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Conserved domains on  [gi|1622934744|ref|XP_014991515|]
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complement factor B [Macaca mulatta]

Protein Classification

serine protease( domain architecture ID 13332040)

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
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 269-465 5.21e-110

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: 332.72  E-value: 5.21e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 269 MNIYLVLDGSDSIGAGNFTGAKKCLVNLIEKVASYGVKPRYALVTYATYPRIWVKVSDQESSNADWVTKKLSEINYEDHK 348
Cdd:cd01470     1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 349 LKSGTNTKRALQAVYSMMSWPEDIPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVF 428
Cdd:cd01470    81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622934744 429 GVGPLVDQVNINALASKKDNEQHVFKVKDMENLEDVF 465
Cdd:cd01470   161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVF 197
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 488-754 3.34e-47

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: 167.45  E-value: 3.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 488 TDYHKQPWQAKISVTRpskGHESCMGAVVSEYFVLTAAHCFTVDDK--------EHSIKVSVGKKRDLEIEKVLFHPDYN 559
Cdd:cd00190     7 AKIGSFPWQVSLQYTG---GRHFCGGSLISPRWVLTAAHCVYSSAPsnytvrlgSHDLSSNEGGGQVIKVKKVIVHPNYN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 560 isgkkeagiPEFYDYDVALIKLKNKLNYDPTIRPICLPCTEGTtralrLPPTTTCQqqkeellpaqdikalfVS-----E 634
Cdd:cd00190    84 ---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCT----------------VSgwgrtS 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 635 EEKKLTR--KEVYIKNGDKKgSCERDAQYAPgydkvkdiseVVTPRFLCTGGvsPYADPNTCRGDSGGPLIVHKRSRFIQ 712
Cdd:cd00190   134 EGGPLPDvlQEVNVPIVSNA-ECKRAYSYGG----------TITDNMLCAGG--LEGGKDACQGDSGGPLVCNDNGRGVL 200

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1622934744 713 VGVISWGVvdVCknqkRQKQVPAhardFHVNLFQVLPWLKEK 754
Cdd:cd00190   201 VGIVSWGS--GC----ARPNYPG----VYTRVSSYLDWIQKT 232
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 103-158 1.11e-15

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: 71.73  E-value: 1.11e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622934744 103 CPRPQDFENGEYRPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 158
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
 55-218 1.46e-13

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 71.61  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  55 GQALEYVCPSGFYPYPVQTRTCR--STGS--WSTlqtqdrktvKKAECRAIRCPRPQDFENGEYRPRSPYYNVSDEISFH 130
Cdd:PHA02927  105 GSSITYSCNSGYQLIGESKSYCElgSTGSmvWNP---------EAPICESVKCQSPPSISNGRHNGYEDFYTDGSVVTYS 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 131 CYDGYTLRGSANRTCQvNGRWSgQTAICDngAGYCSNPGIPIGTRKVGSR--YRLEDSVTYHCSRGLTLRGSQRRTCQEG 208
Cdd:PHA02927  176 CNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGFKrsYSYNDNVDFKCKYGYKLSGSSSSTCSPG 251

                         170
                  ....*....|
gi 1622934744 209 GSWSGTEPSC 218
Cdd:PHA02927  252 NTWQPELPKC 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 ...
 269-465 5.21e-110

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: 332.72  E-value: 5.21e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 269 MNIYLVLDGSDSIGAGNFTGAKKCLVNLIEKVASYGVKPRYALVTYATYPRIWVKVSDQESSNADWVTKKLSEINYEDHK 348
Cdd:cd01470     1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 349 LKSGTNTKRALQAVYSMMSWPEDIPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVF 428
Cdd:cd01470    81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622934744 429 GVGPLVDQVNINALASKKDNEQHVFKVKDMENLEDVF 465
Cdd:cd01470   161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVF 197
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 488-754 3.34e-47

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: 167.45  E-value: 3.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 488 TDYHKQPWQAKISVTRpskGHESCMGAVVSEYFVLTAAHCFTVDDK--------EHSIKVSVGKKRDLEIEKVLFHPDYN 559
Cdd:cd00190     7 AKIGSFPWQVSLQYTG---GRHFCGGSLISPRWVLTAAHCVYSSAPsnytvrlgSHDLSSNEGGGQVIKVKKVIVHPNYN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 560 isgkkeagiPEFYDYDVALIKLKNKLNYDPTIRPICLPCTEGTtralrLPPTTTCQqqkeellpaqdikalfVS-----E 634
Cdd:cd00190    84 ---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCT----------------VSgwgrtS 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 635 EEKKLTR--KEVYIKNGDKKgSCERDAQYAPgydkvkdiseVVTPRFLCTGGvsPYADPNTCRGDSGGPLIVHKRSRFIQ 712
Cdd:cd00190   134 EGGPLPDvlQEVNVPIVSNA-ECKRAYSYGG----------TITDNMLCAGG--LEGGKDACQGDSGGPLVCNDNGRGVL 200

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1622934744 713 VGVISWGVvdVCknqkRQKQVPAhardFHVNLFQVLPWLKEK 754
Cdd:cd00190   201 VGIVSWGS--GC----ARPNYPG----VYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 488-750 1.64e-43

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: 157.07  E-value: 1.64e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  488 TDYHKQPWQAKISVTRpskGHESCMGAVVSEYFVLTAAHCFTvDDKEHSIKVSVG--------KKRDLEIEKVLFHPDYN 559
Cdd:smart00020   8 ANIGSFPWQVSLQYGG---GRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGshdlssgeEGQVIKVSKVIIHPNYN 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  560 isgkkeagiPEFYDYDVALIKLKNKLNYDPTIRPICLPCTegttrALRLPPTTTCQqqkeellpaqdikalfVS------ 633
Cdd:smart00020  84 ---------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCT----------------VSgwgrts 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  634 EEEKKLTR--KEVYIKNGDKKgSCERDAQYapgydkvkdiSEVVTPRFLCTGGvsPYADPNTCRGDSGGPLiVHKRSRFI 711
Cdd:smart00020 134 EGAGSLPDtlQEVNVPIVSNA-TCRRAYSG----------GGAITDNMLCAGG--LEGGKDACQGDSGGPL-VCNDGRWV 199

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1622934744  712 QVGVISWGVvdVCKNqkrqkqvpAHARDFHVNLFQVLPW 750
Cdd:smart00020 200 LVGIVSWGS--GCAR--------PGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
491-751 1.56e-36

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 136.80  E-value: 1.56e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 491 HKQPWQAKISVTRpskGHESCMGAVVSEYFVLTAAHCF------TVDDKEHSIKVSVGKKRDLEIEKVLFHPDYNisgkk 564
Cdd:pfam00089  10 GSFPWQVSLQLSS---GKHFCGGSLISENWVLTAAHCVsgasdvKVVLGAHNIVLREGGEQKFDVEKIIVHPNYN----- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 565 eagiPEFYDYDVALIKLKNKLNYDPTIRPICLPCTEGTtralrLPPTTTCQQQKEELlpaqdikalfVSEEEKKLTRKEV 644
Cdd:pfam00089  82 ----PDTLDNDIALLKLESPVTLGDTVRPICLPDASSD-----LPVGTTCTVSGWGN----------TKTLGPSDTLQEV 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 645 YIKNGDkKGSCERdaqyapgydkvkDISEVVTPRFLCTGGVSPYAdpntCRGDSGGPLIVHKRsrfIQVGVISWGvvDVC 724
Cdd:pfam00089 143 TVPVVS-RETCRS------------AYGGTVTDTMICAGAGGKDA----CQGDSGGPLVCSDG---ELIGIVSWG--YGC 200

                         250       260
                  ....*....|....*....|....*..
gi 1622934744 725 KNQKRqkqvpahaRDFHVNLFQVLPWL 751
Cdd:pfam00089 201 ASGNY--------PGVYTPVSSYLDWI 219
VWA pfam00092
von Willebrand factor type A domain;
270-465 4.25e-31

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 119.69  E-value: 4.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 270 NIYLVLDGSDSIGAGNFTGAKKCLVNLIEKVASYGVKPRYALVTYATYPRIWVKVSDqeSSNADWVTKKLSEINYEDHKL 349
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLND--YSSKEELLSAVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 350 KS-GTNTKRALQAVYSMMSWPEDippegwnRTRHVIILMTDGlHNMGGDPITVIDEIRDllyigkdrknpreDYLDVYVF 428
Cdd:pfam00092  79 TNtGKALKYALENLFSSAAGARP-------GAPKVVVLLTDG-RSQDGDPEEVARELKS-------------AGVTVFAV 137

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622934744 429 GVGPLVDQvNINALASKKDnEQHVFKVKDMENLEDVF 465
Cdd:pfam00092 138 GVGNADDE-ELRKIASEPG-EGHVFTVSDFEALEDLQ 172
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 270-463 4.29e-27

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 108.31  E-value: 4.29e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  270 NIYLVLDGSDSIGAGNFTGAKKCLVNLIEKVASYGVKPRYALVTYATYPRIWVKVSDqeSSNADWVTKKLSEINYedhKL 349
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLND--SRSKDALLEALASLSY---KL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  350 KSGTNTKRALQAVYSMMSWPEdippEGWNR-TRHVIILMTDGLHNMGGDPItvIDEIRDLlyigkdrknpREDYLDVYVF 428
Cdd:smart00327  76 GGGTNLGAALQYALENLFSKS----AGSRRgAPKVVILITDGESNDGPKDL--LKAAKEL----------KRSGVKVFVV 139

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622934744  429 GVGPLVDQVNINALASKKDNEqHVFKVKDMENLED 463
Cdd:smart00327 140 GVGNDVDEEELKKLASAPGGV-YVFLPELLDLLID 173
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 494-719 7.95e-21

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 92.79  E-value: 7.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 494 PWQAKISVTRPSKGHeSCMGAVVSEYFVLTAAHCfTVDDKEHSIKVSVG-------KKRDLEIEKVLFHPDYNisgkkea 566
Cdd:COG5640    43 PWMVALQSSNGPSGQ-FCGGTLIAPRWVLTAAHC-VDGDGPSDLRVVIGstdlstsGGTVVKVARIVVHPDYD------- 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 567 giPEFYDYDVALIKLKNKLnydPTIRPICLPctegtTRALRLPPTT---------TCQQQKEellpaqdikalfVSEEEK 637
Cdd:COG5640   114 --PATPGNDIALLKLATPV---PGVAPAPLA-----TSADAAAPGTpatvagwgrTSEGPGS------------QSGTLR 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 638 KLTrkeVYIKNGDkkgSCERDAQYAPGYDkvkdisevvtprfLCTGGVSPYADpnTCRGDSGGPLIVHKRSRFIQVGVIS 717
Cdd:COG5640   172 KAD---VPVVSDA---TCAAYGGFDGGTM-------------LCAGYPEGGKD--ACQGDSGGPLVVKDGGGWVLVGVVS 230


                  ..
gi 1622934744 718 WG 719
Cdd:COG5640   231 WG 232
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 103-158 1.11e-15

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: 71.73  E-value: 1.11e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622934744 103 CPRPQDFENGEYRPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 158
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 103-158 4.04e-15

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: 70.25  E-value: 4.04e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622934744  103 CPRPQDFENGEYRPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 158
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 55-218 1.46e-13

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 71.61  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  55 GQALEYVCPSGFYPYPVQTRTCR--STGS--WSTlqtqdrktvKKAECRAIRCPRPQDFENGEYRPRSPYYNVSDEISFH 130
Cdd:PHA02927  105 GSSITYSCNSGYQLIGESKSYCElgSTGSmvWNP---------EAPICESVKCQSPPSISNGRHNGYEDFYTDGSVVTYS 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 131 CYDGYTLRGSANRTCQvNGRWSgQTAICDngAGYCSNPGIPIGTRKVGSR--YRLEDSVTYHCSRGLTLRGSQRRTCQEG 208
Cdd:PHA02927  176 CNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGFKrsYSYNDNVDFKCKYGYKLSGSSSSTCSPG 251

                         170
                  ....*....|
gi 1622934744 209 GSWSGTEPSC 218
Cdd:PHA02927  252 NTWQPELPKC 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 165-219 1.92e-12

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: 62.48  E-value: 1.92e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622934744 165 CSNPGIPIGTRKVGS--RYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQ 219
Cdd:cd00033     1 CPPPPVPENGTVTGSkgSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
Sushi pfam00084
Sushi repeat (SCR repeat);
103-158 1.08e-11

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 60.21  E-value: 1.08e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622934744 103 CPRPQDFENGEYRPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 158
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 165-218 2.27e-11

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: 59.46  E-value: 2.27e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622934744  165 CSNPG-IPIGTRKVGS-RYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 218
Cdd:smart00032   1 CPPPPdIENGTVTSSSgTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 225-465 1.52e-08

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: 56.49  E-value: 1.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 225 DTPQEVAEAFLSSLTETIEGVDAEDGHSPGEQQKRRIILDPSGSMNIYLVLDGSDSIGAGN-FTGAKKCLVNLIEkvaSY 303
Cdd:COG1240    49 LLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLD---DY 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 304 GVKPRYALVTYATYPRIWVKVSdqesSNADWVTKKLSEInyedhKLKSGTNTKRALQAVYSMMswpEDIPPEGwnrtRHV 383
Cdd:COG1240   126 RPRDRVGLVAFGGEAEVLLPLT----RDREALKRALDEL-----PPGGGTPLGDALALALELL---KRADPAR----RKV 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 384 IILMTDGLHNMG-GDPITVIDEIrdllyigkdrknpREDYLDVYVFGVG-PLVDQVNINALAskkdnEQ---HVFKVKDM 458
Cdd:COG1240   190 IVLLTDGRDNAGrIDPLEAAELA-------------AAAGIRIYTIGVGtEAVDEGLLREIA-----EAtggRYFRADDL 251


                  ....*..
gi 1622934744 459 ENLEDVF 465
Cdd:COG1240   252 SELAAIY 258
Sushi pfam00084
Sushi repeat (SCR repeat);
180-218 1.10e-07

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.03  E-value: 1.10e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622934744 180 RYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 218
Cdd:pfam00084  18 EYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02817 PHA02817
EEV Host range protein; Provisional
 75-158 1.67e-03

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 40.69  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  75 TCRSTGSWSTlqtqdrktvKKAECRAIRCPRP---QDFENGEYRPRSPYYnvSDEISFHCYDGYTLRGSANRTCQVNGRW 151
Cdd:PHA02817   70 ICEKDGKWNK---------EFPVCKIIRCRFPalqNGFVNGIPDSKKFYY--ESEVSFSCKPGFVLIGTKYSVCGINSSW 138


                  ....*..
gi 1622934744 152 SGQTAIC 158
Cdd:PHA02817  139 IPKVPIC 145
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 269-465 5.21e-110

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: 332.72  E-value: 5.21e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 269 MNIYLVLDGSDSIGAGNFTGAKKCLVNLIEKVASYGVKPRYALVTYATYPRIWVKVSDQESSNADWVTKKLSEINYEDHK 348
Cdd:cd01470     1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 349 LKSGTNTKRALQAVYSMMSWPEDIPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVF 428
Cdd:cd01470    81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622934744 429 GVGPLVDQVNINALASKKDNEQHVFKVKDMENLEDVF 465
Cdd:cd01470   161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVF 197
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 488-754 3.34e-47

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: 167.45  E-value: 3.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 488 TDYHKQPWQAKISVTRpskGHESCMGAVVSEYFVLTAAHCFTVDDK--------EHSIKVSVGKKRDLEIEKVLFHPDYN 559
Cdd:cd00190     7 AKIGSFPWQVSLQYTG---GRHFCGGSLISPRWVLTAAHCVYSSAPsnytvrlgSHDLSSNEGGGQVIKVKKVIVHPNYN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 560 isgkkeagiPEFYDYDVALIKLKNKLNYDPTIRPICLPCTEGTtralrLPPTTTCQqqkeellpaqdikalfVS-----E 634
Cdd:cd00190    84 ---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCT----------------VSgwgrtS 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 635 EEKKLTR--KEVYIKNGDKKgSCERDAQYAPgydkvkdiseVVTPRFLCTGGvsPYADPNTCRGDSGGPLIVHKRSRFIQ 712
Cdd:cd00190   134 EGGPLPDvlQEVNVPIVSNA-ECKRAYSYGG----------TITDNMLCAGG--LEGGKDACQGDSGGPLVCNDNGRGVL 200

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1622934744 713 VGVISWGVvdVCknqkRQKQVPAhardFHVNLFQVLPWLKEK 754
Cdd:cd00190   201 VGIVSWGS--GC----ARPNYPG----VYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 488-750 1.64e-43

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: 157.07  E-value: 1.64e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  488 TDYHKQPWQAKISVTRpskGHESCMGAVVSEYFVLTAAHCFTvDDKEHSIKVSVG--------KKRDLEIEKVLFHPDYN 559
Cdd:smart00020   8 ANIGSFPWQVSLQYGG---GRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGshdlssgeEGQVIKVSKVIIHPNYN 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  560 isgkkeagiPEFYDYDVALIKLKNKLNYDPTIRPICLPCTegttrALRLPPTTTCQqqkeellpaqdikalfVS------ 633
Cdd:smart00020  84 ---------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCT----------------VSgwgrts 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  634 EEEKKLTR--KEVYIKNGDKKgSCERDAQYapgydkvkdiSEVVTPRFLCTGGvsPYADPNTCRGDSGGPLiVHKRSRFI 711
Cdd:smart00020 134 EGAGSLPDtlQEVNVPIVSNA-TCRRAYSG----------GGAITDNMLCAGG--LEGGKDACQGDSGGPL-VCNDGRWV 199

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1622934744  712 QVGVISWGVvdVCKNqkrqkqvpAHARDFHVNLFQVLPW 750
Cdd:smart00020 200 LVGIVSWGS--GCAR--------PGKPGVYTRVSSYLDW 228
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 269-453 4.09e-38

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: 139.35  E-value: 4.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 269 MNIYLVLDGSDSIGAGNFTGAKKCLVNLIEKVASYGVKPRYALVTYATYPRIWVKVSDqeSSNADWVTKKLSEINYEDHk 348
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLND--YKSKDDLLKAVKNLKYLGG- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 349 lkSGTNTKRALQAVYSMMSWPEDIppegWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLlyigkdrknpredYLDVYVF 428
Cdd:cd01450    78 --GGTNTGKALQYALEQLFSESNA----RENVPKVIIVLTDGRSDDGGDPKEAAAKLKDE-------------GIKVFVV 138

                         170       180
                  ....*....|....*....|....*
gi 1622934744 429 GVGPlVDQVNINALASKKdNEQHVF 453
Cdd:cd01450   139 GVGP-ADEEELREIASCP-SERHVF 161
Trypsin pfam00089
Trypsin;
491-751 1.56e-36

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 136.80  E-value: 1.56e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 491 HKQPWQAKISVTRpskGHESCMGAVVSEYFVLTAAHCF------TVDDKEHSIKVSVGKKRDLEIEKVLFHPDYNisgkk 564
Cdd:pfam00089  10 GSFPWQVSLQLSS---GKHFCGGSLISENWVLTAAHCVsgasdvKVVLGAHNIVLREGGEQKFDVEKIIVHPNYN----- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 565 eagiPEFYDYDVALIKLKNKLNYDPTIRPICLPCTEGTtralrLPPTTTCQQQKEELlpaqdikalfVSEEEKKLTRKEV 644
Cdd:pfam00089  82 ----PDTLDNDIALLKLESPVTLGDTVRPICLPDASSD-----LPVGTTCTVSGWGN----------TKTLGPSDTLQEV 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 645 YIKNGDkKGSCERdaqyapgydkvkDISEVVTPRFLCTGGVSPYAdpntCRGDSGGPLIVHKRsrfIQVGVISWGvvDVC 724
Cdd:pfam00089 143 TVPVVS-RETCRS------------AYGGTVTDTMICAGAGGKDA----CQGDSGGPLVCSDG---ELIGIVSWG--YGC 200

                         250       260
                  ....*....|....*....|....*..
gi 1622934744 725 KNQKRqkqvpahaRDFHVNLFQVLPWL 751
Cdd:pfam00089 201 ASGNY--------PGVYTPVSSYLDWI 219
VWA pfam00092
von Willebrand factor type A domain;
270-465 4.25e-31

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 119.69  E-value: 4.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 270 NIYLVLDGSDSIGAGNFTGAKKCLVNLIEKVASYGVKPRYALVTYATYPRIWVKVSDqeSSNADWVTKKLSEINYEDHKL 349
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLND--YSSKEELLSAVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 350 KS-GTNTKRALQAVYSMMSWPEDippegwnRTRHVIILMTDGlHNMGGDPITVIDEIRDllyigkdrknpreDYLDVYVF 428
Cdd:pfam00092  79 TNtGKALKYALENLFSSAAGARP-------GAPKVVVLLTDG-RSQDGDPEEVARELKS-------------AGVTVFAV 137

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622934744 429 GVGPLVDQvNINALASKKDnEQHVFKVKDMENLEDVF 465
Cdd:pfam00092 138 GVGNADDE-ELRKIASEPG-EGHVFTVSDFEALEDLQ 172
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 270-463 4.29e-27

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 108.31  E-value: 4.29e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  270 NIYLVLDGSDSIGAGNFTGAKKCLVNLIEKVASYGVKPRYALVTYATYPRIWVKVSDqeSSNADWVTKKLSEINYedhKL 349
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLND--SRSKDALLEALASLSY---KL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  350 KSGTNTKRALQAVYSMMSWPEdippEGWNR-TRHVIILMTDGLHNMGGDPItvIDEIRDLlyigkdrknpREDYLDVYVF 428
Cdd:smart00327  76 GGGTNLGAALQYALENLFSKS----AGSRRgAPKVVILITDGESNDGPKDL--LKAAKEL----------KRSGVKVFVV 139

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622934744  429 GVGPLVDQVNINALASKKDNEqHVFKVKDMENLED 463
Cdd:smart00327 140 GVGNDVDEEELKKLASAPGGV-YVFLPELLDLLID 173
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 270-453 3.23e-22

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: 93.78  E-value: 3.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 270 NIYLVLDGSDSIGAGNFTGAKKCLVNLIEKVASYGVKPRYALVTYATYPRIWVKVSDqeSSNADWVTKKLSEINYedhKL 349
Cdd:cd00198     2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTT--DTDKADLLEAIDALKK---GL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 350 KSGTNTKRALQAVYSMMSWPEDippegwNRTRHVIILMTDGLHNmgGDPITVIDEIRDLlyigkdrknpREDYLDVYVFG 429
Cdd:cd00198    77 GGGTNIGAALRLALELLKSAKR------PNARRVIILLTDGEPN--DGPELLAEAAREL----------RKLGITVYTIG 138

                         170       180
                  ....*....|....*....|....
gi 1622934744 430 VGPLVDQVNINALASkKDNEQHVF 453
Cdd:cd00198   139 IGDDANEDELKEIAD-KTTGGAVF 161
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 494-719 7.95e-21

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 92.79  E-value: 7.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 494 PWQAKISVTRPSKGHeSCMGAVVSEYFVLTAAHCfTVDDKEHSIKVSVG-------KKRDLEIEKVLFHPDYNisgkkea 566
Cdd:COG5640    43 PWMVALQSSNGPSGQ-FCGGTLIAPRWVLTAAHC-VDGDGPSDLRVVIGstdlstsGGTVVKVARIVVHPDYD------- 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 567 giPEFYDYDVALIKLKNKLnydPTIRPICLPctegtTRALRLPPTT---------TCQQQKEellpaqdikalfVSEEEK 637
Cdd:COG5640   114 --PATPGNDIALLKLATPV---PGVAPAPLA-----TSADAAAPGTpatvagwgrTSEGPGS------------QSGTLR 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 638 KLTrkeVYIKNGDkkgSCERDAQYAPGYDkvkdisevvtprfLCTGGVSPYADpnTCRGDSGGPLIVHKRSRFIQVGVIS 717
Cdd:COG5640   172 KAD---VPVVSDA---TCAAYGGFDGGTM-------------LCAGYPEGGKD--ACQGDSGGPLVVKDGGGWVLVGVVS 230


                  ..
gi 1622934744 718 WG 719
Cdd:COG5640   231 WG 232
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 103-158 1.11e-15

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: 71.73  E-value: 1.11e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622934744 103 CPRPQDFENGEYRPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 158
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 103-158 4.04e-15

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: 70.25  E-value: 4.04e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622934744  103 CPRPQDFENGEYRPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 158
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 55-218 1.46e-13

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 71.61  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  55 GQALEYVCPSGFYPYPVQTRTCR--STGS--WSTlqtqdrktvKKAECRAIRCPRPQDFENGEYRPRSPYYNVSDEISFH 130
Cdd:PHA02927  105 GSSITYSCNSGYQLIGESKSYCElgSTGSmvWNP---------EAPICESVKCQSPPSISNGRHNGYEDFYTDGSVVTYS 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 131 CYDGYTLRGSANRTCQvNGRWSgQTAICDngAGYCSNPGIPIGTRKVGSR--YRLEDSVTYHCSRGLTLRGSQRRTCQEG 208
Cdd:PHA02927  176 CNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGFKrsYSYNDNVDFKCKYGYKLSGSSSSTCSPG 251

                         170
                  ....*....|
gi 1622934744 209 GSWSGTEPSC 218
Cdd:PHA02927  252 NTWQPELPKC 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 165-219 1.92e-12

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: 62.48  E-value: 1.92e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622934744 165 CSNPGIPIGTRKVGS--RYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQ 219
Cdd:cd00033     1 CPPPPVPENGTVTGSkgSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
Sushi pfam00084
Sushi repeat (SCR repeat);
103-158 1.08e-11

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 60.21  E-value: 1.08e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622934744 103 CPRPQDFENGEYRPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 158
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 165-218 2.27e-11

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: 59.46  E-value: 2.27e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622934744  165 CSNPG-IPIGTRKVGS-RYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 218
Cdd:smart00032   1 CPPPPdIENGTVTSSSgTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 55-219 2.63e-11

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 64.67  E-value: 2.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  55 GQALEYVCPSGFYPYPVQTRTCRSTGSWSTLQTQdrktvkkaeCRAIRCPRPQDFENGEYRPRSPYYNVSdeISFHCYDG 134
Cdd:PHA02927   47 GDTIEYLCLPGYRKQKMGPIYAKCTGTGWTLFNQ---------CIKRRCPSPRDIDNGQLDIGGVDFGSS--ITYSCNSG 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 135 YTLRGSANRTCQVNGR----WSGQTAICDNGAgyC-SNPGIPIGTRKVGSRYRLEDS-VTYHCSRGLTLRGSQRRTCQeG 208
Cdd:PHA02927  116 YQLIGESKSYCELGSTgsmvWNPEAPICESVK--CqSPPSISNGRHNGYEDFYTDGSvVTYSCNSGYSLIGNSGVLCS-G 192

                         170
                  ....*....|.
gi 1622934744 209 GSWSgTEPSCQ 219
Cdd:PHA02927  193 GEWS-DPPTCQ 202
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 269-464 1.11e-08

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: 55.44  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 269 MNIYLVLDGSDSIGAGNFTGAKKCLVNLIEKVASYGVKPRYALVTYATYPRIWVKVSDQESSNAdwVTKKLSEInyedHK 348
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEE--PLSLVKHI----SQ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 349 LKSGTNTKRALQAVYSmmswpedippEGWNRTR-------HVIILMTDGLHNMGGDPITVIDE------IRDLLYIGK-- 413
Cdd:cd01469    75 LLGLTNTATAIQYVVT----------ELFSESNgarkdatKVLVVITDGESHDDPLLKDVIPQaeregiIRYAIGVGGhf 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622934744 414 DRKNPREDyldvyvfgvgplvdqvnINALASKKDnEQHVFKVKDMENLEDV 464
Cdd:cd01469   145 QRENSREE-----------------LKTIASKPP-EEHFFNVTDFAALKDI 177
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 225-465 1.52e-08

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: 56.49  E-value: 1.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 225 DTPQEVAEAFLSSLTETIEGVDAEDGHSPGEQQKRRIILDPSGSMNIYLVLDGSDSIGAGN-FTGAKKCLVNLIEkvaSY 303
Cdd:COG1240    49 LLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLD---DY 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 304 GVKPRYALVTYATYPRIWVKVSdqesSNADWVTKKLSEInyedhKLKSGTNTKRALQAVYSMMswpEDIPPEGwnrtRHV 383
Cdd:COG1240   126 RPRDRVGLVAFGGEAEVLLPLT----RDREALKRALDEL-----PPGGGTPLGDALALALELL---KRADPAR----RKV 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 384 IILMTDGLHNMG-GDPITVIDEIrdllyigkdrknpREDYLDVYVFGVG-PLVDQVNINALAskkdnEQ---HVFKVKDM 458
Cdd:COG1240   190 IVLLTDGRDNAGrIDPLEAAELA-------------AAAGIRIYTIGVGtEAVDEGLLREIA-----EAtggRYFRADDL 251


                  ....*..
gi 1622934744 459 ENLEDVF 465
Cdd:COG1240   252 SELAAIY 258
PHA02831 PHA02831
EEV host range protein; Provisional
 50-218 1.97e-08

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 56.15  E-value: 1.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  50 RLLQEGQALEYVCPSGFYPYPVqtrTCrSTGSWSTlqtqdrktvkKAECRAIR-CPRPQDFENGEYRPRSPYYNVSDEIS 128
Cdd:PHA02831   38 KVYEENENLEYKCNNNFDKVFV---TC-NNGSWST----------KNMCIGKRnCKDPVTILNGYIKNKKDQYSFGDSVT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 129 FHC----YDGYTLRGSANRTCqVNGRWSGQTAICDngAGYCSNPGIPIGTRKV-GSRYRLEDSVTYHCSRGLTLRGSQRR 203
Cdd:PHA02831  104 YACkvnkLEKYSIVGNETVKC-INKQWVPKYPVCK--LIRCKYPALQNGFLNVfEKKFYYGDIVNFKCKKGFILLGSSVS 180

                         170
                  ....*....|....*
gi 1622934744 204 TCQEGGSWSGTEPSC 218
Cdd:PHA02831  181 TCDINSIWYPGIPKC 195
PHA02817 PHA02817
EEV Host range protein; Provisional
 98-218 7.26e-08

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 53.79  E-value: 7.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  98 CRAIRCPRPQDFENGEYRPRSPYYNVSDEISFHCYDG-----YTLRGSANRTCQVNGRWSGQTAICDngAGYCSNP---- 168
Cdd:PHA02817   19 CDLNKCCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCK--IIRCRFPalqn 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622934744 169 ----GIPigtrkVGSRYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 218
Cdd:PHA02817   97 gfvnGIP-----DSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPIC 145
Sushi pfam00084
Sushi repeat (SCR repeat);
180-218 1.10e-07

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.03  E-value: 1.10e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622934744 180 RYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 218
Cdd:pfam00084  18 EYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02639 PHA02639
EEV host range protein; Provisional
 35-218 2.74e-07

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 53.13  E-value: 2.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  35 GSCSLEGV---------EIKGGSFRLLQE----GQALEYVCPSGFYPYPVQTRTC---RSTGSWSTlqtqdrktvKKAEC 98
Cdd:PHA02639   10 GVCYVHGVksiycdkpdDISNGFITELMEkyeiGKLIEYTCNTDYALIGDRFRTCikdKNNAIWSN---------KAPFC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  99 RAIRCPRPQDFENGEYRPRSPYYNVSDEISFHCYD----GYTLRGSANRTCQVNGRWSGQTAICDngAGYCSNPGIP--- 171
Cdd:PHA02639   81 MLKECNDPPSIINGKIYNKREMYKVGDEIYYVCNEhkgvQYSLVGNEKITCIQDKSWKPDPPICK--MINCRFPALQngy 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1622934744 172 IGTRKVGSRYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 218
Cdd:PHA02639  159 INGIPSNKKFYYKTRVGFSCKSGFDLVGEKYSTCNINATWFPSIPTC 205
PHA02639 PHA02639
EEV host range protein; Provisional
 99-219 1.21e-06

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 50.82  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  99 RAIRCPRPQDFENGEYRPRSPYYNVSDEISFHCYDGYTLRGSANRTC---QVNGRWSGQTAICdnGAGYCSNPGIPIGTR 175
Cdd:PHA02639   18 KSIYCDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCikdKNNAIWSNKAPFC--MLKECNDPPSIINGK 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622934744 176 KVGSR--YRLEDSVTYHCS--RGL--TLRGSQRRTCQEGGSWSGTEPSCQ 219
Cdd:PHA02639   96 IYNKRemYKVGDEIYYVCNehKGVqySLVGNEKITCIQDKSWKPDPPICK 145
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 270-390 1.68e-06

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: 48.76  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 270 NIYLVLDGSDSIGAGNFTGAKKCLVNLIEKVASYGVKPRYALVTYATYPRIwVKVSDQESSNADwVTKKLSEINYedhkL 349
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRT-EFYLNTYRSKDD-VLEAVKNLRY----I 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1622934744 350 KSGTNTKRALQAVYSMMSWPEDIPPEGWNRtrhVIILMTDG 390
Cdd:cd01472    76 GGGTNTGKALKYVRENLFTEASGSREGVPK---VLVVITDG 113
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 261-465 2.00e-06

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 50.10  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 261 IILDPSGSMNiylvldgSDSIGAgnftgAKKCLVNLIEKVasygvKP--RYALVTYATYPRIWV---KVSDQEssnadwv 335
Cdd:COG2304    96 FVIDVSGSMS-------GDKLEL-----AKEAAKLLVDQL-----RPgdRVSIVTFAGDARVLLpptPATDRA------- 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 336 tKKLSEINyedhKLKSG--TNTKRALQAVYSMmswPEDIPPEGWNRtrhVIILMTDGLHNMGgdpITVIDEIRDLLyigk 413
Cdd:COG2304   152 -KILAAID----RLQAGggTALGAGLELAYEL---ARKHFIPGRVN---RVILLTDGDANVG---ITDPEELLKLA---- 213

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622934744 414 drKNPREDYLDVYVFGVGPLVDQVNINALASKKDNEqhVFKVKDMENLEDVF 465
Cdd:COG2304   214 --EEAREEGITLTTLGVGSDYNEDLLERLADAGGGN--YYYIDDPEEAEKVF 261
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 269-431 7.84e-06

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 46.99  E-value: 7.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 269 MNIYLVLDGSDSIGAGN-FTGAKKCLVNLIEKVASYGVKPRYALVTYATYPRIWVKVSDQESSNAD---WVTKKLSEINY 344
Cdd:cd01471     1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDlalNAIRALLSLYY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 345 EdhklKSGTNTKRALQAV----YSMMSWPEDIPpegwnrtrHVIILMTDGLHNMGGDPITVIDEIRDLLYIgkdrknpre 420
Cdd:cd01471    81 P----NGSTNTTSALLVVekhlFDTRGNRENAP--------QLVIIMTDGIPDSKFRTLKEARKLRERGVI--------- 139

                         170
                  ....*....|.
gi 1622934744 421 dyldVYVFGVG 431
Cdd:cd01471   140 ----IAVLGVG 146
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 510-723 1.35e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 46.59  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 510 SCMGAVVSEYFVLTAAHCFTVDDKEH---SIKVSVGKKRD----LEIEKVLFHPDYNISGKkeagipefYDYDVALIKLK 582
Cdd:COG3591    13 VCTGTLIGPNLVLTAGHCVYDGAGGGwatNIVFVPGYNGGpygtATATRFRVPPGWVASGD--------AGYDYALLRLD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 583 NKLnydptirpiclpctEGTTRALRLPPTTTcqqqkeellpaqdikalfvseeekKLTRKEVYIkngdkkgscerdAQYa 662
Cdd:COG3591    85 EPL--------------GDTTGWLGLAFNDA------------------------PLAGEPVTI------------IGY- 113

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622934744 663 pGYDKVKDISevvtprFLCTGGVSPYADP------NTCRGDSGGPLIVHKRSRFIQVGVISWGVVDV 723
Cdd:COG3591   114 -PGDRPKDLS------LDCSGRVTGVQGNrlsydcDTTGGSSGSPVLDDSDGGGRVVGVHSAGGADR 173
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 271-457 1.49e-05

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 45.74  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 271 IYLVLDGSDSIGAGNFTGAKKCLVNLIEKVASYGVKPRYALVTYATYPRIWVKVsDQESSNADwVTKKLSEINYedhklK 350
Cdd:cd01482     3 IVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDL-NAYTSKED-VLAAIKNLPY-----K 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 351 SG-TNTKRALQAVYSMMSWPEDIPPEGwnrTRHVIILMTDGLHNmggdpitviDEIRDllyIGKDRKNpredyLDVYVFG 429
Cdd:cd01482    76 GGnTRTGKALTHVREKNFTPDAGARPG---VPKVVILITDGKSQ---------DDVEL---PARVLRN-----LGVNVFA 135

                         170       180
                  ....*....|....*....|....*....
gi 1622934744 430 VG-PLVDQVNINALASKKDnEQHVFKVKD 457
Cdd:cd01482   136 VGvKDADESELKMIASKPS-ETHVFNVAD 163
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 267-390 2.00e-05

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 45.84  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 267 GSMNIYLVLDGSDSIGAGNFTGAKKCLVNLIEKVAS-YGVKP-----RYALVTYATYPRIwVKVSDQESSNADWVTKKLS 340
Cdd:cd01480     1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKdYYRKDpagswRVGVVQYSDQQEV-EAGFLRDIRNYTSLKEAVD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622934744 341 EINYedhkLKSGTNTKRALQAVYSMMswpEDIPPEGWNRtrhVIILMTDG 390
Cdd:cd01480    80 NLEY----IGGGTFTDCALKYATEQL---LEGSHQKENK---FLLVITDG 119
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 89-218 4.18e-04

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 43.15  E-value: 4.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  89 DRKTVKKAECRaircprPQDFENGEYRPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGrWSgqtaICDNGAGYCSNP 168
Cdd:PHA02954  121 DTVTCPNAECQ------PLQLEHGSCQPVKEKYSFGEHITINCDVGYEVIGASYISCTANS-WN----VIPSCQQKCDIP 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622934744 169 GIPIGTRKvGSRYRLEDSVTYHCSRGLTLRGSQRRTCQEgGSWSGTEPSC 218
Cdd:PHA02954  190 SLSNGLIS-GSTFSIGGVIHLSCKSGFTLTGSPSSTCID-GKWNPVLPIC 237
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 270-453 7.93e-04

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: 40.85  E-value: 7.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 270 NIYLVLDGSDSIGaGNFTGAKKCLVNLIEKVASYGVKPRYALVTYATYPRIWVKVSDQESSNADWVTKKLSEINYedhkL 349
Cdd:cd01476     2 DLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLPKHNDGEELLEKVDNLRF----I 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 350 KSGTNTKRALQAVYSMMSwpediPPEGWN-RTRHVIILMTDGLHNmggdpitviDEIRDLLYIGKDRKNpredyLDVYVF 428
Cdd:cd01476    77 GGTTATGAAIEVALQQLD-----PSEGRReGIPKVVVVLTDGRSH---------DDPEKQARILRAVPN-----IETFAV 137

                         170       180
                  ....*....|....*....|....*
gi 1622934744 429 GVGPlVDQVNINALASKKDNEQHVF 453
Cdd:cd01476   138 GTGD-PGTVDTEELHSITGNEDHIF 161
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 55-83 8.87e-04

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: 8.87e-04
                           10        20
                   ....*....|....*....|....*....
gi 1622934744   55 GQALEYVCPSGFYPYPVQTRTCRSTGSWS 83
Cdd:smart00032  22 GDTVTYSCDPGYTLIGSSTITCLENGTWS 50
PHA02817 PHA02817
EEV Host range protein; Provisional
 75-158 1.67e-03

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 40.69  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744  75 TCRSTGSWSTlqtqdrktvKKAECRAIRCPRP---QDFENGEYRPRSPYYnvSDEISFHCYDGYTLRGSANRTCQVNGRW 151
Cdd:PHA02817   70 ICEKDGKWNK---------EFPVCKIIRCRFPalqNGFVNGIPDSKKFYY--ESEVSFSCKPGFVLIGTKYSVCGINSSW 138


                  ....*..
gi 1622934744 152 SGQTAIC 158
Cdd:PHA02817  139 IPKVPIC 145
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 271-406 4.55e-03

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 39.66  E-value: 4.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 271 IYLVLDGSDSIGAGNFTGAKKCLVNLIEKVASygvKPRYALVTYATYPRIwvkvsDQESSNADWVTKKLSEInyEDHKLK 350
Cdd:COG2425   121 VVLCVDTSGSMAGSKEAAAKAAALALLRALRP---NRRFGVILFDTEVVE-----DLPLTADDGLEDAIEFL--SGLFAG 190

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622934744 351 SGTNTKRALQAVYSMMSWPEdippegWNRTrhVIILMTDGLhnMGGDPITVIDEIR 406
Cdd:COG2425   191 GGTDIAPALRAALELLEEPD------YRNA--DIVLITDGE--AGVSPEELLREVR 236
VWA_2 pfam13519
von Willebrand factor type A domain;
271-386 5.24e-03

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 37.27  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934744 271 IYLVLDGSDSIGAGNFTGAKK-CLVNLIEKVASY--GVkpRYALVTYATYPRIWVKVSDqessNADWVTKKLSEINYEDh 347
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRLeAAKDAVLALLKSlpGD--RVGLVTFGDGPEVLIPLTK----DRAKILRALRRLEPKG- 73

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622934744 348 klkSGTNTKRALQAVYSMMswpedipPEGWNRTRHVIIL 386
Cdd:pfam13519  74 ---GGTNLAAALQLARAAL-------KHRRKNQPRRIVL 102
Sushi pfam00084
Sushi repeat (SCR repeat);
53-83 9.62e-03

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 35.17  E-value: 9.62e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1622934744  53 QEGQALEYVCPSGFYPYPVQTRTCRSTGSWS 83
Cdd:pfam00084  20 NYGASVSYECDPGYRLVGSPTITCQEDGTWS 50
 
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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