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Conserved domains on  [gi|1839487038|ref|XP_034034299|]
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complement factor B-like isoform X2 [Thalassophryne amazonica]

Protein Classification

VWA domain-containing protein( domain architecture ID 13332055)

VWA (von Willebrand factor type A) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 260-460 2.04e-79

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: 252.98  E-value: 2.04e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 260 LNIYIAVDVSESITKDDFISARNAVLKLITKIASFSVTPNYEIVFFAAEIFEIVNIIDFLDNKqeLHRIKTALETFTVGE 339
Cdd:cd01470     1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSND--ADDVIKRLEDFNYDD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 340 KEL-TGTDLNLVFRKMLEQIAVIKQRAGETFKDYHHVIIVFTDGAYNMGGSPAQTVAAIKQMVYMNPTggeDTNKRDEYL 418
Cdd:cd01470    79 HGDkTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNK---SDNPREDYL 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1839487038 419 DIYIFGIGGEIFDDDLNQLTVGTGG-QHFFKLKDLVQLQETFD 460
Cdd:cd01470   156 DVYVFGVGDDVNKEELNDLASKKDNeRHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 487-713 7.76e-36

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: 135.48  E-value: 7.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 487 HPWIAeiRVQNEGSSQKCLGSLVTPKFVLTAAHCFRfGDLPKHVTV-------DIDDGQGRVKRVQNFTLHPKYNVNaqk 559
Cdd:cd00190    12 FPWQV--SLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVrlgshdlSSNEGGGQVIKVKKVIVHPNYNPS--- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 560 annvdeFYDYDVALIELVEYVQISTDVRPICIPCTQETSAAlkivrDTTC------KQQEQLLLNKQneplmfltksrgq 633
Cdd:cd00190    86 ------TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPA-----GTTCtvsgwgRTSEGGPLPDV------------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 634 meKKDVNAKLGDNrKECISHALKAKGIrtqnvslvvTDNFLCTGGLFPQRDhiACTGDSGGAVFKNYEHRTIQVALVSWG 713
Cdd:cd00190   142 --LQEVNVPIVSN-AECKRAYSYGGTI---------TDNMLCAGGLEGGKD--ACQGDSGGPLVCNDNGRGVLVGIVSWG 207
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 97-152 4.99e-18

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: 78.27  E-value: 4.99e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1839487038  97 CPDPTVLLNGNVVPSQEKYFVNNVTTYECYSGYTLYGSSRRVCLPNGKWSGPTPIC 152
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
 53-213 1.56e-15

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 77.39  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  53 GSILIYHCPEEYYPYPDLVRVCQL--TGK--WNPtpkkfRPQRCRLVECPDPTVLLNGNVVPSQEKYFVNNVTTYECYSG 128
Cdd:PHA02927  105 GSSITYSCNSGYQLIGESKSYCELgsTGSmvWNP-----EAPICESVKCQSPPSISNGRHNGYEDFYTDGSVVTYSCNSG 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 129 YTLYGSSRRVClPNGKWSGPtPICSRGSgdhCADPGIPAGASRNG--NQFGIDDKVKYMCNSNLNLVGPSERVCQENGQW 206
Cdd:PHA02927  180 YSLIGNSGVLC-SGGEWSDP-PTCQIVK---CPHPTISNGYLSSGfkRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTW 254


                  ....*..
gi 1839487038 207 TGTEPAC 213
Cdd:PHA02927  255 QPELPKC 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 ...
 260-460 2.04e-79

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: 252.98  E-value: 2.04e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 260 LNIYIAVDVSESITKDDFISARNAVLKLITKIASFSVTPNYEIVFFAAEIFEIVNIIDFLDNKqeLHRIKTALETFTVGE 339
Cdd:cd01470     1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSND--ADDVIKRLEDFNYDD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 340 KEL-TGTDLNLVFRKMLEQIAVIKQRAGETFKDYHHVIIVFTDGAYNMGGSPAQTVAAIKQMVYMNPTggeDTNKRDEYL 418
Cdd:cd01470    79 HGDkTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNK---SDNPREDYL 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1839487038 419 DIYIFGIGGEIFDDDLNQLTVGTGG-QHFFKLKDLVQLQETFD 460
Cdd:cd01470   156 DVYVFGVGDDVNKEELNDLASKKDNeRHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 487-713 7.76e-36

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: 135.48  E-value: 7.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 487 HPWIAeiRVQNEGSSQKCLGSLVTPKFVLTAAHCFRfGDLPKHVTV-------DIDDGQGRVKRVQNFTLHPKYNVNaqk 559
Cdd:cd00190    12 FPWQV--SLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVrlgshdlSSNEGGGQVIKVKKVIVHPNYNPS--- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 560 annvdeFYDYDVALIELVEYVQISTDVRPICIPCTQETSAAlkivrDTTC------KQQEQLLLNKQneplmfltksrgq 633
Cdd:cd00190    86 ------TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPA-----GTTCtvsgwgRTSEGGPLPDV------------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 634 meKKDVNAKLGDNrKECISHALKAKGIrtqnvslvvTDNFLCTGGLFPQRDhiACTGDSGGAVFKNYEHRTIQVALVSWG 713
Cdd:cd00190   142 --LQEVNVPIVSN-AECKRAYSYGGTI---------TDNMLCAGGLEGGKD--ACQGDSGGPLVCNDNGRGVLVGIVSWG 207
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 487-722 6.60e-34

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: 129.72  E-value: 6.60e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  487 HPWIAeiRVQNEGSSQKCLGSLVTPKFVLTAAHCFRfGDLPKHVTV-----DIDDGQGRVKR-VQNFTLHPKYNvnaqka 560
Cdd:smart00020  13 FPWQV--SLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVrlgshDLSSGEEGQVIkVSKVIIHPNYN------ 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  561 nnvDEFYDYDVALIELVEYVQISTDVRPICIPCTQETSAAlkivrDTTCK----QQEQLLLNKQNEPLMfltksrgqmek 636
Cdd:smart00020  84 ---PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPA-----GTTCTvsgwGRTSEGAGSLPDTLQ----------- 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  637 kDVNAKLGDNrKECISHAlkakgirtqNVSLVVTDNFLCTGGLFPQRDhiACTGDSGGAVFKNYeHRTIQVALVSWGTKn 716
Cdd:smart00020 145 -EVNVPIVSN-ATCRRAY---------SGGGAITDNMLCAGGLEGGKD--ACQGDSGGPLVCND-GRWVLVGIVSWGSG- 209


                   ....*.
gi 1839487038  717 lCQSGG 722
Cdd:smart00020 210 -CARPG 214
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 487-722 7.21e-23

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 98.95  E-value: 7.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 487 HPWIAEIRVQNEGSSQKCLGSLVTPKFVLTAAHCFrFGDLPKHVTV-----DIDDGQGRVKRVQNFTLHPKYNVNAqkan 561
Cdd:COG5640    42 YPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCV-DGDGPSDLRVvigstDLSTSGGTVVKVARIVVHPDYDPAT---- 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 562 nvdefYDYDVALIELVEYVqisTDVRPICIPCTQETSAALKIVR--------DTTCKQQEQLllnkqneplmfltksrgq 633
Cdd:COG5640   117 -----PGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATvagwgrtsEGPGSQSGTL------------------ 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 634 mekKDVNAKLGDNRkECishalkakgirtQNVSLVVTDNFLCTGGLFPQRDhiACTGDSGGAVFKNYEHRTIQVALVSWG 713
Cdd:COG5640   171 ---RKADVPVVSDA-TC------------AAYGGFDGGTMLCAGYPEGGKD--ACQGDSGGPLVVKDGGGWVLVGVVSWG 232


                  ....*....
gi 1839487038 714 TkNLCQSGG 722
Cdd:COG5640   233 G-GPCAAGY 240
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 261-464 2.02e-22

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 94.83  E-value: 2.02e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  261 NIYIAVDVSESITKDDFISARNAVLKLITKIASFSVTPNYEIVFFAAEIFEIVNIIDFlDNKQELHRIKTALETFTVGek 340
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDS-RSKDALLEALASLSYKLGG-- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  341 eltGTDLNLVFRKMLEQIAVIKQRAGetfKDYHHVIIVFTDGAYNMGGSPAQTVAAikqmvymnptggedtNKRDEYLDI 420
Cdd:smart00327  78 ---GTNLGAALQYALENLFSKSAGSR---RGAPKVVILITDGESNDGPKDLLKAAK---------------ELKRSGVKV 136

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1839487038  421 YIFGIGGEIFDDDLNQLTVGTGGQHFFklkdlvqLQETFDEIID 464
Cdd:smart00327 137 FVVGVGNDVDEEELKKLASAPGGVYVF-------LPELLDLLID 173
Trypsin pfam00089
Trypsin;
487-722 2.51e-21

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 93.28  E-value: 2.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 487 HPWIAeiRVQNEGSSQKCLGSLVTPKFVLTAAHCFRFGDLPKHV----TVDIDDGQGRVKRVQNFTLHPKYNVNAqkann 562
Cdd:pfam00089  12 FPWQV--SLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVlgahNIVLREGGEQKFDVEKIIVHPNYNPDT----- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 563 vdefYDYDVALIELVEYVQISTDVRPICIPCTQETSAAlkivrDTTCKQqeqlllnkQNEPLMFLTKSRGQMEKkdVNAK 642
Cdd:pfam00089  85 ----LDNDIALLKLESPVTLGDTVRPICLPDASSDLPV-----GTTCTV--------SGWGNTKTLGPSDTLQE--VTVP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 643 LGDnRKECISHAlkakgirtqnvSLVVTDNFLCTGGlfPQRDhiACTGDSGGAVFKNyehRTIQVALVSWGTKnlCQSGG 722
Cdd:pfam00089 146 VVS-RETCRSAY-----------GGTVTDTMICAGA--GGKD--ACQGDSGGPLVCS---DGELIGIVSWGYG--CASGN 204
VWA pfam00092
von Willebrand factor type A domain;
261-461 4.62e-19

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 85.40  E-value: 4.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 261 NIYIAVDVSESITKDDFISARNAVLKLITKIASFSVTPNYEIVFFAAEIFEIVNIIDFlDNKQELHRiktALETFTVGEK 340
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDY-SSKEELLS---AVDNLRYLGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 341 ELTGTDLNLVFrkMLEQiaVIKQRAGETfKDYHHVIIVFTDGaYNMGGSPAQTVAAIKQmvymnptggedtnkrdeyLDI 420
Cdd:pfam00092  77 GTTNTGKALKY--ALEN--LFSSAAGAR-PGAPKVVVLLTDG-RSQDGDPEEVARELKS------------------AGV 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1839487038 421 YIFGIG-GEIFDDDLNQLTVGTGGQHFFKLKDLVQLQETFDE 461
Cdd:pfam00092 133 TVFAVGvGNADDEELRKIASEPGEGHVFTVSDFEALEDLQDQ 174
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 97-152 4.99e-18

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: 78.27  E-value: 4.99e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1839487038  97 CPDPTVLLNGNVVPSQEKYFVNNVTTYECYSGYTLYGSSRRVCLPNGKWSGPTPIC 152
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 97-152 1.93e-17

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: 76.80  E-value: 1.93e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1839487038   97 CPDPTVLLNGNVVPSQEKYFVNNVTTYECYSGYTLYGSSRRVCLPNGKWSGPTPIC 152
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 53-213 1.56e-15

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 77.39  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  53 GSILIYHCPEEYYPYPDLVRVCQL--TGK--WNPtpkkfRPQRCRLVECPDPTVLLNGNVVPSQEKYFVNNVTTYECYSG 128
Cdd:PHA02927  105 GSSITYSCNSGYQLIGESKSYCELgsTGSmvWNP-----EAPICESVKCQSPPSISNGRHNGYEDFYTDGSVVTYSCNSG 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 129 YTLYGSSRRVClPNGKWSGPtPICSRGSgdhCADPGIPAGASRNG--NQFGIDDKVKYMCNSNLNLVGPSERVCQENGQW 206
Cdd:PHA02927  180 YSLIGNSGVLC-SGGEWSDP-PTCQIVK---CPHPTISNGYLSSGfkRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTW 254


                  ....*..
gi 1839487038 207 TGTEPAC 213
Cdd:PHA02927  255 QPELPKC 261
Sushi pfam00084
Sushi repeat (SCR repeat);
97-152 2.41e-15

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 70.61  E-value: 2.41e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1839487038  97 CPDPTVLLNGNVVPSQEKYFVNNVTTYECYSGYTLYGSSRRVCLPNGKWSGPTPIC 152
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 160-213 1.40e-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: 57.09  E-value: 1.40e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1839487038 160 CADPGIPAGASRNG--NQFGIDDKVKYMCNSNLNLVGPSERVCQENGQWTGTEPAC 213
Cdd:cd00033     1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
160-213 1.28e-09

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 54.43  E-value: 1.28e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1839487038 160 CADP-GIPAG---ASRNGNQFGidDKVKYMCNSNLNLVGPSERVCQENGQWTGTEPAC 213
Cdd:pfam00084   1 CPPPpDIPNGkvsATKNEYNYG--ASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 160-213 4.47e-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: 52.91  E-value: 4.47e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1839487038  160 CADPGIPAGASRNG--NQFGIDDKVKYMCNSNLNLVGPSERVCQENGQWTGTEPAC 213
Cdd:smart00032   1 CPPPPDIENGTVTSssGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 222-462 4.51e-09

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: 58.03  E-value: 4.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 222 PLEVAKAFGSSITETLTTLEPVDDTQEGRKIRLTKNGTLnIYIAVDVSESITKDD-FISARNAVLKLIT------KIAsf 294
Cdd:COG1240    56 LGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRD-VVLVVDASGSMAAENrLEAAKGALLDFLDdyrprdRVG-- 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 295 svtpnyeIVFFAAEIFEIVniiDFLDNKQelhRIKTALETFTVGEkeltGTDLNLVFRKMLEQIAvikqragETFKDYHH 374
Cdd:COG1240   133 -------LVAFGGEAEVLL---PLTRDRE---ALKRALDELPPGG----GTPLGDALALALELLK-------RADPARRK 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 375 VIIVFTDGAYNMGGSPAQTVAAIkqmvymnptggedtnKRDEYLDIYIFGIGGEIFDDD-LNQLTVGTGGQhFFKLKDLV 453
Cdd:COG1240   189 VIVLLTDGRDNAGRIDPLEAAEL---------------AAAAGIRIYTIGVGTEAVDEGlLREIAEATGGR-YFRADDLS 252


                  ....*....
gi 1839487038 454 QLQETFDEI 462
Cdd:COG1240   253 ELAAIYREI 261
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 53-154 5.20e-09

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 57.74  E-value: 5.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  53 GSILIYHCPEEYYPYPDLVRVCQlTGKWNPTPKkfrpqrCRLVECPDPTVLlNGNVVPS-QEKYFVNNVTTYECYSGYTL 131
Cdd:PHA02927  169 GSVVTYSCNSGYSLIGNSGVLCS-GGEWSDPPT------CQIVKCPHPTIS-NGYLSSGfKRSYSYNDNVDFKCKYGYKL 240

                          90       100
                  ....*....|....*....|...
gi 1839487038 132 YGSSRRVCLPNGKWSGPTPICSR 154
Cdd:PHA02927  241 SGSSSSTCSPGNTWQPELPKCVR 263
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 260-460 2.04e-79

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: 252.98  E-value: 2.04e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 260 LNIYIAVDVSESITKDDFISARNAVLKLITKIASFSVTPNYEIVFFAAEIFEIVNIIDFLDNKqeLHRIKTALETFTVGE 339
Cdd:cd01470     1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSND--ADDVIKRLEDFNYDD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 340 KEL-TGTDLNLVFRKMLEQIAVIKQRAGETFKDYHHVIIVFTDGAYNMGGSPAQTVAAIKQMVYMNPTggeDTNKRDEYL 418
Cdd:cd01470    79 HGDkTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNK---SDNPREDYL 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1839487038 419 DIYIFGIGGEIFDDDLNQLTVGTGG-QHFFKLKDLVQLQETFD 460
Cdd:cd01470   156 DVYVFGVGDDVNKEELNDLASKKDNeRHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 487-713 7.76e-36

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: 135.48  E-value: 7.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 487 HPWIAeiRVQNEGSSQKCLGSLVTPKFVLTAAHCFRfGDLPKHVTV-------DIDDGQGRVKRVQNFTLHPKYNVNaqk 559
Cdd:cd00190    12 FPWQV--SLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVrlgshdlSSNEGGGQVIKVKKVIVHPNYNPS--- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 560 annvdeFYDYDVALIELVEYVQISTDVRPICIPCTQETSAAlkivrDTTC------KQQEQLLLNKQneplmfltksrgq 633
Cdd:cd00190    86 ------TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPA-----GTTCtvsgwgRTSEGGPLPDV------------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 634 meKKDVNAKLGDNrKECISHALKAKGIrtqnvslvvTDNFLCTGGLFPQRDhiACTGDSGGAVFKNYEHRTIQVALVSWG 713
Cdd:cd00190   142 --LQEVNVPIVSN-AECKRAYSYGGTI---------TDNMLCAGGLEGGKD--ACQGDSGGPLVCNDNGRGVLVGIVSWG 207
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 487-722 6.60e-34

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: 129.72  E-value: 6.60e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  487 HPWIAeiRVQNEGSSQKCLGSLVTPKFVLTAAHCFRfGDLPKHVTV-----DIDDGQGRVKR-VQNFTLHPKYNvnaqka 560
Cdd:smart00020  13 FPWQV--SLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVrlgshDLSSGEEGQVIkVSKVIIHPNYN------ 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  561 nnvDEFYDYDVALIELVEYVQISTDVRPICIPCTQETSAAlkivrDTTCK----QQEQLLLNKQNEPLMfltksrgqmek 636
Cdd:smart00020  84 ---PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPA-----GTTCTvsgwGRTSEGAGSLPDTLQ----------- 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  637 kDVNAKLGDNrKECISHAlkakgirtqNVSLVVTDNFLCTGGLFPQRDhiACTGDSGGAVFKNYeHRTIQVALVSWGTKn 716
Cdd:smart00020 145 -EVNVPIVSN-ATCRRAY---------SGGGAITDNMLCAGGLEGGKD--ACQGDSGGPLVCND-GRWVLVGIVSWGSG- 209


                   ....*.
gi 1839487038  717 lCQSGG 722
Cdd:smart00020 210 -CARPG 214
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 260-447 1.92e-23

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 97.36  E-value: 1.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 260 LNIYIAVDVSESITKDDFISARNAVLKLITKIASFSVTPNYEIVFFAAEIFEIVNIIDFlDNKQELHRIKTALETFTVGe 339
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDY-KSKDDLLKAVKNLKYLGGG- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 340 keltGTDLNLVFRKMLEQIAVIKQRagetFKDYHHVIIVFTDGAYNMGGSPAQTVAAIkqmvymnptggedtnkRDEYLD 419
Cdd:cd01450    79 ----GTNTGKALQYALEQLFSESNA----RENVPKVIIVLTDGRSDDGGDPKEAAAKL----------------KDEGIK 134

                         170       180
                  ....*....|....*....|....*...
gi 1839487038 420 IYIFGIgGEIFDDDLNQLTVGTGGQHFF 447
Cdd:cd01450   135 VFVVGV-GPADEEELREIASCPSERHVF 161
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 487-722 7.21e-23

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 98.95  E-value: 7.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 487 HPWIAEIRVQNEGSSQKCLGSLVTPKFVLTAAHCFrFGDLPKHVTV-----DIDDGQGRVKRVQNFTLHPKYNVNAqkan 561
Cdd:COG5640    42 YPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCV-DGDGPSDLRVvigstDLSTSGGTVVKVARIVVHPDYDPAT---- 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 562 nvdefYDYDVALIELVEYVqisTDVRPICIPCTQETSAALKIVR--------DTTCKQQEQLllnkqneplmfltksrgq 633
Cdd:COG5640   117 -----PGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATvagwgrtsEGPGSQSGTL------------------ 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 634 mekKDVNAKLGDNRkECishalkakgirtQNVSLVVTDNFLCTGGLFPQRDhiACTGDSGGAVFKNYEHRTIQVALVSWG 713
Cdd:COG5640   171 ---RKADVPVVSDA-TC------------AAYGGFDGGTMLCAGYPEGGKD--ACQGDSGGPLVVKDGGGWVLVGVVSWG 232


                  ....*....
gi 1839487038 714 TkNLCQSGG 722
Cdd:COG5640   233 G-GPCAAGY 240
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 261-464 2.02e-22

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 94.83  E-value: 2.02e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  261 NIYIAVDVSESITKDDFISARNAVLKLITKIASFSVTPNYEIVFFAAEIFEIVNIIDFlDNKQELHRIKTALETFTVGek 340
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDS-RSKDALLEALASLSYKLGG-- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  341 eltGTDLNLVFRKMLEQIAVIKQRAGetfKDYHHVIIVFTDGAYNMGGSPAQTVAAikqmvymnptggedtNKRDEYLDI 420
Cdd:smart00327  78 ---GTNLGAALQYALENLFSKSAGSR---RGAPKVVILITDGESNDGPKDLLKAAK---------------ELKRSGVKV 136

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1839487038  421 YIFGIGGEIFDDDLNQLTVGTGGQHFFklkdlvqLQETFDEIID 464
Cdd:smart00327 137 FVVGVGNDVDEEELKKLASAPGGVYVF-------LPELLDLLID 173
Trypsin pfam00089
Trypsin;
487-722 2.51e-21

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 93.28  E-value: 2.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 487 HPWIAeiRVQNEGSSQKCLGSLVTPKFVLTAAHCFRFGDLPKHV----TVDIDDGQGRVKRVQNFTLHPKYNVNAqkann 562
Cdd:pfam00089  12 FPWQV--SLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVlgahNIVLREGGEQKFDVEKIIVHPNYNPDT----- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 563 vdefYDYDVALIELVEYVQISTDVRPICIPCTQETSAAlkivrDTTCKQqeqlllnkQNEPLMFLTKSRGQMEKkdVNAK 642
Cdd:pfam00089  85 ----LDNDIALLKLESPVTLGDTVRPICLPDASSDLPV-----GTTCTV--------SGWGNTKTLGPSDTLQE--VTVP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 643 LGDnRKECISHAlkakgirtqnvSLVVTDNFLCTGGlfPQRDhiACTGDSGGAVFKNyehRTIQVALVSWGTKnlCQSGG 722
Cdd:pfam00089 146 VVS-RETCRSAY-----------GGTVTDTMICAGA--GGKD--ACQGDSGGPLVCS---DGELIGIVSWGYG--CASGN 204
VWA pfam00092
von Willebrand factor type A domain;
261-461 4.62e-19

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 85.40  E-value: 4.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 261 NIYIAVDVSESITKDDFISARNAVLKLITKIASFSVTPNYEIVFFAAEIFEIVNIIDFlDNKQELHRiktALETFTVGEK 340
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDY-SSKEELLS---AVDNLRYLGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 341 ELTGTDLNLVFrkMLEQiaVIKQRAGETfKDYHHVIIVFTDGaYNMGGSPAQTVAAIKQmvymnptggedtnkrdeyLDI 420
Cdd:pfam00092  77 GTTNTGKALKY--ALEN--LFSSAAGAR-PGAPKVVVLLTDG-RSQDGDPEEVARELKS------------------AGV 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1839487038 421 YIFGIG-GEIFDDDLNQLTVGTGGQHFFKLKDLVQLQETFDE 461
Cdd:pfam00092 133 TVFAVGvGNADDEELRKIASEPGEGHVFTVSDFEALEDLQDQ 174
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 97-152 4.99e-18

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: 78.27  E-value: 4.99e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1839487038  97 CPDPTVLLNGNVVPSQEKYFVNNVTTYECYSGYTLYGSSRRVCLPNGKWSGPTPIC 152
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 260-447 8.19e-18

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 81.46  E-value: 8.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 260 LNIYIAVDVSESITKDDFISARNAVLKLITKIASFSVTPNYEIVFFAAEIFEIVNIIDFlDNKQELHRIKTALETFTVGe 339
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTD-TDKADLLEAIDALKKGLGG- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 340 keltGTDLNLVFRKMLEQIavikqrAGETFKDYHHVIIVFTDGAYNMGGSPAQtvAAIKQMvymnptggedtnkRDEYLD 419
Cdd:cd00198    79 ----GTNIGAALRLALELL------KSAKRPNARRVIILLTDGEPNDGPELLA--EAAREL-------------RKLGIT 133

                         170       180
                  ....*....|....*....|....*...
gi 1839487038 420 IYIFGIGGEIFDDDLNQLTVGTGGQHFF 447
Cdd:cd00198   134 VYTIGIGDDANEDELKEIADKTTGGAVF 161
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 97-152 1.93e-17

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: 76.80  E-value: 1.93e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1839487038   97 CPDPTVLLNGNVVPSQEKYFVNNVTTYECYSGYTLYGSSRRVCLPNGKWSGPTPIC 152
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 53-213 1.56e-15

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 77.39  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  53 GSILIYHCPEEYYPYPDLVRVCQL--TGK--WNPtpkkfRPQRCRLVECPDPTVLLNGNVVPSQEKYFVNNVTTYECYSG 128
Cdd:PHA02927  105 GSSITYSCNSGYQLIGESKSYCELgsTGSmvWNP-----EAPICESVKCQSPPSISNGRHNGYEDFYTDGSVVTYSCNSG 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 129 YTLYGSSRRVClPNGKWSGPtPICSRGSgdhCADPGIPAGASRNG--NQFGIDDKVKYMCNSNLNLVGPSERVCQENGQW 206
Cdd:PHA02927  180 YSLIGNSGVLC-SGGEWSDP-PTCQIVK---CPHPTISNGYLSSGfkRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTW 254


                  ....*..
gi 1839487038 207 TGTEPAC 213
Cdd:PHA02927  255 QPELPKC 261
Sushi pfam00084
Sushi repeat (SCR repeat);
97-152 2.41e-15

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 70.61  E-value: 2.41e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1839487038  97 CPDPTVLLNGNVVPSQEKYFVNNVTTYECYSGYTLYGSSRRVCLPNGKWSGPTPIC 152
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02639 PHA02639
EEV host range protein; Provisional
 28-245 5.11e-13

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 70.46  E-value: 5.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  28 VWCDCPDEllgIEGGDYT-LTKTMEPGSILIYHCPEEYYPYPDLVRVCqLTGKWNPTPKKFRPqRCRLVECPDPTVLLNG 106
Cdd:PHA02639   20 IYCDKPDD---ISNGFITeLMEKYEIGKLIEYTCNTDYALIGDRFRTC-IKDKNNAIWSNKAP-FCMLKECNDPPSIING 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 107 NVVPSQEKYFVNNVTTYEC--YSG--YTLYGSSRRVCLPNGKWSGPTPICSRgsgDHCADPGIPAG---ASRNGNQFGID 179
Cdd:PHA02639   95 KIYNKREMYKVGDEIYYVCneHKGvqYSLVGNEKITCIQDKSWKPDPPICKM---INCRFPALQNGyinGIPSNKKFYYK 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1839487038 180 DKVKYMCNSNLNLVGPSERVCQENGQWTGTEPACYYKHTFDtplevakafgssiteTLTTLEPVDD 245
Cdd:PHA02639  172 TRVGFSCKSGFDLVGEKYSTCNINATWFPSIPTCVRNKPID---------------DIIYLKPVDD 222
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 160-213 1.40e-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: 57.09  E-value: 1.40e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1839487038 160 CADPGIPAGASRNG--NQFGIDDKVKYMCNSNLNLVGPSERVCQENGQWTGTEPAC 213
Cdd:cd00033     1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
160-213 1.28e-09

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 54.43  E-value: 1.28e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1839487038 160 CADP-GIPAG---ASRNGNQFGidDKVKYMCNSNLNLVGPSERVCQENGQWTGTEPAC 213
Cdd:pfam00084   1 CPPPpDIPNGkvsATKNEYNYG--ASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 160-213 4.47e-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: 52.91  E-value: 4.47e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1839487038  160 CADPGIPAGASRNG--NQFGIDDKVKYMCNSNLNLVGPSERVCQENGQWTGTEPAC 213
Cdd:smart00032   1 CPPPPDIENGTVTSssGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 222-462 4.51e-09

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: 58.03  E-value: 4.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 222 PLEVAKAFGSSITETLTTLEPVDDTQEGRKIRLTKNGTLnIYIAVDVSESITKDD-FISARNAVLKLIT------KIAsf 294
Cdd:COG1240    56 LGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRD-VVLVVDASGSMAAENrLEAAKGALLDFLDdyrprdRVG-- 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 295 svtpnyeIVFFAAEIFEIVniiDFLDNKQelhRIKTALETFTVGEkeltGTDLNLVFRKMLEQIAvikqragETFKDYHH 374
Cdd:COG1240   133 -------LVAFGGEAEVLL---PLTRDRE---ALKRALDELPPGG----GTPLGDALALALELLK-------RADPARRK 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 375 VIIVFTDGAYNMGGSPAQTVAAIkqmvymnptggedtnKRDEYLDIYIFGIGGEIFDDD-LNQLTVGTGGQhFFKLKDLV 453
Cdd:COG1240   189 VIVLLTDGRDNAGRIDPLEAAEL---------------AAAAGIRIYTIGVGTEAVDEGlLREIAEATGGR-YFRADDLS 252


                  ....*....
gi 1839487038 454 QLQETFDEI 462
Cdd:COG1240   253 ELAAIYREI 261
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 53-154 5.20e-09

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 57.74  E-value: 5.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  53 GSILIYHCPEEYYPYPDLVRVCQlTGKWNPTPKkfrpqrCRLVECPDPTVLlNGNVVPS-QEKYFVNNVTTYECYSGYTL 131
Cdd:PHA02927  169 GSVVTYSCNSGYSLIGNSGVLCS-GGEWSDPPT------CQIVKCPHPTIS-NGYLSSGfKRSYSYNDNVDFKCKYGYKL 240

                          90       100
                  ....*....|....*....|...
gi 1839487038 132 YGSSRRVCLPNGKWSGPTPICSR 154
Cdd:PHA02927  241 SGSSSSTCSPGNTWQPELPKCVR 263
PHA02817 PHA02817
EEV Host range protein; Provisional
 20-154 6.90e-09

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 56.87  E-value: 6.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  20 VLLFMGAEVWCDCPDELLGI-----EGGDYTLTKTMEPGSILIYHCPEE-----YYPYPDLVRVCQLTGKWNPTPKkfrp 89
Cdd:PHA02817    7 LLILLCNKVYSLCDLNKCCYppsikNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFP---- 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1839487038  90 qRCRLVECPDPTvLLNG--NVVPSQEKYFVNNVTTYECYSGYTLYGSSRRVCLPNGKWSGPTPICSR 154
Cdd:PHA02817   83 -VCKIIRCRFPA-LQNGfvNGIPDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPICSR 147
PHA02831 PHA02831
EEV host range protein; Provisional
 97-213 8.75e-08

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 54.23  E-value: 8.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  97 CPDPTVLLNGNVVPSQEKYFVNNVTTYEC----YSGYTLYGSSRRVCLpNGKWSGPTPICSRgsgDHCADPGIPAGASRN 172
Cdd:PHA02831   78 CKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYSIVGNETVKCI-NKQWVPKYPVCKL---IRCKYPALQNGFLNV 153

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1839487038 173 -GNQFGIDDKVKYMCNSNLNLVGPSERVCQENGQWTGTEPAC 213
Cdd:PHA02831  154 fEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSIWYPGIPKC 195
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 494-576 2.60e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 48.52  E-value: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 494 RVQNEGSSQKCLGSLVTPKFVLTAAHCF---RFGDLPKHVTV--DIDDGQGRVKRVQNFTLHPKYNVNAQkannvdefYD 568
Cdd:COG3591     4 RLETDGGGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFvpGYNGGPYGTATATRFRVPPGWVASGD--------AG 75


                  ....*...
gi 1839487038 569 YDVALIEL 576
Cdd:COG3591    76 YDYALLRL 83
PHA02817 PHA02817
EEV Host range protein; Provisional
 92-213 1.12e-05

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 47.24  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  92 CRLVECPDPTVLLNGNVVPSQEKYFVNNVTTYECYSG-----YTLYGSSRRVCLPNGKWSGPTPICSRgsgDHCADPGIP 166
Cdd:PHA02817   19 CDLNKCCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKI---IRCRFPALQ 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1839487038 167 AGASrNG----NQFGIDDKVKYMCNSNLNLVGPSERVCQENGQWTGTEPAC 213
Cdd:PHA02817   96 NGFV-NGipdsKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPIC 145
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 95-224 2.87e-04

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 43.54  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  95 VECPD----PTVLLNGNVVPSQEKYFVNNVTTYECYSGYTLYGSSRRVCLPNgKWSgPTPICSRgsgdHCADPGIPAGAS 170
Cdd:PHA02954  123 VTCPNaecqPLQLEHGSCQPVKEKYSFGEHITINCDVGYEVIGASYISCTAN-SWN-VIPSCQQ----KCDIPSLSNGLI 196

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1839487038 171 rNGNQFGIDDKVKYMCNSNLNLVGPSERVCQEnGQWTGTEPACYYKHTFDTPLE 224
Cdd:PHA02954  197 -SGSTFSIGGVIHLSCKSGFTLTGSPSSTCID-GKWNPVLPICVRSNEEFDPVD 248
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 260-441 4.35e-04

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


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 41.94  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 260 LNIYIAVDVSESITKDDfISARNAVLKLItkIASFSVTPnyeivfFAAEIFEIvNIIDFlDNKQELHRIKTALETFTVge 339
Cdd:cd01464     4 LPIYLLLDTSGSMAGEP-IEALNQGLQML--QSELRQDP------YALESVEI-SVITF-DSAARVIVPLTPLESFQP-- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038 340 KELT---GTDLNLVFRKMLEQIAVIKQR-AGETFKDYHHVIIVFTDGAYNmgGSPAQTVAAIKQMvymnptggedtnkRD 415
Cdd:cd01464    71 PRLTasgGTSMGAALELALDCIDRRVQRyRADQKGDWRPWVFLLTDGEPT--DDLTAAIERIKEA-------------RD 135

                         170       180
                  ....*....|....*....|....*.
gi 1839487038 416 EYLDIYIFGIGGEIFDDDLNQLTVGT 441
Cdd:cd01464   136 SKGRIVACAVGPKADLDTLKQITEGV 161
Sushi pfam00084
Sushi repeat (SCR repeat);
30-84 5.27e-04

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 38.63  E-value: 5.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1839487038  30 CDCPDELLgiEGGDYTLTKTMEPGSILIYHCPEEYYPYPDLVRVCQLTGKWNPTP 84
Cdd:pfam00084   1 CPPPPDIP--NGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPF 53
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 32-84 1.10e-03

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: 37.89  E-value: 1.10e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1839487038   32 CPDeLLGIEGGDYTLTK-TMEPGSILIYHCPEEYYPYPDLVRVCQLTGKWNPTP 84
Cdd:smart00032   1 CPP-PPDIENGTVTSSSgTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPP 53
PHA02831 PHA02831
EEV host range protein; Provisional
 76-156 1.43e-03

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 41.13  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839487038  76 LTGKWNPtpkkfRPQRCRLVECPDPTvLLNGNVVPSQEKYFVNNVTTYECYSGYTLYGSSRRVCLPNGKWSGPTPICSRG 155
Cdd:PHA02831  125 INKQWVP-----KYPVCKLIRCKYPA-LQNGFLNVFEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSIWYPGIPKCVKD 198


                  .
gi 1839487038 156 S 156
Cdd:PHA02831  199 K 199
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 32-84 2.98e-03

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: 36.67  E-value: 2.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1839487038  32 CPdELLGIEGGDYTLTK-TMEPGSILIYHCPEEYYPYPDLVRVCQLTGKWNPTP 84
Cdd:cd00033     1 CP-PPPVPENGTVTGSKgSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPP 53
 
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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