChGSSNK 719
Cdd:smart00020 208 SGC-ARPGK 215
VWA pfam00092
von Willebrand factor type A domain;
260-457 1.26e-30

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 118.53  E-value: 1.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   260 NLYLLLDASQSVSEKDFNIFKESAFLMVDRIFSFEIKVSVAIITFASRPKIIMSvLNErSQNVMEVMDSLDSVCYKDHEN 339
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFP-LND-YSSKEELLSAVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   340 A-TGTNTYEALNSVYLMMNNQmdRLGmetsawqeIRHAIILLTDGKSNMgGSPKPAVDNIREiLGISrnrndyldIYAIG 418
Cdd:pfam00092  79 TnTGKALKYALENLFSSAAGA--RPG--------APKVVVLLTDGRSQD-GDPEEVARELKS-AGVT--------VFAVG 138

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 47575877   419 VGklDVDWKELNELGSKKDgERHAFILQDAKAVQQVFEH 457
Cdd:pfam00092 139 VG--NADDEELRKIASEPG-EGHVFTVSDFEALEDLQDQ 174
Trypsin pfam00089
Trypsin;
485-745 3.04e-27

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 110.22  E-value: 3.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   485 PWQVTFK-PKSKETCQGSLISDQWVLTAAHCFHdaqmeDRHLWRVIVGDPTSHHG----KEFHVEEVLVAPGFNvhakqs 559
Cdd:pfam00089  13 PWQVSLQlSSGKHFCGGSLISENWVLTAAHCVS-----GASDVKVVLGAHNIVLReggeQKFDVEKIIVHPNYN------ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   560 qgiSEFYADDIALLKLSQRVKMSSHARPICLPCTvganmALRRSPGSTCkdhetellsqqkvpahFVALNGNRMNINLrt 639
Cdd:pfam00089  82 ---PDTLDNDIALLKLESPVTLGDTVRPICLPDA-----SSDLPVGTTC----------------TVSGWGNTKTLGP-- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   640 gPERTSCIE--AVSQNKGSfpglTNVSEVVTDQFLCSGMEGDDSpCKGESGGAVFLERRYrffQVGLVSWGlfDPChgss 717
Cdd:pfam00089 136 -SDTLQEVTvpVVSRETCR----SAYGGTVTDTMICAGAGGKDA-CQGDSGGPLVCSDGE---LIGIVSWG--YGC---- 200

                         250       260
                  ....*....|....*....|....*...
gi 47575877   718 nkNLRRKPphgvvprDFHISLFRLQPWL 745
Cdd:pfam00089 201 --ASGNYP-------GVYTPVSSYLDWI 219
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 260-453 1.53e-25

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: 104.07  E-value: 1.53e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877    260 NLYLLLDASQSVSEKDFNIFKESAFLMVDRIFSFEIKVSVAIITFASRPKIIMSVLNERS-QNVMEVMDSLDSVCYKdhe 338
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSkDALLEALASLSYKLGG--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877    339 natGTNTYEALNSVYLMMNNQMDRlgmetsaWQE-IRHAIILLTDGKSNMGgsPKPAVDNIREIlgisrnRNDYLDIYAI 417
Cdd:smart00327  78 ---GTNLGAALQYALENLFSKSAG-------SRRgAPKVVILITDGESNDG--PKDLLKAAKEL------KRSGVKVFVV 139

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 47575877    418 GVGKlDVDWKELNELgSKKDGERHAFILQDAKAVQQ 453
Cdd:smart00327 140 GVGN-DVDEEELKKL-ASAPGGVYVFLPELLDLLID 173
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 477-751 2.05e-20

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 91.63  E-value: 2.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 477 NASDQERtPWQVTFKPKS---KETCQGSLISDQWVLTAAHCFHDAQMEDrhlWRVIVG--DPTSHHGKEFHVEEVLVAPG 551
Cdd:COG5640  36 PATVGEY-PWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVVIGstDLSTSGGTVVKVARIVVHPD 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 552 FNVHAkqsqgisefYADDIALLKLSQRVkmsSHARPICLpctvgANMALRRSPGSTckdhetellsqqkvpahFVAL--- 628
Cdd:COG5640 112 YDPAT---------PGNDIALLKLATPV---PGVAPAPL-----ATSADAAAPGTP-----------------ATVAgwg 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 629 ----NGNRMNINLRTGPertscIEAVSQNKgsfpgLTNVSEVVTDQFLCSG-MEGDDSPCKGESGGAVFLERRYRFFQVG 703
Cdd:COG5640 158 rtseGPGSQSGTLRKAD-----VPVVSDAT-----CAAYGGFDGGTMLCAGyPEGGKDACQGDSGGPLVVKDGGGWVLVG 227

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 47575877 704 LVSWGLfDPCHGSSNknlrrkpphGVVPRdfhISLFRlqPWLRQHLDG 751
Cdd:COG5640 228 VVSWGG-GPCAAGYP---------GVYTR---VSAYR--DWIKSTAGG 260
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 94-149 8.19e-16

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: 72.11  E-value: 8.19e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 47575877  94 CPAPTSFENGIYIPRLGSYPVGGNLSFECEHGFTLRGSPVRYCRPNGVWDGETAVC 149
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 94-149 1.30e-13

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: 65.63  E-value: 1.30e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 47575877     94 CPAPTSFENGIYIPRLGSYPVGGNLSFECEHGFTLRGSPVRYCRPNGVWDGETAVC 149
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
94-149 3.62e-12

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 61.75  E-value: 3.62e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 47575877    94 CPAPTSFENGIYIPRLGSYPVGGNLSFECEHGFTLRGSPVRYCRPNGVWDGETAVC 149
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 211-458 1.74e-11

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: 65.34  E-value: 1.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 211 RQPYSYDFPEDVASALGTSFTHLLGATNPIQKRTENLGRKIQIQRSGHLNLYLLLDASQSVSEKD-FNIFKESAFLMVDR 289
Cdd:COG1240  45 AGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDD 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 290 IFSfeiKVSVAIITFASRPKIIMSVlnerSQNVMEVMDSLDSVcykdhENATGTNTYEALnsvyLMMNNQMDRLGMETSA 369
Cdd:COG1240 125 YRP---RDRVGLVAFGGEAEVLLPL----TRDREALKRALDEL-----PPGGGTPLGDAL----ALALELLKRADPARRK 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 370 wqeirhAIILLTDGKSNMG-GSPKPAVDNIREiLGIsrnrndylDIYAIGVGKLDVDWKELNELGSKKDGErhAFILQDA 448
Cdd:COG1240 189 ------VIVLLTDGRDNAGrIDPLEAAELAAA-AGI--------RIYTIGVGTEAVDEGLLREIAEATGGR--YFRADDL 251

                       250
                ....*....|
gi 47575877 449 KAVQQVFEHI 458
Cdd:COG1240 252 SELAAIYREI 261
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 22-210 5.12e-10

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 60.82  E-value: 5.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   22 CPQNVNIVGGNFTLSrGWAPGSVLIYSCPLGRY---PSPAWRECQSNGQ--WQtPRASslptlrssrlakaVCKPVRCPA 96
Cdd:PHA02927  86 CPSPRDIDNGQLDIG-GVDFGSSITYSCNSGYQligESKSYCELGSTGSmvWN-PEAP-------------ICESVKCQS 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   97 PTSFENGIYIPRLGSYPVGGNLSFECEHGFTLRGSPVRYCRpNGVWDgETAVCDngASHCPNPGISVGTMRTG--SSFDL 174
Cdd:PHA02927 151 PPSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGfkRSYSY 226

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 47575877  175 GDKVSYRCSStNLVLTGSVERECLSNGVWSGSEPIC 210
Cdd:PHA02927 227 NDNVDFKCKY-GYKLSGSSSSTCSPGNTWQPELPKC 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 156-211 1.80e-09

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: 54.01  E-value: 1.80e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 47575877 156 CPNPGISV-GTMRTGS-SFDLGDKVSYRCSStNLVLTGSVERECLSNGVWSGSEPICR 211
Cdd:cd00033   1 CPPPPVPEnGTVTGSKgSYSYGSTVTYSCNE-GYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 156-210 3.54e-09

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: 53.30  E-value: 3.54e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 47575877    156 CPNPG-ISVGTMRTGS-SFDLGDKVSYRCSStNLVLTGSVERECLSNGVWSGSEPIC 210
Cdd:smart00032   1 CPPPPdIENGTVTSSSgTYSYGDTVTYSCDP-GYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
168-210 1.70e-04

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 40.18  E-value: 1.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 47575877   168 TGSSFDLGDKVSYRCSStNLVLTGSVERECLSNGVWSGSEPIC 210
Cdd:pfam00084  15 TKNEYNYGASVSYECDP-GYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02831 PHA02831
EEV host range protein; Provisional
 88-142 2.01e-03

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 40.75  E-value: 2.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 47575877   88 VCKPVRCPAPtSFENGIYIPRLGSYPVGGNLSFECEHGFTLRGSPVRYCRPNGVW 142
Cdd:PHA02831 135 VCKLIRCKYP-ALQNGFLNVFEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSIW 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 ...
 259-456 1.10e-83

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: 264.15  E-value: 1.10e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 259 LNLYLLLDASQSVSEKDFNIFKESAFLMVDRIFSFEIKVSVAIITFASRPKIIMSVLNERSQNVMEVMDSLDSVCYKDHE 338
Cdd:cd01470   1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 339 NATGTNTYEALNSVYLMMNNQMDRLGMetsAWQEIRHAIILLTDGKSNMGGSPKPAVDNIREILGISR----NRNDYLDI 414
Cdd:cd01470  81 DKTGTNTAAALKKVYERMALEKVRNKE---AFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNksdnPREDYLDV 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 47575877 415 YAIGVGKlDVDWKELNELGSKKDGERHAFILQDAKAVQQVFE 456
Cdd:cd01470 158 YVFGVGD-DVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 479-748 2.25e-37

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: 139.72  E-value: 2.25e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 479 SDQERTPWQVT-FKPKSKETCQGSLISDQWVLTAAHCFHDAQMEDrhlWRVIVGD----PTSHHGKEFHVEEVLVAPGFN 553
Cdd:cd00190   7 AKIGSFPWQVSlQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGShdlsSNEGGGQVIKVKKVIVHPNYN 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 554 vhakqsqgiSEFYADDIALLKLSQRVKMSSHARPICLPCTvGANMAlrrsPGSTC------KDHETELLSQ--QKVpahf 625
Cdd:cd00190  84 ---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSS-GYNLP----AGTTCtvsgwgRTSEGGPLPDvlQEV---- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 626 valngnrmNINLRTgpeRTSCIEAVSQNkgsfpgltnvsEVVTDQFLCSG-MEGDDSPCKGESGGAVFLERRYRFFQVGL 704
Cdd:cd00190 146 --------NVPIVS---NAECKRAYSYG-----------GTITDNMLCAGgLEGGKDACQGDSGGPLVCNDNGRGVLVGI 203

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 47575877 705 VSWGLFdpChGSSNKnlrrkpphgvvPRDFHIsLFRLQPWLRQH 748
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 ...
 479-719 8.94e-36

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: 135.11  E-value: 8.94e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877    479 SDQERTPWQVT-FKPKSKETCQGSLISDQWVLTAAHCFHDAqmeDRHLWRVIVGD---PTSHHGKEFHVEEVLVAPGFNv 554
Cdd:smart00020   8 ANIGSFPWQVSlQYGGGRHFCGGSLISPRWVLTAAHCVRGS---DPSNIRVRLGShdlSSGEEGQVIKVSKVIIHPNYN- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877    555 hakqsqgiSEFYADDIALLKLSQRVKMSSHARPICLPCTvganmALRRSPGSTCKD---HETELlsqqKVPAHFVALngn 631
Cdd:smart00020  84 --------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCTVsgwGRTSE----GAGSLPDTL--- 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877    632 rMNINLRTGPERTsCIEAVSQNkgsfpgltnvsEVVTDQFLCSG-MEGDDSPCKGESGGAVFLERRyRFFQVGLVSWGlf 710
Cdd:smart00020 144 -QEVNVPIVSNAT-CRRAYSGG-----------GAITDNMLCAGgLEGGKDACQGDSGGPLVCNDG-RWVLVGIVSWG-- 207


                   ....*....
gi 47575877    711 DPChGSSNK 719
Cdd:smart00020 208 SGC-ARPGK 215
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 259-443 7.81e-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: 7.81e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 259 LNLYLLLDASQSVSEKDFNIFKESAFLMVDRIFSFEIKVSVAIITFASRPKIIMSVLNERSQNvmEVMDSLDSVCYKDHe 338
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKD--DLLKAVKNLKYLGG- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 339 naTGTNTYEALNSVYLMMNNqmdrlgmETSAWQEIRHAIILLTDGKSNMGGSPKPAVDNIREIlgisrnrndYLDIYAIG 418
Cdd:cd01450  78 --GGTNTGKALQYALEQLFS-------ESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDE---------GIKVFVVG 139

                       170       180
                ....*....|....*....|....*
gi 47575877 419 VGklDVDWKELNELGSKKdGERHAF 443
Cdd:cd01450 140 VG--PADEEELREIASCP-SERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
260-457 1.26e-30

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 118.53  E-value: 1.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   260 NLYLLLDASQSVSEKDFNIFKESAFLMVDRIFSFEIKVSVAIITFASRPKIIMSvLNErSQNVMEVMDSLDSVCYKDHEN 339
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFP-LND-YSSKEELLSAVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   340 A-TGTNTYEALNSVYLMMNNQmdRLGmetsawqeIRHAIILLTDGKSNMgGSPKPAVDNIREiLGISrnrndyldIYAIG 418
Cdd:pfam00092  79 TnTGKALKYALENLFSSAAGA--RPG--------APKVVVLLTDGRSQD-GDPEEVARELKS-AGVT--------VFAVG 138

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 47575877   419 VGklDVDWKELNELGSKKDgERHAFILQDAKAVQQVFEH 457
Cdd:pfam00092 139 VG--NADDEELRKIASEPG-EGHVFTVSDFEALEDLQDQ 174
Trypsin pfam00089
Trypsin;
485-745 3.04e-27

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 110.22  E-value: 3.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   485 PWQVTFK-PKSKETCQGSLISDQWVLTAAHCFHdaqmeDRHLWRVIVGDPTSHHG----KEFHVEEVLVAPGFNvhakqs 559
Cdd:pfam00089  13 PWQVSLQlSSGKHFCGGSLISENWVLTAAHCVS-----GASDVKVVLGAHNIVLReggeQKFDVEKIIVHPNYN------ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   560 qgiSEFYADDIALLKLSQRVKMSSHARPICLPCTvganmALRRSPGSTCkdhetellsqqkvpahFVALNGNRMNINLrt 639
Cdd:pfam00089  82 ---PDTLDNDIALLKLESPVTLGDTVRPICLPDA-----SSDLPVGTTC----------------TVSGWGNTKTLGP-- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   640 gPERTSCIE--AVSQNKGSfpglTNVSEVVTDQFLCSGMEGDDSpCKGESGGAVFLERRYrffQVGLVSWGlfDPChgss 717
Cdd:pfam00089 136 -SDTLQEVTvpVVSRETCR----SAYGGTVTDTMICAGAGGKDA-CQGDSGGPLVCSDGE---LIGIVSWG--YGC---- 200

                         250       260
                  ....*....|....*....|....*...
gi 47575877   718 nkNLRRKPphgvvprDFHISLFRLQPWL 745
Cdd:pfam00089 201 --ASGNYP-------GVYTPVSSYLDWI 219
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 260-453 1.53e-25

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: 104.07  E-value: 1.53e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877    260 NLYLLLDASQSVSEKDFNIFKESAFLMVDRIFSFEIKVSVAIITFASRPKIIMSVLNERS-QNVMEVMDSLDSVCYKdhe 338
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSkDALLEALASLSYKLGG--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877    339 natGTNTYEALNSVYLMMNNQMDRlgmetsaWQE-IRHAIILLTDGKSNMGgsPKPAVDNIREIlgisrnRNDYLDIYAI 417
Cdd:smart00327  78 ---GTNLGAALQYALENLFSKSAG-------SRRgAPKVVILITDGESNDG--PKDLLKAAKEL------KRSGVKVFVV 139

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 47575877    418 GVGKlDVDWKELNELgSKKDGERHAFILQDAKAVQQ 453
Cdd:smart00327 140 GVGN-DVDEEELKKL-ASAPGGVYVFLPELLDLLID 173
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 477-751 2.05e-20

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 91.63  E-value: 2.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 477 NASDQERtPWQVTFKPKS---KETCQGSLISDQWVLTAAHCFHDAQMEDrhlWRVIVG--DPTSHHGKEFHVEEVLVAPG 551
Cdd:COG5640  36 PATVGEY-PWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVVIGstDLSTSGGTVVKVARIVVHPD 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 552 FNVHAkqsqgisefYADDIALLKLSQRVkmsSHARPICLpctvgANMALRRSPGSTckdhetellsqqkvpahFVAL--- 628
Cdd:COG5640 112 YDPAT---------PGNDIALLKLATPV---PGVAPAPL-----ATSADAAAPGTP-----------------ATVAgwg 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 629 ----NGNRMNINLRTGPertscIEAVSQNKgsfpgLTNVSEVVTDQFLCSG-MEGDDSPCKGESGGAVFLERRYRFFQVG 703
Cdd:COG5640 158 rtseGPGSQSGTLRKAD-----VPVVSDAT-----CAAYGGFDGGTMLCAGyPEGGKDACQGDSGGPLVVKDGGGWVLVG 227

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 47575877 704 LVSWGLfDPCHGSSNknlrrkpphGVVPRdfhISLFRlqPWLRQHLDG 751
Cdd:COG5640 228 VVSWGG-GPCAAGYP---------GVYTR---VSAYR--DWIKSTAGG 260
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 259-440 7.48e-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: 84.15  E-value: 7.48e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 259 LNLYLLLDASQSVSEKDFNIFKESAFLMVDRIFSFEIKVSVAIITFASRPKIIMSVLNERS-QNVMEVMDSLdsvcykDH 337
Cdd:cd00198   1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDkADLLEAIDAL------KK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 338 ENATGTNTYEALNSVYLMMNNQMDRLGmetsawqeiRHAIILLTDGKSNmgGSPKPAVDNIREIlgisrnRNDYLDIYAI 417
Cdd:cd00198  75 GLGGGTNIGAALRLALELLKSAKRPNA---------RRVIILLTDGEPN--DGPELLAEAAREL------RKLGITVYTI 137

                       170       180
                ....*....|....*....|...
gi 47575877 418 GVGkLDVDWKELNELGSKKDGER 440
Cdd:cd00198 138 GIG-DDANEDELKEIADKTTGGA 159
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 94-149 8.19e-16

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: 72.11  E-value: 8.19e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 47575877  94 CPAPTSFENGIYIPRLGSYPVGGNLSFECEHGFTLRGSPVRYCRPNGVWDGETAVC 149
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 94-149 1.30e-13

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: 65.63  E-value: 1.30e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 47575877     94 CPAPTSFENGIYIPRLGSYPVGGNLSFECEHGFTLRGSPVRYCRPNGVWDGETAVC 149
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
94-149 3.62e-12

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 61.75  E-value: 3.62e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 47575877    94 CPAPTSFENGIYIPRLGSYPVGGNLSFECEHGFTLRGSPVRYCRPNGVWDGETAVC 149
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 211-458 1.74e-11

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: 65.34  E-value: 1.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 211 RQPYSYDFPEDVASALGTSFTHLLGATNPIQKRTENLGRKIQIQRSGHLNLYLLLDASQSVSEKD-FNIFKESAFLMVDR 289
Cdd:COG1240  45 AGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDD 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 290 IFSfeiKVSVAIITFASRPKIIMSVlnerSQNVMEVMDSLDSVcykdhENATGTNTYEALnsvyLMMNNQMDRLGMETSA 369
Cdd:COG1240 125 YRP---RDRVGLVAFGGEAEVLLPL----TRDREALKRALDEL-----PPGGGTPLGDAL----ALALELLKRADPARRK 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 370 wqeirhAIILLTDGKSNMG-GSPKPAVDNIREiLGIsrnrndylDIYAIGVGKLDVDWKELNELGSKKDGErhAFILQDA 448
Cdd:COG1240 189 ------VIVLLTDGRDNAGrIDPLEAAELAAA-AGI--------RIYTIGVGTEAVDEGLLREIAEATGGR--YFRADDL 251

                       250
                ....*....|
gi 47575877 449 KAVQQVFEHI 458
Cdd:COG1240 252 SELAAIYREI 261
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 248-490 4.28e-11

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 64.35  E-value: 4.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 248 GRKIQIQRSGHLNLYLLLDASQSVSEKDFNIFKESAFLMVDRIfsfEIKVSVAIITFASRPKIIMSVLneRSQNVMEVMD 327
Cdd:COG2304  81 PPKAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQL---RPGDRVSIVTFAGDARVLLPPT--PATDRAKILA 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 328 SLDSVcykdheNATG-TNTYEALNSVYLMMNNQMDRLGmetsawqeIRHaIILLTDGKSNMGGSpkpAVDNIREILGISR 406
Cdd:COG2304 156 AIDRL------QAGGgTALGAGLELAYELARKHFIPGR--------VNR-VILLTDGDANVGIT---DPEELLKLAEEAR 217

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 407 NRNdyLDIYAIGVGkldVDWKE--LNELGSKKDGeRHAFIlQDAKAVQQVFEhildvsKLTDTIcGVGNMSVNASDQERT 484
Cdd:COG2304 218 EEG--ITLTTLGVG---SDYNEdlLERLADAGGG-NYYYI-DDPEEAEKVFV------REFSRI-GYENRALATEDFPLP 283


                ....*.
gi 47575877 485 PWQVTF 490
Cdd:COG2304 284 YGTLKL 289
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 260-447 4.08e-10

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: 59.16  E-value: 4.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 260 NLYLLLDASQSVSEKDFNIFKESAFLMVDRifsFEI---KVSVAIITFASRPKIImSVLNeRSQNVMEVMDSLDSVCYKd 336
Cdd:cd01472   2 DIVFLVDGSESIGLSNFNLVKDFVKRVVER---LDIgpdGVRVGVVQYSDDPRTE-FYLN-TYRSKDDVLEAVKNLRYI- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 337 henATGTNTYEALNsvYLMMNNQMDRLGMEtsawQEIRHAIILLTDGKSNMGGsPKPAVdNIREiLGISrnrndyldIYA 416
Cdd:cd01472  76 ---GGGTNTGKALK--YVRENLFTEASGSR----EGVPKVLVVITDGKSQDDV-EEPAV-ELKQ-AGIE--------VFA 135

                       170       180       190
                ....*....|....*....|....*....|.
gi 47575877 417 IGVGKLDVDwkELNELGSkKDGERHAFILQD 447
Cdd:cd01472 136 VGVKNADEE--ELKQIAS-DPKELYVFNVAD 163
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 22-210 5.12e-10

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 60.82  E-value: 5.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   22 CPQNVNIVGGNFTLSrGWAPGSVLIYSCPLGRY---PSPAWRECQSNGQ--WQtPRASslptlrssrlakaVCKPVRCPA 96
Cdd:PHA02927  86 CPSPRDIDNGQLDIG-GVDFGSSITYSCNSGYQligESKSYCELGSTGSmvWN-PEAP-------------ICESVKCQS 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   97 PTSFENGIYIPRLGSYPVGGNLSFECEHGFTLRGSPVRYCRpNGVWDgETAVCDngASHCPNPGISVGTMRTG--SSFDL 174
Cdd:PHA02927 151 PPSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGfkRSYSY 226

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 47575877  175 GDKVSYRCSStNLVLTGSVERECLSNGVWSGSEPIC 210
Cdd:PHA02927 227 NDNVDFKCKY-GYKLSGSSSSTCSPGNTWQPELPKC 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 156-211 1.80e-09

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: 54.01  E-value: 1.80e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 47575877 156 CPNPGISV-GTMRTGS-SFDLGDKVSYRCSStNLVLTGSVERECLSNGVWSGSEPICR 211
Cdd:cd00033   1 CPPPPVPEnGTVTGSKgSYSYGSTVTYSCNE-GYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 156-210 3.54e-09

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: 53.30  E-value: 3.54e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 47575877    156 CPNPG-ISVGTMRTGS-SFDLGDKVSYRCSStNLVLTGSVERECLSNGVWSGSEPIC 210
Cdd:smart00032   1 CPPPPdIENGTVTSSSgTYSYGDTVTYSCDP-GYTLIGSSTITCLENGTWSPPPPTC 56
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 263-447 1.11e-08

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: 54.99  E-value: 1.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 263 LLLDASQSVSEKDFNIFKEsaFLmVDRIFSFEI---KVSVAIITFASRPKI--IMSVLNERSQnvmeVMDSLDSVCYKdh 337
Cdd:cd01482   5 FLVDGSWSIGRSNFNLVRS--FL-SSVVEAFEIgpdGVQVGLVQYSDDPRTefDLNAYTSKED----VLAAIKNLPYK-- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 338 enATGTNTYEALNsvYLMMNNQMDRLGMEtsawQEIRHAIILLTDGKSNmggspkpavDNIREIlgISRNRNDYLDIYAI 417
Cdd:cd01482  76 --GGNTRTGKALT--HVREKNFTPDAGAR----PGVPKVVILITDGKSQ---------DDVELP--ARVLRNLGVNVFAV 136

                       170       180       190
                ....*....|....*....|....*....|
gi 47575877 418 GVGklDVDWKELNELGSKKDgERHAFILQD 447
Cdd:cd01482 137 GVK--DADESELKMIASKPS-ETHVFNVAD 163
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 259-451 1.31e-08

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: 54.97  E-value: 1.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 259 LNLYLLLDASQSVSEKDFNIFKESAFLMVDRIfsfEIKVSVAIITFASRPKIIMSvlNERSQNVMEVMDSLDSVcykdhE 338
Cdd:cd01465   1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQL---RPDDRLAIVTYDGAAETVLP--ATPVRDKAAILAAIDRL-----T 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 339 NATGTNTYEALNSVYLMMNNQMDRLGMetsawqeirHAIILLTDGKSNMGgspkpaVDNIREILGISRNRNDY-LDIYAI 417
Cdd:cd01465  71 AGGSTAGGAGIQLGYQEAQKHFVPGGV---------NRILLATDGDFNVG------ETDPDELARLVAQKRESgITLSTL 135

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 47575877 418 GVGKldvDWKE--LNELGSKKDGeRHAFI--LQDAKAV 451
Cdd:cd01465 136 GFGD---NYNEdlMEAIADAGNG-NTAYIdnLAEARKV 169
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 257-471 4.13e-08

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: 54.70  E-value: 4.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 257 GHLNLYLLLDASQSVSEKDFNIFKESAFLMVDRIFSFEIKVSVAIITFASRPKIIMSVLNERSQNVME----VMDSLdsv 332
Cdd:cd01475   1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKravrRMEYL--- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 333 cykdhenATGTNTYEALNsvYLMMNNQMDRLGMETSAwQEIRHAIILLTDGKSNmggspkpavDNIREIlgISRNRNDYL 412
Cdd:cd01475  78 -------ETGTMTGLAIQ--YAMNNAFSEAEGARPGS-ERVPRVGIVVTDGRPQ---------DDVSEV--AAKARALGI 136

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 47575877 413 DIYAIGVGKLDVDwkELNELGSKKDGErHAFILQDAKAVQQVfehildVSKLTDTICGV 471
Cdd:cd01475 137 EMFAVGVGRADEE--ELREIASEPLAD-HVFYVEDFSTIEEL------TKKFQGKICVV 186
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 257-462 2.89e-07

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: 51.36  E-value: 2.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 257 GHLNLYLLLDASQSVSEKDFNIFKesaFL--MVDRIFSFEIKVSvaIITFASRPKIIMSVLNERSQnVMEVMDSLDSVcy 334
Cdd:cd01474   3 GHFDLYFVLDKSGSVAANWIEIYD---FVeqLVDRFNSPGLRFS--FITFSTRATKILPLTDDSSA-IIKGLEVLKKV-- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 335 kdhenATGTNTY--EALNSVYLMMNNQmDRLGMETSAwqeirhAIILLTDGKSNMggspKPAVDNIREilgISRNRNDYL 412
Cdd:cd01474  75 -----TPSGQTYihEGLENANEQIFNR-NGGGRETVS------VIIALTDGQLLL----NGHKYPEHE---AKLSRKLGA 135

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 47575877 413 DIYAIGVgkLDVDWKELNELGSKKDgerHAFILQDA-KAVQQVFEHILDVS 462
Cdd:cd01474 136 IVYCVGV--TDFLKSQLINIADSKE---YVFPVTSGfQALSGIIESVVKKA 181
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 498-579 6.18e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 50.45  E-value: 6.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 498 CQGSLISDQWVLTAAHCFHDAQMEDRH-LWRVIVGDPTSHHGkEFHVEEVLVAPGFnvhakqsqGISEFYADDIALLKLS 576
Cdd:COG3591  14 CTGTLIGPNLVLTAGHCVYDGAGGGWAtNIVFVPGYNGGPYG-TATATRFRVPPGW--------VASGDAGYDYALLRLD 84


                ...
gi 47575877 577 QRV 579
Cdd:COG3591  85 EPL 87
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 89-211 6.29e-07

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 51.58  E-value: 6.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   89 CKPVRCPAPTSFENGIYipRLGSYPVGGNLSFECEHGFTLRGSPVRYCRPNG----VWDGETAVCDNGASHCPnPGISVG 164
Cdd:PHA02927  81 CIKRRCPSPRDIDNGQL--DIGGVDFGSSITYSCNSGYQLIGESKSYCELGStgsmVWNPEAPICESVKCQSP-PSISNG 157

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 47575877  165 TMRTGSSFDL-GDKVSYRCSStNLVLTGSVEREClSNGVWSgSEPICR 211
Cdd:PHA02927 158 RHNGYEDFYTdGSVVTYSCNS-GYSLIGNSGVLC-SGGEWS-DPPTCQ 202
PHA02639 PHA02639
EEV host range protein; Provisional
 90-211 1.71e-05

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 47.35  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   90 KPVRCPAPTSFENGIYIPRLGSYPVGGNLSFECEHGFTLRGSPVRYC---RPNGVWDGETAVCDNGASHCPNPGISVGTM 166
Cdd:PHA02639  18 KSIYCDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCikdKNNAIWSNKAPFCMLKECNDPPSIINGKIY 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 47575877  167 RTGSSFDLGDKVSYRCSSTNLV---LTGSVERECLSNGVWSGSEPICR 211
Cdd:PHA02639  98 NKREMYKVGDEIYYVCNEHKGVqysLVGNEKITCIQDKSWKPDPPICK 145
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 259-444 1.74e-05

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 45.85  E-value: 1.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 259 LNLYLLLDASQSVSEKdfniFKESAFLMVDRIFSFEI---KVSVAIITFASRPKIIMSVLNERSQNVMEVMDSLDSVCYK 335
Cdd:cd01476   1 LDLLFVLDSSGSVRGK----FEKYKKYIERIVEGLEIgptATRVALITYSGRGRQRVRFNLPKHNDGEELLEKVDNLRFI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 336 DHENATGTNTYEALNSvylmmnnqmdrlgMETSAWQEIRHA--IILLTDGKSNmgGSPKPAVDNIREILGIsrnrndylD 413
Cdd:cd01476  77 GGTTATGAAIEVALQQ-------------LDPSEGRREGIPkvVVVLTDGRSH--DDPEKQARILRAVPNI--------E 133

                       170       180       190
                ....*....|....*....|....*....|..
gi 47575877 414 IYAIGVG-KLDVDWKELNELGSKkdgERHAFI 444
Cdd:cd01476 134 TFAVGTGdPGTVDTEELHSITGN---EDHIFT 162
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 92-221 4.69e-05

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 46.23  E-value: 4.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   92 VRCP----APTSFENGIYIPRLGSYPVGGNLSFECEHGFTLRGSPVRYCRPNGvWDgetaVCDNGASHCPNPGISVGTMr 167
Cdd:PHA02954 123 VTCPnaecQPLQLEHGSCQPVKEKYSFGEHITINCDVGYEVIGASYISCTANS-WN----VIPSCQQKCDIPSLSNGLI- 196

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 47575877  168 TGSSFDLGDKVSYRCSStNLVLTGSVERECLsNGVWSGSEPIC-RQPYSYDFPED 221
Cdd:PHA02954 197 SGSTFSIGGVIHLSCKS-GFTLTGSPSSTCI-DGKWNPVLPICvRSNEEFDPVDD 249
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 264-450 4.76e-05

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: 44.65  E-value: 4.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 264 LLDASQSVSEKDFNIFKEsaFL--MVDRIFSFEIKVSVAIITFASRPKIIMSvLNErSQNVMEVMDSLDSVcykdHENAT 341
Cdd:cd01469   6 VLDGSGSIYPDDFQKVKN--FLstVMKKLDIGPTKTQFGLVQYSESFRTEFT-LNE-YRTKEEPLSLVKHI----SQLLG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 342 GTNTYEALNSVylmmnnqMDRLGMETS-AWQEIRHAIILLTDGKSNmGGSPKPAVDNIREILGISRnrndyldiYAIGVG 420
Cdd:cd01469  78 LTNTATAIQYV-------VTELFSESNgARKDATKVLVVITDGESH-DDPLLKDVIPQAEREGIIR--------YAIGVG 141

                       170       180       190
                ....*....|....*....|....*....|...
gi 47575877 421 KL---DVDWKELNELGSKKDgERHAFILQDAKA 450
Cdd:cd01469 142 GHfqrENSREELKTIASKPP-EEHFFNVTDFAA 173
PHA02817 PHA02817
EEV Host range protein; Provisional
 89-238 4.86e-05

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 45.32  E-value: 4.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   89 CKPVRCPAPTSFENGIYIPRLGSYPVGGNLSFECEHG-----FTLRGSPVRYCRPNGVWDGETAVCDngASHCPNPGIS- 162
Cdd:PHA02817  19 CDLNKCCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCK--IIRCRFPALQn 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877  163 --VGTMRTGSSFDLGDKVSYRCSStNLVLTGSVERECLSNGVWSGSEPIC-RQPYSY------------DFPEDVASALG 227
Cdd:PHA02817  97 gfVNGIPDSKKFYYESEVSFSCKP-GFVLIGTKYSVCGINSSWIPKVPICsRDNITYnkiyinkvniddNFFNQINNSNT 175

                        170
                 ....*....|.
gi 47575877  228 TSFTHLLGATN 238
Cdd:PHA02817 176 YYFDKILQINN 186
Sushi pfam00084
Sushi repeat (SCR repeat);
168-210 1.70e-04

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 40.18  E-value: 1.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 47575877   168 TGSSFDLGDKVSYRCSStNLVLTGSVERECLSNGVWSGSEPIC 210
Cdd:pfam00084  15 TKNEYNYGASVSYECDP-GYRLVGSPTITCQEDGTWSPPFPEC 56
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
258-458 5.86e-04

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 41.83  E-value: 5.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 258 HLNLYLLLDASQSVSEKDFNIFKESAFLMVDRIFSFEI---KVSVAIITFASRPKIIMSvLNERSQNVMEVMdsldsvcy 334
Cdd:COG4245   5 RLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYaleTVEVSVITFDGEAKVLLP-LTDLEDFQPPDL-------- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 335 kdheNATG-TNTYEALNsvylMMNNQMDRLGMETSAWQEIRHA--IILLTDGKSNmGGSPKPAVDNIREilgisRNRNDY 411
Cdd:COG4245  76 ----SASGgTPLGAALE----LLLDLIERRVQKYTAEGKGDWRpvVFLITDGEPT-DSDWEAALQRLKD-----GEAAKK 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 47575877 412 LDIYAIGVGKlDVDWKELNELGskkDGERhAFILQDAKAVQQVFEHI 458
Cdd:COG4245 142 ANIFAIGVGP-DADTEVLKQLT---DPVR-ALDALDGLDFREFFKWL 183
VWA_2 pfam13519
von Willebrand factor type A domain;
261-359 1.27e-03

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 38.81  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   261 LYLLLDASQSVSEKDFNIFKESAFL-MVDRIFSFEIKVSVAIITFASRPKIIMSvLNERSQNVMEVMDSLDsvcykdhEN 339
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRLEAAKdAVLALLKSLPGDRVGLVTFGDGPEVLIP-LTKDRAKILRALRRLE-------PK 72

                          90       100
                  ....*....|....*....|
gi 47575877   340 ATGTNTYEALNSVYLMMNNQ 359
Cdd:pfam13519  73 GGGTNLAAALQLARAALKHR 92
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 257-385 1.77e-03

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: 40.06  E-value: 1.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877 257 GHLNLYLLLDASQSVSEKDFNIFKESAFLMVDRIFSFEIK------VSVAIITFASRPKIImSVLNERSQNVMEVMDSLD 330
Cdd:cd01480   1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRkdpagsWRVGVVQYSDQQEVE-AGFLRDIRNYTSLKEAVD 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 47575877 331 SVCYKdhenATGTNTYEALNSVYlmmnNQMdrlgMETSAWQEIRHAiILLTDGKS 385
Cdd:cd01480  80 NLEYI----GGGTFTDCALKYAT----EQL----LEGSHQKENKFL-LVITDGHS 121
PHA02831 PHA02831
EEV host range protein; Provisional
 88-142 2.01e-03

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 40.75  E-value: 2.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 47575877   88 VCKPVRCPAPtSFENGIYIPRLGSYPVGGNLSFECEHGFTLRGSPVRYCRPNGVW 142
Cdd:PHA02831 135 VCKLIRCKYP-ALQNGFLNVFEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSIW 188
PHA02831 PHA02831
EEV host range protein; Provisional
 64-210 5.35e-03

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 39.59  E-value: 5.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575877   64 SNGQWQTprasslptlrssrlaKAVCKPVR-CPAPTSFENGIYIPRLGSYPVGGNLSFECE----HGFTLRGSPVRYCrP 138
Cdd:PHA02831  62 NNGSWST---------------KNMCIGKRnCKDPVTILNGYIKNKKDQYSFGDSVTYACKvnklEKYSIVGNETVKC-I 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47575877  139 NGVWDGETAVCDngASHCPNPGISVGTMRT-GSSFDLGDKVSYRCSsTNLVLTGSVERECLSNGVWSGSEPIC 210
Cdd:PHA02831 126 NKQWVPKYPVCK--LIRCKYPALQNGFLNVfEKKFYYGDIVNFKCK-KGFILLGSSVSTCDINSIWYPGIPKC 195
PHA02817 PHA02817
EEV Host range protein; Provisional
 88-149 7.06e-03

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 38.77  E-value: 7.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47575877   88 VCKPVRCPAPtSFENGIY--IPRLGSYPVGGNLSFECEHGFTLRGSPVRYCRPNGVWDGETAVC 149
Cdd:PHA02817  83 VCKIIRCRFP-ALQNGFVngIPDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPIC 145
Sushi pfam00084
Sushi repeat (SCR repeat);
22-71 7.47e-03

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 35.55  E-value: 7.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 47575877    22 CPQNVNIVGGNFTLSRG-WAPGSVLIYSCPLG-RYPSPAWRECQSNGQWQTP 71
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNeYNYGASVSYECDPGyRLVGSPTITCQEDGTWSPP 52
 
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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