NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|291395817|ref|XP_002714337|]
View 

PREDICTED: complement factor B [Oryctolagus cuniculus]

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 1.80e-104

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  Cd Length: 198  Bit Score: 321.16  E-value: 1.80e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 269 MNIYLVLDGSDSIGASNFTGAKRCLVNLIEKVASYGVRPRYGLVTYATYPNVLVRVSDPKSSDANWVTEKLNQISYEDHK 348
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 349 LKTGTNTKRALVEVYNMMSWPGDVPPEGWNRTRHVIILMTDGLHNMGGDPVTVINEIRDLLNIGKDRKNPREDYLDVYVF 428
Cdd:cd01470   81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 291395817 429 GVGPLVEPANINALASKKENEQHVFRVKDMEHLEDVF 465
Cdd:cd01470  161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVF 197
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
488-755 3.88e-43

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: 156.28  E-value: 3.88e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 488 TDYHKQPWHAKISVTRpqkGHENCMGAVVSEYFVLTAAHCFtVDDQKHSIKVSVG--------GKRRDLEVEEVLFHANY 559
Cdd:cd00190    7 AKIGSFPWQVSLQYTG---GRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGshdlssneGGGQVIKVKKVIVHPNY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 560 NingkkaegiPEFYDYDVALVKLKSKLTYSQTLRPICLPCTEGTtralrLPQSTTCQqhkeellpaknvkalfVS----- 634
Cdd:cd00190   83 N---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCT----------------VSgwgrt 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 635 EEEKKLTR--KEVYIKNGDKkASCERDAQYAPgydkvkdisaVVTPRFLCTGGVDpyADPNTCRGDSGGPLIIHKRSRFI 712
Cdd:cd00190  133 SEGGPLPDvlQEVNVPIVSN-AECKRAYSYGG----------TITDNMLCAGGLE--GGKDACQGDSGGPLVCNDNGRGV 199
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 291395817 713 QVGVISWGVvdVCkdhkRRLQAPA-YARdfhinLFQVLPWLKDK 755
Cdd:cd00190  200 LVGIVSWGS--GC----ARPNYPGvYTR-----VSSYLDWIQKT 232
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
103-158 1.08e-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  Cd Length: 57  Bit Score: 72.88  E-value: 1.08e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 291395817 103 CPKPQDFENGDYWPRSPYYNVNDEISFHCYHGYTLRGSANRTCQVNGRWDGQTAIC 158
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
165-219 1.29e-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  Cd Length: 57  Bit Score: 64.02  E-value: 1.29e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 291395817 165 CPNPGIPIGTRKAGS--RYRLEDTVTYHCSQGLTLRGSQQRTCQEGGSWSGTEPSCQ 219
Cdd:cd00033    1 CPPPPVPENGTVTGSkgSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
55-84 2.86e-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  Cd Length: 56  Bit Score: 36.74  E-value: 2.86e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 291395817    55 GQALEYVCPSGFYPYPVQTRTCRSMGSWSP 84
Cdd:smart00032  22 GDTVTYSCDPGYTLIGSSTITCLENGTWSP 51
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
488-751 2.10e-40

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 [Multi-domain]  Cd Length: 229  Bit Score: 148.59  E-value: 2.10e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817   488 TDYHKQPWHAKISVTRpqkGHENCMGAVVSEYFVLTAAHCFTvDDQKHSIKVSVG-------GKRRDLEVEEVLFHANYN 560
Cdd:smart00020   8 ANIGSFPWQVSLQYGG---GRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGshdlssgEEGQVIKVSKVIIHPNYN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817   561 ingkkaegiPEFYDYDVALVKLKSKLTYSQTLRPICLPCTegttrALRLPQSTTCQ---QHKEELLPAKNVKALfvseee 637
Cdd:smart00020  84 ---------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCTvsgWGRTSEGAGSLPDTL------ 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817   638 kkltrKEVYIKNGDKKAsCERDAQYAPgydkvkdisaVVTPRFLCTGGvdPYADPNTCRGDSGGPLiIHKRSRFIQVGVI 717
Cdd:smart00020 144 -----QEVNVPIVSNAT-CRRAYSGGG----------AITDNMLCAGG--LEGGKDACQGDSGGPL-VCNDGRWVLVGIV 204
                          250       260       270
                   ....*....|....*....|....*....|....
gi 291395817   718 SWGVvdVCkdhkrrlqAPAYARDFHINLFQVLPW 751
Cdd:smart00020 205 SWGS--GC--------ARPGKPGVYTRVSSYLDW 228
 
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 1.80e-104

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  Cd Length: 198  Bit Score: 321.16  E-value: 1.80e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 269 MNIYLVLDGSDSIGASNFTGAKRCLVNLIEKVASYGVRPRYGLVTYATYPNVLVRVSDPKSSDANWVTEKLNQISYEDHK 348
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 349 LKTGTNTKRALVEVYNMMSWPGDVPPEGWNRTRHVIILMTDGLHNMGGDPVTVINEIRDLLNIGKDRKNPREDYLDVYVF 428
Cdd:cd01470   81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 291395817 429 GVGPLVEPANINALASKKENEQHVFRVKDMEHLEDVF 465
Cdd:cd01470  161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVF 197
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
488-755 3.88e-43

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: 156.28  E-value: 3.88e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 488 TDYHKQPWHAKISVTRpqkGHENCMGAVVSEYFVLTAAHCFtVDDQKHSIKVSVG--------GKRRDLEVEEVLFHANY 559
Cdd:cd00190    7 AKIGSFPWQVSLQYTG---GRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGshdlssneGGGQVIKVKKVIVHPNY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 560 NingkkaegiPEFYDYDVALVKLKSKLTYSQTLRPICLPCTEGTtralrLPQSTTCQqhkeellpaknvkalfVS----- 634
Cdd:cd00190   83 N---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCT----------------VSgwgrt 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 635 EEEKKLTR--KEVYIKNGDKkASCERDAQYAPgydkvkdisaVVTPRFLCTGGVDpyADPNTCRGDSGGPLIIHKRSRFI 712
Cdd:cd00190  133 SEGGPLPDvlQEVNVPIVSN-AECKRAYSYGG----------TITDNMLCAGGLE--GGKDACQGDSGGPLVCNDNGRGV 199
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 291395817 713 QVGVISWGVvdVCkdhkRRLQAPA-YARdfhinLFQVLPWLKDK 755
Cdd:cd00190  200 LVGIVSWGS--GC----ARPNYPGvYTR-----VSSYLDWIQKT 232
VWA pfam00092
von Willebrand factor type A domain;
270-465 4.02e-28

von Willebrand factor type A domain;


Pssm-ID: 278519  Cd Length: 174  Bit Score: 111.99  E-value: 4.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  270 NIYLVLDGSDSIGASNFTGAKRCLVNLIEKVASYGVRPRYGLVTYATYPNVLVRVSDPKSSDAnwVTEKLNQISYEDHKL 349
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLSKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEE--LLSAVDNLRYSGGGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  350 K-TGTNTKRALVEVYNMMSWPGDvppegwnRTRHVIILMTDGlHNMGGDPVTVINEIRDllnigkdrknpreDYLDVYVF 428
Cdd:pfam00092  79 TnTGKALKYALENLFSSSAGARP-------GAPKVVVLLTDG-RSNDGDPEEAARELKS-------------AGVTVFAV 137
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 291395817  429 GVGPLVEpANINALASKKeNEQHVFRVKDMEHLEDVF 465
Cdd:pfam00092 138 GVGNADN-EELNKIASEP-DEGHVFTVSDFEALQDLQ 172
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
270-463 2.58e-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  Cd Length: 175  Bit Score: 109.85  E-value: 2.58e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817   270 NIYLVLDGSDSIGASNFTGAKRCLVNLIEKVASYGVRPRYGLVTYATYPNVLVRVSDPKSSDAnwVTEKLNQISYedhKL 349
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDA--LLEALASLSY---KL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817   350 KTGTNTKRALVEVYNMMSwpgdVPPEGWNR-TRHVIILMTDGLHNMGG-DPVTVINEIrdllnigkdrknpREDYLDVYV 427
Cdd:smart00327  76 GGGTNLGAALQYALENLF----SKSAGSRRgAPKVVILITDGESNDGPkDLLKAAKEL-------------KRSGVKVFV 138
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 291395817   428 FGVGPLVEPANINALASKKENEqHVFRVKDMEHLED 463
Cdd:smart00327 139 VGVGNDVDEEELKKLASAPGGV-YVFLPELLDLLID 173
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
103-158 1.08e-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  Cd Length: 57  Bit Score: 72.88  E-value: 1.08e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 291395817 103 CPKPQDFENGDYWPRSPYYNVNDEISFHCYHGYTLRGSANRTCQVNGRWDGQTAIC 158
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
103-158 1.89e-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  Cd Length: 56  Bit Score: 69.48  E-value: 1.89e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 291395817   103 CPKPQDFENGDYWPRSPYYNVNDEISFHCYHGYTLRGSANRTCQVNGRWDGQTAIC 158
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
165-219 1.29e-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  Cd Length: 57  Bit Score: 64.02  E-value: 1.29e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 291395817 165 CPNPGIPIGTRKAGS--RYRLEDTVTYHCSQGLTLRGSQQRTCQEGGSWSGTEPSCQ 219
Cdd:cd00033    1 CPPPPVPENGTVTGSkgSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
165-218 2.67e-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  Cd Length: 56  Bit Score: 60.23  E-value: 2.67e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 291395817   165 CPNPGIPIGTRKAGS--RYRLEDTVTYHCSQGLTLRGSQQRTCQEGGSWSGTEPSC 218
Cdd:smart00032   1 CPPPPDIENGTVTSSsgTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
103-158 3.94e-11

Sushi repeat (SCR repeat);


Pssm-ID: 278512  Cd Length: 56  Bit Score: 59.83  E-value: 3.94e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 291395817  103 CPKPQDFENGDYWPRSPYYNVNDEISFHCYHGYTLRGSANRTCQVNGRWDGQTAIC 158
Cdd:pfam00084   1 CPPPPDLPNGSVSATKNEYNYGAKVEYECDPGYRLVGNPVITCQEDGTWSPPFPEC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
165-218 1.02e-07

Sushi repeat (SCR repeat);


Pssm-ID: 278512  Cd Length: 56  Bit Score: 49.81  E-value: 1.02e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 291395817  165 CPNPGIP--IGTRKAGSRYRLEDTVTYHCSQGLTLRGSQQRTCQEGGSWSGTEPSC 218
Cdd:pfam00084   1 CPPPPDLpnGSVSATKNEYNYGAKVEYECDPGYRLVGNPVITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
55-84 2.86e-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  Cd Length: 56  Bit Score: 36.74  E-value: 2.86e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 291395817    55 GQALEYVCPSGFYPYPVQTRTCRSMGSWSP 84
Cdd:smart00032  22 GDTVTYSCDPGYTLIGSSTITCLENGTWSP 51
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
55-84 9.26e-03

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


Pssm-ID: 153056  Cd Length: 57  Bit Score: 35.13  E-value: 9.26e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 291395817  55 GQALEYVCPSGFYPYPVQTRTCRSMGSWSP 84
Cdd:cd00033   22 GSTVTYSCNEGYTLVGSSTITCTENGGWSP 51
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
488-751 2.10e-40

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 [Multi-domain]  Cd Length: 229  Bit Score: 148.59  E-value: 2.10e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817   488 TDYHKQPWHAKISVTRpqkGHENCMGAVVSEYFVLTAAHCFTvDDQKHSIKVSVG-------GKRRDLEVEEVLFHANYN 560
Cdd:smart00020   8 ANIGSFPWQVSLQYGG---GRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGshdlssgEEGQVIKVSKVIIHPNYN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817   561 ingkkaegiPEFYDYDVALVKLKSKLTYSQTLRPICLPCTegttrALRLPQSTTCQ---QHKEELLPAKNVKALfvseee 637
Cdd:smart00020  84 ---------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCTvsgWGRTSEGAGSLPDTL------ 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817   638 kkltrKEVYIKNGDKKAsCERDAQYAPgydkvkdisaVVTPRFLCTGGvdPYADPNTCRGDSGGPLiIHKRSRFIQVGVI 717
Cdd:smart00020 144 -----QEVNVPIVSNAT-CRRAYSGGG----------AITDNMLCAGG--LEGGKDACQGDSGGPL-VCNDGRWVLVGIV 204
                          250       260       270
                   ....*....|....*....|....*....|....
gi 291395817   718 SWGVvdVCkdhkrrlqAPAYARDFHINLFQVLPW 751
Cdd:smart00020 205 SWGS--GC--------ARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
491-752 7.91e-30

Trypsin;


Pssm-ID: 278516 [Multi-domain]  Cd Length: 218  Bit Score: 118.31  E-value: 7.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  491 HKQPWHAKISVTRpqkGHENCMGAVVSEYFVLTAAHCFtvdDQKHSIKVSVG--------GKRRDLEVEEVLFHANYNIN 562
Cdd:pfam00089  10 GSFPWQVSLQVSS---GKHFCGGSLISENWVLTAAHCV---SNASSVRVVLGahnivlreGGEQKFDVEKIIVHPNYNPD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  563 GkkaegipefyDYDVALVKLKSKLTYSQTLRPICLPCTEGTtralrLPQSTTCqqhkeellpaknvkalFVS------EE 636
Cdd:pfam00089  84 T----------DNDIALLKLKSPVTLGDTVRPICLPTASSD-----LPVGTTC----------------TVSgwgntkTL 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  637 EKKLTRKEVYIKNGDkKASCERdaqyapgydkvkDISAVVTPRFLCTGGVDPYAdpntCRGDSGGPLIIHKRsrfIQVGV 716
Cdd:pfam00089 133 GRPDTLQEVTVPVVS-RETCRS------------AYGGTVTDTMICAGAGGKDA----CQGDSGGPLVCSDG---ELVGI 192
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 291395817  717 ISWGvvDVCkdhkrrlqAPAYARDFHINLFQVLPWL 752
Cdd:pfam00089 193 VSWG--YGC--------ASGNYPGVYTPVSSYLDWI 218
PHA02927 PHA02927
secreted complement-binding protein; Provisional
55-218 2.13e-14

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 72.76  E-value: 2.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  55 GQALEYVCPSGFYPYPVQTRTCR--SMGS--WSPlrtqdqktvAKAECRAIRCPKPQDFENGDYWPRSPYYNVNDEISFH 130
Cdd:PHA02927 105 GSSITYSCNSGYQLIGESKSYCElgSTGSmvWNP---------EAPICESVKCQSPPSISNGRHNGYEDFYTDGSVVTYS 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 131 CYHGYTLRGSANRTCQvNGRWDgQTAICDdgAGYCPNPGIPIGTRKAGSR--YRLEDTVTYHCSQGLTLRGSQQRTCQEG 208
Cdd:PHA02927 176 CNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGFKrsYSYNDNVDFKCKYGYKLSGSSSSTCSPG 251
                        170
                 ....*....|
gi 291395817 209 GSWSGTEPSC 218
Cdd:PHA02927 252 NTWQPELPKC 261
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
503-720 2.48e-04

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 42.94  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 503 RPQKGHENCMGAVVSEYFVLTAAHCFtvdDQKHSIKVSVGGKRRDLE---------VEEVLFHANYningkkaegIPEFY 573
Cdd:COG5640   55 SDYVSGTFCGGSKLGGRYVLTAAHCA---DASSPISSDVNRVVVDLNdssqaerghVRTIYVHEFY---------SPGNL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 574 DYDVALVKL-------KSKLTYSQTLRPICLPCTE---------GTTRALRLPQSTtcqqhkEELLPAKNVKALFVSEEe 637
Cdd:COG5640  123 GNDIAVLELaraaslpRVKITSFDASDTFLNSVTTvspmtngtfGVTTPSDVPRSS------PKGTILHEVAVLFVPLS- 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 638 kklTRKEVYikngdkkasceRDAQYAPGYDKVKDISAVVTPRflctggvdpyadpNTCRGDSGGPLIIHKRSRFIQVGVI 717
Cdd:COG5640  196 ---TCAQYK-----------GCANASDGATGLTGFCAGRPPK-------------DACQGDSGGPIFHKGEEGRVQRGVV 248

                 ...
gi 291395817 718 SWG 720
Cdd:COG5640  249 SWG 251
 
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 1.80e-104

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  Cd Length: 198  Bit Score: 321.16  E-value: 1.80e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 269 MNIYLVLDGSDSIGASNFTGAKRCLVNLIEKVASYGVRPRYGLVTYATYPNVLVRVSDPKSSDANWVTEKLNQISYEDHK 348
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 349 LKTGTNTKRALVEVYNMMSWPGDVPPEGWNRTRHVIILMTDGLHNMGGDPVTVINEIRDLLNIGKDRKNPREDYLDVYVF 428
Cdd:cd01470   81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 291395817 429 GVGPLVEPANINALASKKENEQHVFRVKDMEHLEDVF 465
Cdd:cd01470  161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVF 197
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
488-755 3.88e-43

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: 156.28  E-value: 3.88e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 488 TDYHKQPWHAKISVTRpqkGHENCMGAVVSEYFVLTAAHCFtVDDQKHSIKVSVG--------GKRRDLEVEEVLFHANY 559
Cdd:cd00190    7 AKIGSFPWQVSLQYTG---GRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGshdlssneGGGQVIKVKKVIVHPNY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 560 NingkkaegiPEFYDYDVALVKLKSKLTYSQTLRPICLPCTEGTtralrLPQSTTCQqhkeellpaknvkalfVS----- 634
Cdd:cd00190   83 N---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCT----------------VSgwgrt 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 635 EEEKKLTR--KEVYIKNGDKkASCERDAQYAPgydkvkdisaVVTPRFLCTGGVDpyADPNTCRGDSGGPLIIHKRSRFI 712
Cdd:cd00190  133 SEGGPLPDvlQEVNVPIVSN-AECKRAYSYGG----------TITDNMLCAGGLE--GGKDACQGDSGGPLVCNDNGRGV 199
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 291395817 713 QVGVISWGVvdVCkdhkRRLQAPA-YARdfhinLFQVLPWLKDK 755
Cdd:cd00190  200 LVGIVSWGS--GC----ARPNYPGvYTR-----VSSYLDWIQKT 232
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
269-453 1.09e-34

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  Cd Length: 161  Bit Score: 130.10  E-value: 1.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 269 MNIYLVLDGSDSIGASNFTGAKRCLVNLIEKVASYGVRPRYGLVTYATYPNVLVRVSDpkSSDANWVTEKLNQISYEDHk 348
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLND--YKSKDDLLKAVKNLKYLGG- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 349 lkTGTNTKRALVEVYNMMSWPGdvppEGWNRTRHVIILMTDGLHNMGGDPVTVINEIRDLlnigkdrknpredYLDVYVF 428
Cdd:cd01450   78 --GGTNTGKALQYALEQLFSES----NARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDE-------------GIKVFVV 138
                        170       180
                 ....*....|....*....|....*
gi 291395817 429 GVGPLVEpANINALASKKeNEQHVF 453
Cdd:cd01450  139 GVGPADE-EELREIASCP-SERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
270-465 4.02e-28

von Willebrand factor type A domain;


Pssm-ID: 278519  Cd Length: 174  Bit Score: 111.99  E-value: 4.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  270 NIYLVLDGSDSIGASNFTGAKRCLVNLIEKVASYGVRPRYGLVTYATYPNVLVRVSDPKSSDAnwVTEKLNQISYEDHKL 349
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLSKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEE--LLSAVDNLRYSGGGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  350 K-TGTNTKRALVEVYNMMSWPGDvppegwnRTRHVIILMTDGlHNMGGDPVTVINEIRDllnigkdrknpreDYLDVYVF 428
Cdd:pfam00092  79 TnTGKALKYALENLFSSSAGARP-------GAPKVVVLLTDG-RSNDGDPEEAARELKS-------------AGVTVFAV 137
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 291395817  429 GVGPLVEpANINALASKKeNEQHVFRVKDMEHLEDVF 465
Cdd:pfam00092 138 GVGNADN-EELNKIASEP-DEGHVFTVSDFEALQDLQ 172
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
270-463 2.58e-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  Cd Length: 175  Bit Score: 109.85  E-value: 2.58e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817   270 NIYLVLDGSDSIGASNFTGAKRCLVNLIEKVASYGVRPRYGLVTYATYPNVLVRVSDPKSSDAnwVTEKLNQISYedhKL 349
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDA--LLEALASLSY---KL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817   350 KTGTNTKRALVEVYNMMSwpgdVPPEGWNR-TRHVIILMTDGLHNMGG-DPVTVINEIrdllnigkdrknpREDYLDVYV 427
Cdd:smart00327  76 GGGTNLGAALQYALENLF----SKSAGSRRgAPKVVILITDGESNDGPkDLLKAAKEL-------------KRSGVKVFV 138
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 291395817   428 FGVGPLVEPANINALASKKENEqHVFRVKDMEHLED 463
Cdd:smart00327 139 VGVGNDVDEEELKKLASAPGGV-YVFLPELLDLLID 173
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
270-453 5.61e-21

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  Cd Length: 161  Bit Score: 91.09  E-value: 5.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 270 NIYLVLDGSDSIGASNFTGAKRCLVNLIEKVASYGVRPRYGLVTYATYPNVLVRVSDPKSSDAnwVTEKLNQISYedhKL 349
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKAD--LLEAIDALKK---GL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 350 KTGTNTKRALVEVYNMMSWPGDvppegwNRTRHVIILMTDGLHNmgGDPVTVINEIRDLlnigkdrknpREDYLDVYVFG 429
Cdd:cd00198   77 GGGTNIGAALRLALELLKSAKR------PNARRVIILLTDGEPN--DGPELLAEAAREL----------RKLGITVYTIG 138
                        170       180
                 ....*....|....*....|....
gi 291395817 430 VGPLVEPANINALASkKENEQHVF 453
Cdd:cd00198  139 IGDDANEDELKEIAD-KTTGGAVF 161
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
103-158 1.08e-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  Cd Length: 57  Bit Score: 72.88  E-value: 1.08e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 291395817 103 CPKPQDFENGDYWPRSPYYNVNDEISFHCYHGYTLRGSANRTCQVNGRWDGQTAIC 158
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
103-158 1.89e-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  Cd Length: 56  Bit Score: 69.48  E-value: 1.89e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 291395817   103 CPKPQDFENGDYWPRSPYYNVNDEISFHCYHGYTLRGSANRTCQVNGRWDGQTAIC 158
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
165-219 1.29e-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  Cd Length: 57  Bit Score: 64.02  E-value: 1.29e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 291395817 165 CPNPGIPIGTRKAGS--RYRLEDTVTYHCSQGLTLRGSQQRTCQEGGSWSGTEPSCQ 219
Cdd:cd00033    1 CPPPPVPENGTVTGSkgSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
165-218 2.67e-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  Cd Length: 56  Bit Score: 60.23  E-value: 2.67e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 291395817   165 CPNPGIPIGTRKAGS--RYRLEDTVTYHCSQGLTLRGSQQRTCQEGGSWSGTEPSC 218
Cdd:smart00032   1 CPPPPDIENGTVTSSsgTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
103-158 3.94e-11

Sushi repeat (SCR repeat);


Pssm-ID: 278512  Cd Length: 56  Bit Score: 59.83  E-value: 3.94e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 291395817  103 CPKPQDFENGDYWPRSPYYNVNDEISFHCYHGYTLRGSANRTCQVNGRWDGQTAIC 158
Cdd:pfam00084   1 CPPPPDLPNGSVSATKNEYNYGAKVEYECDPGYRLVGNPVITCQEDGTWSPPFPEC 56
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
269-431 3.80e-08

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  Cd Length: 186  Bit Score: 52.77  E-value: 3.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 269 MNIYLVLDGSDSIGASN-FTGAKRCLVNLIEKVASYGVRPRYGLVTYATYPNVLVRVSDPKSSD---ANWVTEKLNQISY 344
Cdd:cd01471    1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNkdlALNAIRALLSLYY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 345 edhklKTG-TNTKRALVEVYNMMSwpgDVPPEGWNRTRHVIIlMTDGLHNMGGDPVTVINEIRDLLNIgkdrknpredyl 423
Cdd:cd01471   81 -----PNGsTNTTSALLVVEKHLF---DTRGNRENAPQLVII-MTDGIPDSKFRTLKEARKLRERGVI------------ 139

                 ....*...
gi 291395817 424 dVYVFGVG 431
Cdd:cd01471  140 -IAVLGVG 146
Sushi pfam00084
Sushi repeat (SCR repeat);
165-218 1.02e-07

Sushi repeat (SCR repeat);


Pssm-ID: 278512  Cd Length: 56  Bit Score: 49.81  E-value: 1.02e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 291395817  165 CPNPGIP--IGTRKAGSRYRLEDTVTYHCSQGLTLRGSQQRTCQEGGSWSGTEPSC 218
Cdd:pfam00084   1 CPPPPDLpnGSVSATKNEYNYGAKVEYECDPGYRLVGNPVITCQEDGTWSPPFPEC 56
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
267-459 6.57e-07

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  Cd Length: 186  Bit Score: 48.92  E-value: 6.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 267 GSMNIYLVLDGSDSIGASNFTGAKRCLVNLIEKVASYGVRP------RYGLVTYATYPNVlVRVSDPKSSDANWVTEKLN 340
Cdd:cd01480    1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKdpagswRVGVVQYSDQQEV-EAGFLRDIRNYTSLKEAVD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 341 QISYedhkLKTGTNTKRALVEVYNMMSwpgDVPPEGWNRtrhVIILMTDGlHNMGGDPVTVINEIRDLLNIGkdrknpre 420
Cdd:cd01480   80 NLEY----IGGGTFTDCALKYATEQLL---EGSHQKENK---FLLVITDG-HSDGSPDGGIEKAVNEADHLG-------- 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 291395817 421 dyLDVYVFGVGPLVEPANINALASKKENEQHV--------FRVKDME 459
Cdd:cd01480  141 --IKIFFVAVGSQNEEPLSRIACDGKSALYREnfaellwsFFIDDET 185
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
269-464 8.42e-07

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  Cd Length: 177  Bit Score: 48.51  E-value: 8.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 269 MNIYLVLDGSDSIGASNFTGAKRCLVNLIEKVASYGVRPRYGLVTYATYPNVLVRVSDPKSSDAnwVTEKLNQISYEDHK 348
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEE--PLSLVKHISQLLGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 349 LKTGTNTKRALVEVYNmmswpgdvPPEGWNR-TRHVIILMTDGLHNMGGDPVTVINE------IRDLLNIGK--DRKNPR 419
Cdd:cd01469   79 TNTATAIQYVVTELFS--------ESNGARKdATKVLVVITDGESHDDPLLKDVIPQaeregiIRYAIGVGGhfQRENSR 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 291395817 420 EDyldvyvfgvgplvepanINALASKKEnEQHVFRVKDMEHLEDV 464
Cdd:cd01469  151 EE-----------------LKTIASKPP-EEHFFNVTDFAALKDI 177
VWA_2 pfam13519
von Willebrand factor type A domain;
261-445 1.68e-06

von Willebrand factor type A domain;


Pssm-ID: 290253  Cd Length: 172  Bit Score: 47.72  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  261 IVLDPAGSMNiylvldgSDSIGASNFTGAKRCLVNLIEKvasygvRP--RYGLVTYATYPNVLVrvsdPKSSDANWVTEK 338
Cdd:pfam13519   4 IVLDTSGSMN-------ATDLGPTRLTAARAALADLLKA------LPgdRVGLVAFAGSAYLVS----PLTDDRAALLAA 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  339 LNQISYEDHKLkTGTNTKRALVEVYNMMSWPGDVppegwnrtRHVIILMTDglhnmGGDPVTVINEIRDLLNIGkdrknp 418
Cdd:pfam13519  67 LNALSPRIMPG-GGTNLAAALALALRLLASAGGG--------SGAIVLITD-----GEDAPSLLAAARALKAAG------ 126
                         170       180
                  ....*....|....*....|....*...
gi 291395817  419 redyLDVYVFGVGPLVE-PANINALASK 445
Cdd:pfam13519 127 ----VRLYVIGVGTDEGaEAALQRLAEA 150
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
270-390 7.33e-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  Cd Length: 164  Bit Score: 45.68  E-value: 7.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 270 NIYLVLDGSDSIGASNFTGAKRCLVNLIEkvaSYGVRP---RYGLVTYATYPNV---LVRVSDPKSsdanwVTEKLNQIS 343
Cdd:cd01472    2 DIVFLVDGSESIGLSNFNLVKDFVKRVVE---RLDIGPdgvRVGVVQYSDDPRTefyLNTYRSKDD-----VLEAVKNLR 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 291395817 344 YedhkLKTGTNTKRALVEVYNMMSWPGDVPPEGWNRtrhVIILMTDG 390
Cdd:cd01472   74 Y----IGGGTNTGKALKYVRENLFTEASGSREGVPK---VLVVITDG 113
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
271-457 5.54e-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  Cd Length: 164  Bit Score: 43.04  E-value: 5.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 271 IYLVLDGSDSIGASNFTGAKRCLVNLIEKVASYGVRPRYGLVTYAtypnvlvrvSDPKS-------SDANWVTEKLNQIS 343
Cdd:cd01482    3 IVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYS---------DDPRTefdlnayTSKEDVLAAIKNLP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 344 YedhklKTG-TNTKRALVEVY-NMMSWPGDVPPEgwnrTRHVIILMTDGlhnmggdpvtvinEIRDLLNIGKDRKnpRED 421
Cdd:cd01482   74 Y-----KGGnTRTGKALTHVReKNFTPDAGARPG----VPKVVILITDG-------------KSQDDVELPARVL--RNL 129
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 291395817 422 YLDVYVFGVGPLVEpANINALASKKeNEQHVFRVKD 457
Cdd:cd01482  130 GVNVFAVGVKDADE-SELKMIASKP-SETHVFNVAD 163
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
270-431 7.67e-04

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


Pssm-ID: 238744  Cd Length: 180  Bit Score: 40.01  E-value: 7.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 270 NIYLVLDGSDSIGA------SNFTGAKRCLVNLIEKvasygvRP--RYGLVTYATYPNVLVrvsdPKSSDANWVTEKLNQ 341
Cdd:cd01467    4 DIMIALDVSGSMLAqdfvkpSRLEAAKEVLSDFIDR------REndRIGLVVFAGAAFTQA----PLTLDRESLKELLED 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 342 ISYEDhkLKTGTNTKRALVEVYNMMSwpgdvPPEGWNRtrhVIILMTDGLHNMGG-DPVTVIneirdllNIGKDRKnpre 420
Cdd:cd01467   74 IKIGL--AGQGTAIGDAIGLAIKRLK-----NSEAKER---VIVLLTDGENNAGEiDPATAA-------ELAKNKG---- 132
                        170
                 ....*....|.
gi 291395817 421 dyLDVYVFGVG 431
Cdd:cd01467  133 --VRIYTIGVG 141
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
270-453 1.68e-03

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  Cd Length: 163  Bit Score: 38.53  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 270 NIYLVLDGSDSIGaSNFTGAKRCLVNLIEKVASYGVRPRYGLVTYATYPNVLVRVSDPKSSDANWVTEKLNQISYedhkL 349
Cdd:cd01476    2 DLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLPKHNDGEELLEKVDNLRF----I 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 350 KTGTNTKRALVEVYNMMSwpgdvPPEGWN-RTRHVIILMTDGLHNmgGDPVTVINEIRDLLNIgkdrknpredylDVYVF 428
Cdd:cd01476   77 GGTTATGAAIEVALQQLD-----PSEGRReGIPKVVVVLTDGRSH--DDPEKQARILRAVPNI------------ETFAV 137
                        170       180
                 ....*....|....*....|....*
gi 291395817 429 GVGPLVEPANiNALASKKENEQHVF 453
Cdd:cd01476  138 GTGDPGTVDT-EELHSITGNEDHIF 161
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
55-84 2.86e-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  Cd Length: 56  Bit Score: 36.74  E-value: 2.86e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 291395817    55 GQALEYVCPSGFYPYPVQTRTCRSMGSWSP 84
Cdd:smart00032  22 GDTVTYSCDPGYTLIGSSTITCLENGTWSP 51
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
55-84 9.26e-03

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


Pssm-ID: 153056  Cd Length: 57  Bit Score: 35.13  E-value: 9.26e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 291395817  55 GQALEYVCPSGFYPYPVQTRTCRSMGSWSP 84
Cdd:cd00033   22 GSTVTYSCNEGYTLVGSSTITCTENGGWSP 51
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
488-751 2.10e-40

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 [Multi-domain]  Cd Length: 229  Bit Score: 148.59  E-value: 2.10e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817   488 TDYHKQPWHAKISVTRpqkGHENCMGAVVSEYFVLTAAHCFTvDDQKHSIKVSVG-------GKRRDLEVEEVLFHANYN 560
Cdd:smart00020   8 ANIGSFPWQVSLQYGG---GRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGshdlssgEEGQVIKVSKVIIHPNYN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817   561 ingkkaegiPEFYDYDVALVKLKSKLTYSQTLRPICLPCTegttrALRLPQSTTCQ---QHKEELLPAKNVKALfvseee 637
Cdd:smart00020  84 ---------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCTvsgWGRTSEGAGSLPDTL------ 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817   638 kkltrKEVYIKNGDKKAsCERDAQYAPgydkvkdisaVVTPRFLCTGGvdPYADPNTCRGDSGGPLiIHKRSRFIQVGVI 717
Cdd:smart00020 144 -----QEVNVPIVSNAT-CRRAYSGGG----------AITDNMLCAGG--LEGGKDACQGDSGGPL-VCNDGRWVLVGIV 204
                          250       260       270
                   ....*....|....*....|....*....|....
gi 291395817   718 SWGVvdVCkdhkrrlqAPAYARDFHINLFQVLPW 751
Cdd:smart00020 205 SWGS--GC--------ARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
491-752 7.91e-30

Trypsin;


Pssm-ID: 278516 [Multi-domain]  Cd Length: 218  Bit Score: 118.31  E-value: 7.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  491 HKQPWHAKISVTRpqkGHENCMGAVVSEYFVLTAAHCFtvdDQKHSIKVSVG--------GKRRDLEVEEVLFHANYNIN 562
Cdd:pfam00089  10 GSFPWQVSLQVSS---GKHFCGGSLISENWVLTAAHCV---SNASSVRVVLGahnivlreGGEQKFDVEKIIVHPNYNPD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  563 GkkaegipefyDYDVALVKLKSKLTYSQTLRPICLPCTEGTtralrLPQSTTCqqhkeellpaknvkalFVS------EE 636
Cdd:pfam00089  84 T----------DNDIALLKLKSPVTLGDTVRPICLPTASSD-----LPVGTTC----------------TVSgwgntkTL 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  637 EKKLTRKEVYIKNGDkKASCERdaqyapgydkvkDISAVVTPRFLCTGGVDPYAdpntCRGDSGGPLIIHKRsrfIQVGV 716
Cdd:pfam00089 133 GRPDTLQEVTVPVVS-RETCRS------------AYGGTVTDTMICAGAGGKDA----CQGDSGGPLVCSDG---ELVGI 192
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 291395817  717 ISWGvvDVCkdhkrrlqAPAYARDFHINLFQVLPWL 752
Cdd:pfam00089 193 VSWG--YGC--------ASGNYPGVYTPVSSYLDWI 218
PHA02927 PHA02927
secreted complement-binding protein; Provisional
55-218 2.13e-14

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 72.76  E-value: 2.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  55 GQALEYVCPSGFYPYPVQTRTCR--SMGS--WSPlrtqdqktvAKAECRAIRCPKPQDFENGDYWPRSPYYNVNDEISFH 130
Cdd:PHA02927 105 GSSITYSCNSGYQLIGESKSYCElgSTGSmvWNP---------EAPICESVKCQSPPSISNGRHNGYEDFYTDGSVVTYS 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 131 CYHGYTLRGSANRTCQvNGRWDgQTAICDdgAGYCPNPGIPIGTRKAGSR--YRLEDTVTYHCSQGLTLRGSQQRTCQEG 208
Cdd:PHA02927 176 CNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGFKrsYSYNDNVDFKCKYGYKLSGSSSSTCSPG 251
                        170
                 ....*....|
gi 291395817 209 GSWSGTEPSC 218
Cdd:PHA02927 252 NTWQPELPKC 261
PHA02927 PHA02927
secreted complement-binding protein; Provisional
55-219 2.03e-10

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 60.82  E-value: 2.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  55 GQALEYVCPSGFYPYPVQTRTCRSMGSWSPLRTQdqktvakaeCRAIRCPKPQDFENGDYwpRSPYYNVNDEISFHCYHG 134
Cdd:PHA02927  47 GDTIEYLCLPGYRKQKMGPIYAKCTGTGWTLFNQ---------CIKRRCPSPRDIDNGQL--DIGGVDFGSSITYSCNSG 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 135 YTLRGSANRTCQVNGR----WDGQTAICDdgAGYCPNPGIPIGTRKAGSR--YRLEDTVTYHCSQGLTLRGSQQRTCQeG 208
Cdd:PHA02927 116 YQLIGESKSYCELGSTgsmvWNPEAPICE--SVKCQSPPSISNGRHNGYEdfYTDGSVVTYSCNSGYSLIGNSGVLCS-G 192
                        170
                 ....*....|.
gi 291395817 209 GSWSgTEPSCQ 219
Cdd:PHA02927 193 GEWS-DPPTCQ 202
PHA02817 PHA02817
EEV Host range protein; Provisional
98-218 1.11e-08

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 54.95  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  98 CRAIRCPKPQDFENGDYWPRSPYYNVNDEISFHCYHG-----YTLRGSANRTCQVNGRWDGQTAICDdgAGYCPNP---- 168
Cdd:PHA02817  19 CDLNKCCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCK--IIRCRFPalqn 96
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 291395817 169 ----GIPigtrkAGSRYRLEDTVTYHCSQGLTLRGSQQRTCQEGGSWSGTEPSC 218
Cdd:PHA02817  97 gfvnGIP-----DSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPIC 145
PHA02927 PHA02927
secreted complement-binding protein; Provisional
34-158 1.46e-07

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 52.35  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  34 QSPCSLEGVEiKGGSFQLLQEGQALEYVCPSGFYPYPVQTRTCrSMGSWSPLRTqdqktvakaeCRAIRCPKPQdFENG- 112
Cdd:PHA02927 149 QSPPSISNGR-HNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLC-SGGEWSDPPT----------CQIVKCPHPT-ISNGy 215
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 291395817 113 --DYWPRSpyYNVNDEISFHCYHGYTLRGSANRTCQVNGRWDGQTAIC 158
Cdd:PHA02927 216 lsSGFKRS--YSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
PHA02639 PHA02639
EEV host range protein; Provisional
55-218 3.34e-07

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 51.59  E-value: 3.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  55 GQALEYVCPSGFYPYPVQTRTC---RSMGSWSplrtqdqktvAKAE-CRAIRCPKPQDFENGDYWPRSPYYNVNDEISFH 130
Cdd:PHA02639  43 GKLIEYTCNTDYALIGDRFRTCikdKNNAIWS----------NKAPfCMLKECNDPPSIINGKIYNKREMYKVGDEIYYV 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 131 C--YHG--YTLRGSANRTCQVNGRWDGQTAICDdgAGYCPNPGIP---IGTRKAGSRYRLEDTVTYHCSQGLTLRGSQQR 203
Cdd:PHA02639 113 CneHKGvqYSLVGNEKITCIQDKSWKPDPPICK--MINCRFPALQngyINGIPSNKKFYYKTRVGFSCKSGFDLVGEKYS 190
                        170
                 ....*....|....*
gi 291395817 204 TCQEGGSWSGTEPSC 218
Cdd:PHA02639 191 TCNINATWFPSIPTC 205
PHA02831 PHA02831
EEV host range protein; Provisional
53-218 1.53e-06

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 49.22  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  53 QEGQALEYVCPSGFYPYPVqtrTCRSmGSWSplrtqdqktvAKAECRAIR-CPKPQDFENGDYWPRSPYYNVNDEISFHC 131
Cdd:PHA02831  41 EENENLEYKCNNNFDKVFV---TCNN-GSWS----------TKNMCIGKRnCKDPVTILNGYIKNKKDQYSFGDSVTYAC 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 132 ----YHGYTLRGSANRTCqVNGRWDGQTAICDdgAGYCPNPGIPIGTRKA-GSRYRLEDTVTYHCSQGLTLRGSQQRTCQ 206
Cdd:PHA02831 107 kvnkLEKYSIVGNETVKC-INKQWVPKYPVCK--LIRCKYPALQNGFLNVfEKKFYYGDIVNFKCKKGFILLGSSVSTCD 183
                        170
                 ....*....|..
gi 291395817 207 EGGSWSGTEPSC 218
Cdd:PHA02831 184 INSIWYPGIPKC 195
PHA02639 PHA02639
EEV host range protein; Provisional
99-219 3.38e-06

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 48.12  E-value: 3.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  99 RAIRCPKPQDFENGDYWPRSPYYNVNDEISFHCYHGYTLRGSANRTC---QVNGRWDGQTAICddGAGYCPNPGIPIGTR 175
Cdd:PHA02639  18 KSIYCDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCikdKNNAIWSNKAPFC--MLKECNDPPSIINGK 95
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 291395817 176 KAGSR--YRLEDTVTYHCSQ----GLTLRGSQQRTCQEGGSWSGTEPSCQ 219
Cdd:PHA02639  96 IYNKRemYKVGDEIYYVCNEhkgvQYSLVGNEKITCIQDKSWKPDPPICK 145
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
89-218 8.06e-05

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 43.92  E-value: 8.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  89 DQKTVAKAECraircpKPQDFENGDYWPRSPYYNVNDEISFHCYHGYTLRGSANRTCQVNGrWDgqtaICDDGAGYCPNP 168
Cdd:PHA02954 121 DTVTCPNAEC------QPLQLEHGSCQPVKEKYSFGEHITINCDVGYEVIGASYISCTANS-WN----VIPSCQQKCDIP 189
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 291395817 169 GIPIGTrKAGSRYRLEDTVTYHCSQGLTLRGSQQRTCQEgGSWSGTEPSC 218
Cdd:PHA02954 190 SLSNGL-ISGSTFSIGGVIHLSCKSGFTLTGSPSSTCID-GKWNPVLPIC 237
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
503-720 2.48e-04

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 42.94  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 503 RPQKGHENCMGAVVSEYFVLTAAHCFtvdDQKHSIKVSVGGKRRDLE---------VEEVLFHANYningkkaegIPEFY 573
Cdd:COG5640   55 SDYVSGTFCGGSKLGGRYVLTAAHCA---DASSPISSDVNRVVVDLNdssqaerghVRTIYVHEFY---------SPGNL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 574 DYDVALVKL-------KSKLTYSQTLRPICLPCTE---------GTTRALRLPQSTtcqqhkEELLPAKNVKALFVSEEe 637
Cdd:COG5640  123 GNDIAVLELaraaslpRVKITSFDASDTFLNSVTTvspmtngtfGVTTPSDVPRSS------PKGTILHEVAVLFVPLS- 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817 638 kklTRKEVYikngdkkasceRDAQYAPGYDKVKDISAVVTPRflctggvdpyadpNTCRGDSGGPLIIHKRSRFIQVGVI 717
Cdd:COG5640  196 ---TCAQYK-----------GCANASDGATGLTGFCAGRPPK-------------DACQGDSGGPIFHKGEEGRVQRGVV 248

                 ...
gi 291395817 718 SWG 720
Cdd:COG5640  249 SWG 251
PHA02817 PHA02817
EEV Host range protein; Provisional
75-158 1.50e-03

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 39.54  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291395817  75 TCRSMGSWSPlrtqdqktvAKAECRAIRC--PKPQD-FENGdyWPRSPYYNVNDEISFHCYHGYTLRGSANRTCQVNGRW 151
Cdd:PHA02817  70 ICEKDGKWNK---------EFPVCKIIRCrfPALQNgFVNG--IPDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSW 138

                 ....*..
gi 291395817 152 DGQTAIC 158
Cdd:PHA02817 139 IPKVPIC 145
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH