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Conserved domains on  [gi|540344557|ref|NP_001269388|]
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complement C2 isoform 6 precursor [Homo sapiens]

Protein Classification

CCP domain-containing protein( domain architecture ID 13332024)

CCP domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 89-144 7.40e-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: 67.87  E-value: 7.40e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 540344557  89 CPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVC 144
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
 24-204 2.54e-14

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 71.61  E-value: 2.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344557  24 CPQNVNISGGTFTLShGWAPGSLLTYSCPQGLYpspasrLCKSSGQWQTPGATRSL----SKAVCKPVRCPAPVSFENGI 99
Cdd:PHA02927  86 CPSPRDIDNGQLDIG-GVDFGSSITYSCNSGYQ------LIGESKSYCELGSTGSMvwnpEAPICESVKCQSPPSISNGR 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344557 100 YTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRpNGMWDgETAVCDngAGHCPNPGISLGAVRTGFR--FGHGDKVRYRC 177
Cdd:PHA02927 159 HNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGFKrsYSYNDNVDFKC 234

                        170       180
                 ....*....|....*....|....*..
gi 540344557 178 SSNLVLTGSSERECQGNGVWSGTEPIC 204
Cdd:PHA02927 235 KYGYKLSGSSSSTCSPGNTWQPELPKC 261
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 253-284 6.88e-07

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


The actual alignment was detected with superfamily member cd01470:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 198  Bit Score: 49.21  E-value: 6.88e-07
                         10        20        30
                 ....*....|....*....|....*....|..
gi 540344557 253 LNLYLLLDCSQSVSENDFLIFKESASLMVDRV 284
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKI 32
 
Name Accession Description Interval E-value
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 89-144 7.40e-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: 67.87  E-value: 7.40e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 540344557  89 CPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVC 144
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 24-204 2.54e-14

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 71.61  E-value: 2.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344557  24 CPQNVNISGGTFTLShGWAPGSLLTYSCPQGLYpspasrLCKSSGQWQTPGATRSL----SKAVCKPVRCPAPVSFENGI 99
Cdd:PHA02927  86 CPSPRDIDNGQLDIG-GVDFGSSITYSCNSGYQ------LIGESKSYCELGSTGSMvwnpEAPICESVKCQSPPSISNGR 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344557 100 YTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRpNGMWDgETAVCDngAGHCPNPGISLGAVRTGFR--FGHGDKVRYRC 177
Cdd:PHA02927 159 HNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGFKrsYSYNDNVDFKC 234

                        170       180
                 ....*....|....*....|....*..
gi 540344557 178 SSNLVLTGSSERECQGNGVWSGTEPIC 204
Cdd:PHA02927 235 KYGYKLSGSSSSTCSPGNTWQPELPKC 261
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 89-144 1.13e-12

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: 61.77  E-value: 1.13e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 540344557    89 CPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVC 144
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
89-144 7.63e-11

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 56.74  E-value: 7.63e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 540344557   89 CPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVC 144
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 151-205 7.78e-11

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: 56.70  E-value: 7.78e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 540344557 151 CPNPGISLGAVRTGF--RFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPICR 205
Cdd:cd00033    1 CPPPPVPENGTVTGSkgSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 151-204 8.18e-10

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: 54.07  E-value: 8.18e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 540344557   151 CPNPG-ISLGAVRTGF-RFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPIC 204
Cdd:smart00032   1 CPPPPdIENGTVTSSSgTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 253-284 6.88e-07

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: 49.21  E-value: 6.88e-07
                         10        20        30
                 ....*....|....*....|....*....|..
gi 540344557 253 LNLYLLLDCSQSVSENDFLIFKESASLMVDRV 284
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKI 32
Sushi pfam00084
Sushi repeat (SCR repeat);
151-204 7.54e-07

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 45.57  E-value: 7.54e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 540344557  151 CPNPGISLGAVRTGFRFGH--GDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPIC 204
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYnyGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
 
Name Accession Description Interval E-value
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 89-144 7.40e-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: 67.87  E-value: 7.40e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 540344557  89 CPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVC 144
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 24-204 2.54e-14

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 71.61  E-value: 2.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344557  24 CPQNVNISGGTFTLShGWAPGSLLTYSCPQGLYpspasrLCKSSGQWQTPGATRSL----SKAVCKPVRCPAPVSFENGI 99
Cdd:PHA02927  86 CPSPRDIDNGQLDIG-GVDFGSSITYSCNSGYQ------LIGESKSYCELGSTGSMvwnpEAPICESVKCQSPPSISNGR 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344557 100 YTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRpNGMWDgETAVCDngAGHCPNPGISLGAVRTGFR--FGHGDKVRYRC 177
Cdd:PHA02927 159 HNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGFKrsYSYNDNVDFKC 234

                        170       180
                 ....*....|....*....|....*..
gi 540344557 178 SSNLVLTGSSERECQGNGVWSGTEPIC 204
Cdd:PHA02927 235 KYGYKLSGSSSSTCSPGNTWQPELPKC 261
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 89-144 1.13e-12

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: 61.77  E-value: 1.13e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 540344557    89 CPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVC 144
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
89-144 7.63e-11

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 56.74  E-value: 7.63e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 540344557   89 CPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVC 144
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 151-205 7.78e-11

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: 56.70  E-value: 7.78e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 540344557 151 CPNPGISLGAVRTGF--RFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPICR 205
Cdd:cd00033    1 CPPPPVPENGTVTGSkgSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 151-204 8.18e-10

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: 54.07  E-value: 8.18e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 540344557   151 CPNPG-ISLGAVRTGF-RFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPIC 204
Cdd:smart00032   1 CPPPPdIENGTVTSSSgTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 253-284 6.88e-07

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: 49.21  E-value: 6.88e-07
                         10        20        30
                 ....*....|....*....|....*....|..
gi 540344557 253 LNLYLLLDCSQSVSENDFLIFKESASLMVDRV 284
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKI 32
Sushi pfam00084
Sushi repeat (SCR repeat);
151-204 7.54e-07

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 45.57  E-value: 7.54e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 540344557  151 CPNPGISLGAVRTGFRFGH--GDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPIC 204
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYnyGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02817 PHA02817
EEV Host range protein; Provisional
 84-237 8.14e-07

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 49.17  E-value: 8.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344557  84 CKPVRCPAPVSFENGIYTPRLGSYPVGGNVSFECEDG-----FILRGSPVRQCRPNGMWDGETAVCDngAGHCPNPGISL 158
Cdd:PHA02817  19 CDLNKCCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCK--IIRCRFPALQN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344557 159 GAVR---TGFRFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPIC-RQPYSY------------DFPEDVAPALGT 222
Cdd:PHA02817  97 GFVNgipDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPICsRDNITYnkiyinkvniddNFFNQINNSNTY 176

                        170
                 ....*....|....*
gi 540344557 223 SFSHMLGATNPTQKT 237
Cdd:PHA02817 177 YFDKILQINNVNRYT 191
PHA02831 PHA02831
EEV host range protein; Provisional
 47-204 8.52e-07

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 49.61  E-value: 8.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344557  47 LTYSCPQGLypSPASRLCkSSGQWQTpgatrslsKAVCKPVR-CPAPVSFENGIYTPRLGSYPVGGNVSFECE----DGF 121
Cdd:PHA02831  46 LEYKCNNNF--DKVFVTC-NNGSWST--------KNMCIGKRnCKDPVTILNGYIKNKKDQYSFGDSVTYACKvnklEKY 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344557 122 ILRGSPVRQCrPNGMWDGETAVCDngAGHCPNPgislgAVRTGF------RFGHGDKVRYRCSSNLVLTGSSERECQGNG 195
Cdd:PHA02831 115 SIVGNETVKC-INKQWVPKYPVCK--LIRCKYP-----ALQNGFlnvfekKFYYGDIVNFKCKKGFILLGSSVSTCDINS 186


                 ....*....
gi 540344557 196 VWSGTEPIC 204
Cdd:PHA02831 187 IWYPGIPKC 195
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 84-205 3.97e-06

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 47.34  E-value: 3.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344557  84 CKPVRCPAPVSFENGIYTprLGSYPVGGNVSFECEDGFILRGSPVRQCRPNG----MWDGETAVCDNGAGHCPnPGISLG 159
Cdd:PHA02927  81 CIKRRCPSPRDIDNGQLD--IGGVDFGSSITYSCNSGYQLIGESKSYCELGStgsmVWNPEAPICESVKCQSP-PSISNG 157

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 540344557 160 AvRTGFR--FGHGDKVRYRCSSNLVLTGSSERECQGnGVWSgTEPICR 205
Cdd:PHA02927 158 R-HNGYEdfYTDGSVVTYSCNSGYSLIGNSGVLCSG-GEWS-DPPTCQ 202
PHA02817 PHA02817
EEV Host range protein; Provisional
 4-144 9.85e-06

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 46.09  E-value: 9.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344557   4 LMVLFCLLFLYPGL----ADSAPSC--PQNVNisGGTFTLSHGWAPGSLLTYSCPQGLYPSPASRL------CKSSGQWQ 71
Cdd:PHA02817   1 MKNIHMLLILLCNKvyslCDLNKCCypPSIKN--GYIYNKKTEYNIGSNVTFFCGNNTRGVRYTLVgekniiCEKDGKWN 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 540344557  72 TpgatrslSKAVCKPVRCPAPV---SFENGIytPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVC 144
Cdd:PHA02817  79 K-------EFPVCKIIRCRFPAlqnGFVNGI--PDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPIC 145
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 87-241 4.41e-05

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 44.69  E-value: 4.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344557  87 VRCP----APVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGmWDgetaVCDNGAGHCPNPGISLGAVr 162
Cdd:PHA02954 123 VTCPnaecQPLQLEHGSCQPVKEKYSFGEHITINCDVGYEVIGASYISCTANS-WN----VIPSCQQKCDIPSLSNGLI- 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344557 163 TGFRFGHGDKVRYRCSSNLVLTGSSERECQgNGVWSGTEPIC-RQPYSYDfPEDVAPALGTSFSHMLGATNPTQKTKESL 241
Cdd:PHA02954 197 SGSTFSIGGVIHLSCKSGFTLTGSPSSTCI-DGKWNPVLPICvRSNEEFD-PVDDGPDDETDLSKLSKDVVQYEQEIESL 274
PHA02639 PHA02639
EEV host range protein; Provisional
 85-205 7.66e-05

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 43.88  E-value: 7.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344557  85 KPVRCPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQC---RPNGMWDGETAVCDNGAGHCPnPGISLGAV 161
Cdd:PHA02639  18 KSIYCDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCikdKNNAIWSNKAPFCMLKECNDP-PSIINGKI 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 540344557 162 RTGFR-FGHGDKVRYRCSSN----LVLTGSSERECQGNGVWSGTEPICR 205
Cdd:PHA02639  97 YNKREmYKVGDEIYYVCNEHkgvqYSLVGNEKITCIQDKSWKPDPPICK 145
PHA02639 PHA02639
EEV host range protein; Provisional
 24-204 1.43e-03

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 39.65  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344557  24 CPQNVNISGGTFT-LSHGWAPGSLLTYSCPQGlYPSPASRL--C---KSSGQWqtpgatrSLSKAVCKPVRCPAPVSFEN 97
Cdd:PHA02639  22 CDKPDDISNGFITeLMEKYEIGKLIEYTCNTD-YALIGDRFrtCikdKNNAIW-------SNKAPFCMLKECNDPPSIIN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344557  98 G-IYTPRlGSYPVGGNVSFECED----GFILRGSPVRQCRPNGMWDGETAVCDngAGHCPNPGISLG---AVRTGFRFGH 169
Cdd:PHA02639  94 GkIYNKR-EMYKVGDEIYYVCNEhkgvQYSLVGNEKITCIQDKSWKPDPPICK--MINCRFPALQNGyinGIPSNKKFYY 170

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 540344557 170 GDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPIC 204
Cdd:PHA02639 171 KTRVGFSCKSGFDLVGEKYSTCNINATWFPSIPTC 205
 
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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