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Conserved domains on  [gi|584908|sp|P00751|]
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RecName: Full=Complement factor B; AltName: Full=C3/C5 convertase; AltName: Full=Glycine-rich beta glycoprotein; Short=GBG; AltName: Full=PBF2; AltName: Full=Properdin factor B; Contains: RecName: Full=Complement factor B Ba fragment; Contains: RecName: Full=Complement factor B Bb fragment; Flags: Precursor

Protein Classification

serine protease( domain architecture ID 10636848)

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 ...
 269-466 1.26e-114

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: 344.66  E-value: 1.26e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   269 MNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHK 348
Cdd:cd01470   1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   349 LKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVF 428
Cdd:cd01470  81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 584908   429 GVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFY 466
Cdd:cd01470 161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 488-755 3.01e-46

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: 164.76  E-value: 3.01e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   488 TDYHKQPWQAKIsviRPSKGHESCMGAVVSEYFVLTAAHCFtVDDKEHSIKVSVG--------GEKRDLEIEVVLFHPNY 559
Cdd:cd00190   7 AKIGSFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGshdlssneGGGQVIKVKKVIVHPNY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   560 NingkkeagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTtralrLPPTTTCQqqkeellpaqdikalfVS----- 634
Cdd:cd00190  83 N---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCT----------------VSgwgrt 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   635 EEEKKLTR--KEVYIKNGDKKgSCERDAQYAPgydkvkdiseVVTPRFLCTGGvsPYADPNTCRGDSGGPLIVHKRSRFI 712
Cdd:cd00190 133 SEGGPLPDvlQEVNVPIVSNA-ECKRAYSYGG----------TITDNMLCAGG--LEGGKDACQGDSGGPLVCNDNGRGV 199

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 584908   713 QVGVISWGVvdVCknqkRQKQVPAhardFHINLFQVLPWLKEK 755
Cdd:cd00190 200 LVGIVSWGS--GC----ARPNYPG----VYTRVSSYLDWIQKT 232
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 103-158 1.27e-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: 1.27e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 584908   103 CPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 158
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 165-219 1.97e-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: 1.97e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 584908   165 CSNPGIPIGTRKVGSQ--YRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQ 219
Cdd:cd00033   1 CPPPPVPENGTVTGSKgsYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 55-83 1.04e-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: 1.04e-03
                           10        20
                   ....*....|....*....|....*....
gi 584908       55 GQALEYVCPSGFYPYPVQTRTCRSTGSWS 83
Cdd:smart00032  22 GDTVTYSCDPGYTLIGSSTITCLENGTWS 50
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 269-466 1.26e-114

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: 344.66  E-value: 1.26e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   269 MNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHK 348
Cdd:cd01470   1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   349 LKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVF 428
Cdd:cd01470  81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 584908   429 GVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFY 466
Cdd:cd01470 161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 488-755 3.01e-46

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: 164.76  E-value: 3.01e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   488 TDYHKQPWQAKIsviRPSKGHESCMGAVVSEYFVLTAAHCFtVDDKEHSIKVSVG--------GEKRDLEIEVVLFHPNY 559
Cdd:cd00190   7 AKIGSFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGshdlssneGGGQVIKVKKVIVHPNY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   560 NingkkeagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTtralrLPPTTTCQqqkeellpaqdikalfVS----- 634
Cdd:cd00190  83 N---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCT----------------VSgwgrt 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   635 EEEKKLTR--KEVYIKNGDKKgSCERDAQYAPgydkvkdiseVVTPRFLCTGGvsPYADPNTCRGDSGGPLIVHKRSRFI 712
Cdd:cd00190 133 SEGGPLPDvlQEVNVPIVSNA-ECKRAYSYGG----------TITDNMLCAGG--LEGGKDACQGDSGGPLVCNDNGRGV 199

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 584908   713 QVGVISWGVvdVCknqkRQKQVPAhardFHINLFQVLPWLKEK 755
Cdd:cd00190 200 LVGIVSWGS--GC----ARPNYPG----VYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 488-721 5.15e-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: 155.53  E-value: 5.15e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908      488 TDYHKQPWQAKIsviRPSKGHESCMGAVVSEYFVLTAAHCFTvDDKEHSIKVSVG-------GEKRDLEIEVVLFHPNYN 560
Cdd:smart00020   8 ANIGSFPWQVSL---QYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGshdlssgEEGQVIKVSKVIIHPNYN 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908      561 ingkkeagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTegttrALRLPPTTTCQqqkeellpaqdikalfVS------ 634
Cdd:smart00020  84 ---------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCT----------------VSgwgrts 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908      635 EEEKKLTR--KEVYIKNGDKKgSCERDAQYapgydkvkdiSEVVTPRFLCTGGvsPYADPNTCRGDSGGPLiVHKRSRFI 712
Cdd:smart00020 134 EGAGSLPDtlQEVNVPIVSNA-TCRRAYSG----------GGAITDNMLCAGG--LEGGKDACQGDSGGPL-VCNDGRWV 199


                   ....*....
gi 584908      713 QVGVISWGV 721
Cdd:smart00020 200 LVGIVSWGS 208
Trypsin pfam00089
Trypsin;
491-752 1.31e-35

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 134.11  E-value: 1.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     491 HKQPWQAKISVirpSKGHESCMGAVVSEYFVLTAAHCF------TVDDKEHSIKVSVGGEKRdLEIEVVLFHPNYNingk 564
Cdd:pfam00089  10 GSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVsgasdvKVVLGAHNIVLREGGEQK-FDVEKIIVHPNYN---- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     565 keagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTtralrLPPTTTCQQQKEELlpaqdikalfVSEEEKKLTRKE 644
Cdd:pfam00089  82 -----PDTLDNDIALLKLESPVTLGDTVRPICLPDASSD-----LPVGTTCTVSGWGN----------TKTLGPSDTLQE 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     645 VYIKNGDkKGSCERdaqyapgydkvkDISEVVTPRFLCTGGVSPYAdpntCRGDSGGPLIVHKRsrfIQVGVISWGvvDV 724
Cdd:pfam00089 142 VTVPVVS-RETCRS------------AYGGTVTDTMICAGAGGKDA----CQGDSGGPLVCSDG---ELIGIVSWG--YG 199

                         250       260
                  ....*....|....*....|....*...
gi 584908     725 CKNQKRqkqvpahaRDFHINLFQVLPWL 752
Cdd:pfam00089 200 CASGNY--------PGVYTPVSSYLDWI 219
VWA pfam00092
von Willebrand factor type A domain;
270-467 1.04e-31

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 121.61  E-value: 1.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     270 NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeaDSSNADWVTKQLNEINYEDHKL 349
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLN--DYSSKEELLSAVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     350 KS-GTNTKKALQAVYSMMSWPDDvppegwnRTRHVIILMTDGlHNMGGDPITVIDEIRDllyigkdrknpreDYLDVYVF 428
Cdd:pfam00092  79 TNtGKALKYALENLFSSAAGARP-------GAPKVVVLLTDG-RSQDGDPEEVARELKS-------------AGVTVFAV 137

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 584908     429 GVGPLVNQvNINALASKKDnEQHVFKVKDMENLEDVFYQ 467
Cdd:pfam00092 138 GVGNADDE-ELRKIASEPG-EGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 270-463 1.71e-27

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 109.47  E-value: 1.71e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908      270 NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeaDSSNADWVTKQLNEINYedhKL 349
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLN--DSRSKDALLEALASLSY---KL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908      350 KSGTNTKKALQAVYSMMSwpddVPPEGWNR-TRHVIILMTDGLHNMGGDPItvIDEIRDLlyigkdrknpREDYLDVYVF 428
Cdd:smart00327  76 GGGTNLGAALQYALENLF----SKSAGSRRgAPKVVILITDGESNDGPKDL--LKAAKEL----------KRSGVKVFVV 139

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 584908      429 GVGPLVNQVNINALASKKDNEqHVFKVKDMENLED 463
Cdd:smart00327 140 GVGNDVDEEELKKLASAPGGV-YVFLPELLDLLID 173
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 494-720 2.05e-19

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 88.55  E-value: 2.05e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   494 PWQAKISVIRPSKGHeSCMGAVVSEYFVLTAAHCfTVDDKEHSIKVSVGGEKRD------LEIEVVLFHPNYNingkkea 567
Cdd:COG5640  43 PWMVALQSSNGPSGQ-FCGGTLIAPRWVLTAAHC-VDGDGPSDLRVVIGSTDLStsggtvVKVARIVVHPDYD------- 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   568 giPEFYDYDVALIKLKnklkygqtiRPIclpcteGTTRALRLPPTTTcqqqkeelLPAQDIKALFV-----SEEEKKL-- 640
Cdd:COG5640 114 --PATPGNDIALLKLA---------TPV------PGVAPAPLATSAD--------AAAPGTPATVAgwgrtSEGPGSQsg 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   641 TRKEVYIKNGDkkgscERDAQYAPGYDkvkdisevvTPRFLCTGGVSPYADpnTCRGDSGGPLIVHKRSRFIQVGVISWG 720
Cdd:COG5640 169 TLRKADVPVVS-----DATCAAYGGFD---------GGTMLCAGYPEGGKD--ACQGDSGGPLVVKDGGGWVLVGVVSWG 232
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 103-158 1.27e-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: 1.27e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 584908   103 CPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 158
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 103-158 1.37e-14

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: 68.71  E-value: 1.37e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 584908      103 CPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 158
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 165-219 1.97e-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: 1.97e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 584908   165 CSNPGIPIGTRKVGSQ--YRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQ 219
Cdd:cd00033   1 CPPPPVPENGTVTGSKgsYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 55-218 3.65e-12

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 67.37  E-value: 3.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     55 GQALEYVCPSGFYPYPVQTRTCR--STGS--WSTlktqdqktvRKAECRAIHCPRPHDFENGEYWPRSPYYNVSDEISFH 130
Cdd:PHA02927 105 GSSITYSCNSGYQLIGESKSYCElgSTGSmvWNP---------EAPICESVKCQSPPSISNGRHNGYEDFYTDGSVVTYS 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908    131 CYDGYTLRGSANRTCQvNGRWSgQTAICDngAGYCSNPGIPIGTRKVG--SQYRLEDSVTYHCSRGLTLRGSQRRTCQEG 208
Cdd:PHA02927 176 CNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGfkRSYSYNDNVDFKCKYGYKLSGSSSSTCSPG 251

                        170
                 ....*....|
gi 584908    209 GSWSGTEPSC 218
Cdd:PHA02927 252 NTWQPELPKC 261
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 165-218 2.55e-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: 2.55e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 584908      165 CSNPGIPIGTRKVGSQ--YRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 218
Cdd:smart00032   1 CPPPPDIENGTVTSSSgtYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
103-158 3.24e-10

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 56.35  E-value: 3.24e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 584908     103 CPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 158
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 225-465 9.57e-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: 56.87  E-value: 9.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   225 DTPQEVAEAFLSSLTETIEGVDAEDGHGPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGASN-FTGAKKCLVNLIEkvaSY 303
Cdd:COG1240  49 LLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLD---DY 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   304 GVKPRYGLVTYATYPKIWVKVSeadsSNADWVTKQLNEInyedhKLKSGTNTKKALQAVYSMMswpDDVPPEGwnrtRHV 383
Cdd:COG1240 126 RPRDRVGLVAFGGEAEVLLPLT----RDREALKRALDEL-----PPGGGTPLGDALALALELL---KRADPAR----RKV 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   384 IILMTDGLHNMG-GDPITVIDEIrdllyigkdrknpREDYLDVYVFGVG-PLVNQVNINALAskkdnEQ---HVFKVKDM 458
Cdd:COG1240 190 IVLLTDGRDNAGrIDPLEAAELA-------------AAAGIRIYTIGVGtEAVDEGLLREIA-----EAtggRYFRADDL 251


                ....*..
gi 584908   459 ENLEDVF 465
Cdd:COG1240 252 SELAAIY 258
Sushi pfam00084
Sushi repeat (SCR repeat);
180-218 9.12e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.42  E-value: 9.12e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 584908     180 QYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 218
Cdd:pfam00084  18 EYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 55-83 1.04e-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: 1.04e-03
                           10        20
                   ....*....|....*....|....*....
gi 584908       55 GQALEYVCPSGFYPYPVQTRTCRSTGSWS 83
Cdd:smart00032  22 GDTVTYSCDPGYTLIGSSTITCLENGTWS 50
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 269-466 1.26e-114

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: 344.66  E-value: 1.26e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   269 MNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHK 348
Cdd:cd01470   1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   349 LKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVF 428
Cdd:cd01470  81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 584908   429 GVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFY 466
Cdd:cd01470 161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 488-755 3.01e-46

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: 164.76  E-value: 3.01e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   488 TDYHKQPWQAKIsviRPSKGHESCMGAVVSEYFVLTAAHCFtVDDKEHSIKVSVG--------GEKRDLEIEVVLFHPNY 559
Cdd:cd00190   7 AKIGSFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGshdlssneGGGQVIKVKKVIVHPNY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   560 NingkkeagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTtralrLPPTTTCQqqkeellpaqdikalfVS----- 634
Cdd:cd00190  83 N---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCT----------------VSgwgrt 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   635 EEEKKLTR--KEVYIKNGDKKgSCERDAQYAPgydkvkdiseVVTPRFLCTGGvsPYADPNTCRGDSGGPLIVHKRSRFI 712
Cdd:cd00190 133 SEGGPLPDvlQEVNVPIVSNA-ECKRAYSYGG----------TITDNMLCAGG--LEGGKDACQGDSGGPLVCNDNGRGV 199

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 584908   713 QVGVISWGVvdVCknqkRQKQVPAhardFHINLFQVLPWLKEK 755
Cdd:cd00190 200 LVGIVSWGS--GC----ARPNYPG----VYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 488-721 5.15e-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: 155.53  E-value: 5.15e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908      488 TDYHKQPWQAKIsviRPSKGHESCMGAVVSEYFVLTAAHCFTvDDKEHSIKVSVG-------GEKRDLEIEVVLFHPNYN 560
Cdd:smart00020   8 ANIGSFPWQVSL---QYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGshdlssgEEGQVIKVSKVIIHPNYN 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908      561 ingkkeagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTegttrALRLPPTTTCQqqkeellpaqdikalfVS------ 634
Cdd:smart00020  84 ---------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCT----------------VSgwgrts 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908      635 EEEKKLTR--KEVYIKNGDKKgSCERDAQYapgydkvkdiSEVVTPRFLCTGGvsPYADPNTCRGDSGGPLiVHKRSRFI 712
Cdd:smart00020 134 EGAGSLPDtlQEVNVPIVSNA-TCRRAYSG----------GGAITDNMLCAGG--LEGGKDACQGDSGGPL-VCNDGRWV 199


                   ....*....
gi 584908      713 QVGVISWGV 721
Cdd:smart00020 200 LVGIVSWGS 208
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 269-453 1.69e-39

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: 143.20  E-value: 1.69e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   269 MNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeaDSSNADWVTKQLNEINYEDHk 348
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLN--DYKSKDDLLKAVKNLKYLGG- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   349 lkSGTNTKKALQAVYSMMSWPDdvppEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLlyigkdrknpredYLDVYVF 428
Cdd:cd01450  78 --GGTNTGKALQYALEQLFSES----NARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDE-------------GIKVFVV 138

                       170       180
                ....*....|....*....|....*
gi 584908   429 GVGPlVNQVNINALASKKdNEQHVF 453
Cdd:cd01450 139 GVGP-ADEEELREIASCP-SERHVF 161
Trypsin pfam00089
Trypsin;
491-752 1.31e-35

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 134.11  E-value: 1.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     491 HKQPWQAKISVirpSKGHESCMGAVVSEYFVLTAAHCF------TVDDKEHSIKVSVGGEKRdLEIEVVLFHPNYNingk 564
Cdd:pfam00089  10 GSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVsgasdvKVVLGAHNIVLREGGEQK-FDVEKIIVHPNYN---- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     565 keagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTtralrLPPTTTCQQQKEELlpaqdikalfVSEEEKKLTRKE 644
Cdd:pfam00089  82 -----PDTLDNDIALLKLESPVTLGDTVRPICLPDASSD-----LPVGTTCTVSGWGN----------TKTLGPSDTLQE 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     645 VYIKNGDkKGSCERdaqyapgydkvkDISEVVTPRFLCTGGVSPYAdpntCRGDSGGPLIVHKRsrfIQVGVISWGvvDV 724
Cdd:pfam00089 142 VTVPVVS-RETCRS------------AYGGTVTDTMICAGAGGKDA----CQGDSGGPLVCSDG---ELIGIVSWG--YG 199

                         250       260
                  ....*....|....*....|....*...
gi 584908     725 CKNQKRqkqvpahaRDFHINLFQVLPWL 752
Cdd:pfam00089 200 CASGNY--------PGVYTPVSSYLDWI 219
VWA pfam00092
von Willebrand factor type A domain;
270-467 1.04e-31

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 121.61  E-value: 1.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     270 NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeaDSSNADWVTKQLNEINYEDHKL 349
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLN--DYSSKEELLSAVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     350 KS-GTNTKKALQAVYSMMSWPDDvppegwnRTRHVIILMTDGlHNMGGDPITVIDEIRDllyigkdrknpreDYLDVYVF 428
Cdd:pfam00092  79 TNtGKALKYALENLFSSAAGARP-------GAPKVVVLLTDG-RSQDGDPEEVARELKS-------------AGVTVFAV 137

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 584908     429 GVGPLVNQvNINALASKKDnEQHVFKVKDMENLEDVFYQ 467
Cdd:pfam00092 138 GVGNADDE-ELRKIASEPG-EGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 270-463 1.71e-27

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 109.47  E-value: 1.71e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908      270 NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeaDSSNADWVTKQLNEINYedhKL 349
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLN--DSRSKDALLEALASLSY---KL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908      350 KSGTNTKKALQAVYSMMSwpddVPPEGWNR-TRHVIILMTDGLHNMGGDPItvIDEIRDLlyigkdrknpREDYLDVYVF 428
Cdd:smart00327  76 GGGTNLGAALQYALENLF----SKSAGSRRgAPKVVILITDGESNDGPKDL--LKAAKEL----------KRSGVKVFVV 139

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 584908      429 GVGPLVNQVNINALASKKDNEqHVFKVKDMENLED 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 6.71e-23

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 95.71  E-value: 6.71e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   270 NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeaDSSNADWVTKQLNEINYedhKL 349
Cdd:cd00198   2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLT--TDTDKADLLEAIDALKK---GL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   350 KSGTNTKKALQAVYSMMSWPDDvppegwNRTRHVIILMTDGLHNmgGDPITVIDEIRDLlyigkdrknpREDYLDVYVFG 429
Cdd:cd00198  77 GGGTNIGAALRLALELLKSAKR------PNARRVIILLTDGEPN--DGPELLAEAAREL----------RKLGITVYTIG 138

                       170       180
                ....*....|....*....|....
gi 584908   430 VGPLVNQVNINALASkKDNEQHVF 453
Cdd:cd00198 139 IGDDANEDELKEIAD-KTTGGAVF 161
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 494-720 2.05e-19

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 88.55  E-value: 2.05e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   494 PWQAKISVIRPSKGHeSCMGAVVSEYFVLTAAHCfTVDDKEHSIKVSVGGEKRD------LEIEVVLFHPNYNingkkea 567
Cdd:COG5640  43 PWMVALQSSNGPSGQ-FCGGTLIAPRWVLTAAHC-VDGDGPSDLRVVIGSTDLStsggtvVKVARIVVHPDYD------- 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   568 giPEFYDYDVALIKLKnklkygqtiRPIclpcteGTTRALRLPPTTTcqqqkeelLPAQDIKALFV-----SEEEKKL-- 640
Cdd:COG5640 114 --PATPGNDIALLKLA---------TPV------PGVAPAPLATSAD--------AAAPGTPATVAgwgrtSEGPGSQsg 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   641 TRKEVYIKNGDkkgscERDAQYAPGYDkvkdisevvTPRFLCTGGVSPYADpnTCRGDSGGPLIVHKRSRFIQVGVISWG 720
Cdd:COG5640 169 TLRKADVPVVS-----DATCAAYGGFD---------GGTMLCAGYPEGGKD--ACQGDSGGPLVVKDGGGWVLVGVVSWG 232
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 103-158 1.27e-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: 1.27e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 584908   103 CPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 158
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 103-158 1.37e-14

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: 68.71  E-value: 1.37e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 584908      103 CPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 158
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 165-219 1.97e-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: 1.97e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 584908   165 CSNPGIPIGTRKVGSQ--YRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQ 219
Cdd:cd00033   1 CPPPPVPENGTVTGSKgsYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 55-218 3.65e-12

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 67.37  E-value: 3.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     55 GQALEYVCPSGFYPYPVQTRTCR--STGS--WSTlktqdqktvRKAECRAIHCPRPHDFENGEYWPRSPYYNVSDEISFH 130
Cdd:PHA02927 105 GSSITYSCNSGYQLIGESKSYCElgSTGSmvWNP---------EAPICESVKCQSPPSISNGRHNGYEDFYTDGSVVTYS 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908    131 CYDGYTLRGSANRTCQvNGRWSgQTAICDngAGYCSNPGIPIGTRKVG--SQYRLEDSVTYHCSRGLTLRGSQRRTCQEG 208
Cdd:PHA02927 176 CNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGfkRSYSYNDNVDFKCKYGYKLSGSSSSTCSPG 251

                        170
                 ....*....|
gi 584908    209 GSWSGTEPSC 218
Cdd:PHA02927 252 NTWQPELPKC 261
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 165-218 2.55e-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: 2.55e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 584908      165 CSNPGIPIGTRKVGSQ--YRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 218
Cdd:smart00032   1 CPPPPDIENGTVTSSSgtYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
103-158 3.24e-10

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 56.35  E-value: 3.24e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 584908     103 CPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 158
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 55-219 4.71e-10

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 61.21  E-value: 4.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     55 GQALEYVCPSGFYPYPVQTRTCRSTGSWSTLKTQdqktvrkaeCRAIHCPRPHDFENGEYWPRSPYYNVSdeISFHCYDG 134
Cdd:PHA02927  47 GDTIEYLCLPGYRKQKMGPIYAKCTGTGWTLFNQ---------CIKRRCPSPRDIDNGQLDIGGVDFGSS--ITYSCNSG 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908    135 YTLRGSANRTCQVNGR----WSGQTAICDNGAgyC-SNPGIPIGTRKVGSQYRLEDS-VTYHCSRGLTLRGSQRRTCQeG 208
Cdd:PHA02927 116 YQLIGESKSYCELGSTgsmvWNPEAPICESVK--CqSPPSISNGRHNGYEDFYTDGSvVTYSCNSGYSLIGNSGVLCS-G 192

                        170
                 ....*....|.
gi 584908    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 7.03e-09

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: 55.82  E-value: 7.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   269 MNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSE-ADSSNADWVTKQLneinyedH 347
Cdd:cd01469   1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEyRTKEEPLSLVKHI-------S 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   348 KLKSGTNTKKALQAVYSmmswpddvppEGWNRTR-------HVIILMTDGLHNMGGDPITVIDEirdllyigkdrknPRE 420
Cdd:cd01469  74 QLLGLTNTATAIQYVVT----------ELFSESNgarkdatKVLVVITDGESHDDPLLKDVIPQ-------------AER 130

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 584908   421 DYLDVYVFGVGPLVNQVN----INALASKKDnEQHVFKVKDMENLEDV 464
Cdd:cd01469 131 EGIIRYAIGVGGHFQRENsreeLKTIASKPP-EEHFFNVTDFAALKDI 177
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 225-465 9.57e-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: 56.87  E-value: 9.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   225 DTPQEVAEAFLSSLTETIEGVDAEDGHGPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGASN-FTGAKKCLVNLIEkvaSY 303
Cdd:COG1240  49 LLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLD---DY 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   304 GVKPRYGLVTYATYPKIWVKVSeadsSNADWVTKQLNEInyedhKLKSGTNTKKALQAVYSMMswpDDVPPEGwnrtRHV 383
Cdd:COG1240 126 RPRDRVGLVAFGGEAEVLLPLT----RDREALKRALDEL-----PPGGGTPLGDALALALELL---KRADPAR----RKV 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   384 IILMTDGLHNMG-GDPITVIDEIrdllyigkdrknpREDYLDVYVFGVG-PLVNQVNINALAskkdnEQ---HVFKVKDM 458
Cdd:COG1240 190 IVLLTDGRDNAGrIDPLEAAELA-------------AAAGIRIYTIGVGtEAVDEGLLREIA-----EAtggRYFRADDL 251


                ....*..
gi 584908   459 ENLEDVF 465
Cdd:COG1240 252 SELAAIY 258
PHA02817 PHA02817
EEV Host range protein; Provisional
 98-218 7.48e-08

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 53.79  E-value: 7.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     98 CRAIHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDG-----YTLRGSANRTCQVNGRWSGQTAICDngAGYCSNP---- 168
Cdd:PHA02817  19 CDLNKCCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCK--IIRCRFPalqn 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 584908    169 ----GIPigtrkVGSQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 218
Cdd:PHA02817  97 gfvnGIP-----DSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPIC 145
Sushi pfam00084
Sushi repeat (SCR repeat);
180-218 9.12e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.42  E-value: 9.12e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 584908     180 QYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 218
Cdd:pfam00084  18 EYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 269-435 1.27e-07

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: 52.39  E-value: 1.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   269 MNIYLVLDGSDSIGASN-FTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNAD---WVTKQLNEINY 344
Cdd:cd01471   1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDlalNAIRALLSLYY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   345 EdhklKSGTNTKKALQAV----YSMMSWPDDVPpegwnrtrHVIILMTDGLHNMGGDPITVIDEIRDLLYIgkdrknpre 420
Cdd:cd01471  81 P----NGSTNTTSALLVVekhlFDTRGNRENAP--------QLVIIMTDGIPDSKFRTLKEARKLRERGVI--------- 139

                       170
                ....*....|....*
gi 584908   421 dyldVYVFGVGPLVN 435
Cdd:cd01471 140 ----IAVLGVGQGVN 150
PHA02831 PHA02831
EEV host range protein; Provisional
 50-218 2.36e-07

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 53.07  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     50 RLLQEGQALEYVCPSGFYPYPVqtrTCrSTGSWSTLKTQDQKTvrkaecraiHCPRPHDFENGEYWPRSPYYNVSDEISF 129
Cdd:PHA02831  38 KVYEENENLEYKCNNNFDKVFV---TC-NNGSWSTKNMCIGKR---------NCKDPVTILNGYIKNKKDQYSFGDSVTY 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908    130 HC----YDGYTLRGSANRTCqVNGRWSGQTAICDngAGYCSNPGIPIGTRKV-GSQYRLEDSVTYHCSRGLTLRGSQRRT 204
Cdd:PHA02831 105 ACkvnkLEKYSIVGNETVKC-INKQWVPKYPVCK--LIRCKYPALQNGFLNVfEKKFYYGDIVNFKCKKGFILLGSSVST 181

                        170
                 ....*....|....
gi 584908    205 CQEGGSWSGTEPSC 218
Cdd:PHA02831 182 CDINSIWYPGIPKC 195
PHA02639 PHA02639
EEV host range protein; Provisional
 55-218 3.79e-07

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 52.36  E-value: 3.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     55 GQALEYVCPSGFYPYPVQTRTC---RSTGSWSTlktqdqktvRKAECRAIHCPRPHDFENGEYWPRSPYYNVSDEISFHC 131
Cdd:PHA02639  43 GKLIEYTCNTDYALIGDRFRTCikdKNNAIWSN---------KAPFCMLKECNDPPSIINGKIYNKREMYKVGDEIYYVC 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908    132 YD----GYTLRGSANRTCQVNGRWSGQTAICDngAGYCSNPGIP---IGTRKVGSQYRLEDSVTYHCSRGLTLRGSQRRT 204
Cdd:PHA02639 114 NEhkgvQYSLVGNEKITCIQDKSWKPDPPICK--MINCRFPALQngyINGIPSNKKFYYKTRVGFSCKSGFDLVGEKYST 191

                        170
                 ....*....|....
gi 584908    205 CQEGGSWSGTEPSC 218
Cdd:PHA02639 192 CNINATWFPSIPTC 205
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 270-390 4.36e-07

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


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 50.30  E-value: 4.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   270 NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIwvkvsEADS---SNADWVTKQLNEINYed 346
Cdd:cd01472   2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRT-----EFYLntyRSKDDVLEAVKNLRY-- 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 584908   347 hkLKSGTNTKKALQAVYSMMSWPDDVPPEGWNRtrhVIILMTDG 390
Cdd:cd01472  75 --IGGGTNTGKALKYVRENLFTEASGSREGVPK---VLVVITDG 113
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 261-465 5.16e-07

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 52.03  E-value: 5.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   261 IVLDPSGSMNiylvldgSDSIGAsnftgAKKCLVNLIEKVasygvKP--RYGLVTYATYPKIWVKVSEADSsnadwVTKQ 338
Cdd:COG2304  96 FVIDVSGSMS-------GDKLEL-----AKEAAKLLVDQL-----RPgdRVSIVTFAGDARVLLPPTPATD-----RAKI 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   339 LNEINyedhKLKSG--TNTKKALQAVYSMmswPDDVPPEGWNRtrhVIILMTDGLHNMGgdpITVIDEIRDLLyigkdrK 416
Cdd:COG2304 154 LAAID----RLQAGggTALGAGLELAYEL---ARKHFIPGRVN---RVILLTDGDANVG---ITDPEELLKLA------E 214

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 584908   417 NPREDYLDVYVFGVGPLVNQVNINALASKKDNEqhVFKVKDMENLEDVF 465
Cdd:COG2304 215 EAREEGITLTTLGVGSDYNEDLLERLADAGGGN--YYYIDDPEEAEKVF 261
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 267-450 1.04e-06

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: 49.69  E-value: 1.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   267 GSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVAS-YGVKP-----RYGLVTYATYPKIwVKVSEADSSNADWVTKQLN 340
Cdd:cd01480   1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKdYYRKDpagswRVGVVQYSDQQEV-EAGFLRDIRNYTSLKEAVD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   341 EINYedhkLKSGTNTKKALQAVYSMMSwpdDVPPEGWNRtrhVIILMTDGlHNMGGDPITVIDEIRDLLYIGkdrknpre 420
Cdd:cd01480  80 NLEY----IGGGTFTDCALKYATEQLL---EGSHQKENK---FLLVITDG-HSDGSPDGGIEKAVNEADHLG-------- 140

                       170       180       190
                ....*....|....*....|....*....|
gi 584908   421 dyLDVYVFGVGPLVNQVNINALASKKDNEQ 450
Cdd:cd01480 141 --IKIFFVAVGSQNEEPLSRIACDGKSALY 168
PHA02639 PHA02639
EEV host range protein; Provisional
 99-219 3.69e-06

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 49.66  E-value: 3.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     99 RAIHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTC---QVNGRWSGQTAICdnGAGYCSNPGIPIGTR 175
Cdd:PHA02639  18 KSIYCDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCikdKNNAIWSNKAPFC--MLKECNDPPSIINGK 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 584908    176 KVGSQ--YRLEDSVTYHCS--RGL--TLRGSQRRTCQEGGSWSGTEPSCQ 219
Cdd:PHA02639  96 IYNKRemYKVGDEIYYVCNehKGVqySLVGNEKITCIQDKSWKPDPPICK 145
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 271-457 1.01e-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: 46.51  E-value: 1.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   271 IYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeADSSNADwVTKQLNEINYedhklK 350
Cdd:cd01482   3 IVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLN-AYTSKED-VLAAIKNLPY-----K 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   351 SG-TNTKKALQAVYSMMSWPDDVPPEGwnrTRHVIILMTDGLHNmggdpitviDEIRDllyIGKDRKNpredyLDVYVFG 429
Cdd:cd01482  76 GGnTRTGKALTHVREKNFTPDAGARPG---VPKVVILITDGKSQ---------DDVEL---PARVLRN-----LGVNVFA 135

                       170       180       190
                ....*....|....*....|....*....|
gi 584908   430 VGplVNQVNINALAS--KKDNEQHVFKVKD 457
Cdd:cd01482 136 VG--VKDADESELKMiaSKPSETHVFNVAD 163
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 510-724 5.88e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 44.67  E-value: 5.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   510 SCMGAVVSEYFVLTAAHCFTVDDKEH---SIKVSVGGEKRD---LEIEVVLFHPNYNINGKkeagipefYDYDVALIKLK 583
Cdd:COG3591  13 VCTGTLIGPNLVLTAGHCVYDGAGGGwatNIVFVPGYNGGPygtATATRFRVPPGWVASGD--------AGYDYALLRLD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908   584 NKLkygqtirpiclpctEGTTRALRLPPTTTcqqqkeellpaqdikalfvseeekKLTRKEVYIkngdkkgscerdAQYa 663
Cdd:COG3591  85 EPL--------------GDTTGWLGLAFNDA------------------------PLAGEPVTI------------IGY- 113

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 584908   664 pGYDKVKDISevvtprFLCTGGVSPYADP------NTCRGDSGGPLIVHKRSRFIQVGVISWGVVDV 724
Cdd:COG3591 114 -PGDRPKDLS------LDCSGRVTGVQGNrlsydcDTTGGSSGSPVLDDSDGGGRVVGVHSAGGADR 173
VWA_2 pfam13519
von Willebrand factor type A domain;
261-386 6.42e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 39.58  E-value: 6.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     261 IVLDPSGSMniylvldGSDSIGASNFTGAKKCLVNLIEKVAsyGVkpRYGLVTYATYPKIWVKVseadSSNADWVTKQLN 340
Cdd:pfam13519   3 FVLDTSGSM-------RNGDYGPTRLEAAKDAVLALLKSLP--GD--RVGLVTFGDGPEVLIPL----TKDRAKILRALR 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 584908     341 EINYEDhklkSGTNTKKALQAVYSMMswpddvpPEGWNRTRHVIIL 386
Cdd:pfam13519  68 RLEPKG----GGTNLAAALQLARAAL-------KHRRKNQPRRIVL 102
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 55-83 1.04e-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: 1.04e-03
                           10        20
                   ....*....|....*....|....*....
gi 584908       55 GQALEYVCPSGFYPYPVQTRTCRSTGSWS 83
Cdd:smart00032  22 GDTVTYSCDPGYTLIGSSTITCLENGTWS 50
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 89-218 1.35e-03

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 41.61  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584908     89 DQKTVRKAECRaihcprPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGrWSgqtaICDNGAGYCSNP 168
Cdd:PHA02954 121 DTVTCPNAECQ------PLQLEHGSCQPVKEKYSFGEHITINCDVGYEVIGASYISCTANS-WN----VIPSCQQKCDIP 189

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 584908    169 GIPIGTRKvGSQYRLEDSVTYHCSRGLTLRGSQRRTCQEgGSWSGTEPSC 218
Cdd:PHA02954 190 SLSNGLIS-GSTFSIGGVIHLSCKSGFTLTGSPSSTCID-GKWNPVLPIC 237
 
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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