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Conserved domains on  [gi|1958749009|ref|XP_008758969|]
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complement component C6 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 292-514 3.28e-54

MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms transmembrane channels. These channels disrupt the phospholipid bilayer of target cells, leading to cell lysis and death. A number of proteins participate in the assembly of the MAC. Freshly activated C5b binds to C6 to form a C5b-6 complex, then to C7 forming the C5b-7 complex. The C5b-7 complex binds to C8, which is composed of three chains (alpha, beta, and gamma), thus forming the C5b-8 complex. C5b-8 subsequently binds to C9 and acts as a catalyst in the polymerization of C9. Active MAC has a subunit composition of C5b-C6-C7-C8-C9{n}. Perforin is a protein found in cytolytic T-cell and killer cells. In the presence of calcium, perforin polymerizes into transmembrane tubules and is capable of lysing, non-specifically, a variety of target cells. There are a number of regions of similarity in the sequences of complement components C6, C7, C8-alpha, C8-beta, C9 and perforin. The X-ray crystal structure of a MACPF domain reveals that it shares a common fold with bacterial cholesterol dependent cytolysins (pfam01289) such as perfringolysin O. Three key pieces of evidence suggests that MACPF domains and CDCs are homologous: Functional similarity (pore formation), conservation of three glycine residues at a hinge in both families and conservation of a complex core fold.


:

Pssm-ID: 460349  Cd Length: 211  Bit Score: 187.23  E-value: 3.28e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749009 292 NFQRNSGFKNAIEASHKKDSSFVRIHKVIKVLNFTMKTT-DLQLSDVFLKALIHLPLEYNFAL---YSRIFDDFGTHYFT 367
Cdd:pfam01823   2 SFSASSEFKKMSDKSKQKKKSLIISKSTCSLYQFTLKRSnKLQLSDEFLQALSDLPDNYDYAAkatYIQFFDKYGTHYIT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749009 368 SGSLGGKYDLLYQFSRQELQNSGLTEEETRNCVryetKKRFLFFTKTYKEDRCTTNRLSEKYKGSFLQGSEKSISLVQGG 447
Cdd:pfam01823  82 SVTLGGKIVYVLKLDKSQLEDLKLKGEDVKICL----SASAGASIGSVNLKGCSKNSSSTKEKKSFNQEIESSITLVIGG 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749009 448 RSqqaaalawekGSSGPEANVFSEWLESVKENPAVVDYELAPIIDLvrnIPCAVTKRNNLRKALQEY 514
Cdd:pfam01823 158 TP----------ESIDDDSKTYSDWAESVKDNPMPIDFELTPISEL---LKGVPLKKENLRKALEEY 211
FIMAC super family cl42952
factor I membrane attack complex;
862-934 4.43e-15

factor I membrane attack complex;


The actual alignment was detected with superfamily member smart00057:

Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 70.65  E-value: 4.43e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958749009  862 CGYDTCYDWEKCSAhtSNCVCLLPPQCPKdENQLHCVKMGSSMrgKTVNICTLGAVRCANRKVEILNPGRCLD 934
Cdd:smart00057   1 CAKGFCQLWQKCSA--STCVCKLPYECPK-AGTDVCVEDGRSE--KTLTYCKQGALRCLNQKYKFLHIGSCTA 68
FIMAC super family cl42952
factor I membrane attack complex;
768-839 1.49e-14

factor I membrane attack complex;


The actual alignment was detected with superfamily member smart00057:

Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 69.11  E-value: 1.49e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958749009  768 KSKGLCQPGQKQSGSECVCMSPEEdCSSYSEDLCIFDEGSsqYFTSSACKFLAEKCLNSnQFHFVHAGSCQE 839
Cdd:smart00057   1 CAKGFCQLWQKCSASTCVCKLPYE-CPKAGTDVCVEDGRS--EKTLTYCKQGALRCLNQ-KYKFLHIGSCTA 68
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 142-173 8.54e-10

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 54.52  E-value: 8.54e-10
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958749009 142 NKFLCDSGRCIPSKLECNGENDCGDNSDERNC 173
Cdd:cd00112     4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 644-700 5.93e-09

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: 52.85  E-value: 5.93e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749009 644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTGFKAVGYQYFRCLPDRTWRQGDVECQ 700
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
TSP1_spondin super family cl46269
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 28-78 3.07e-08

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


The actual alignment was detected with superfamily member pfam19028:

Pssm-ID: 480609  Cd Length: 52  Bit Score: 50.74  E-value: 3.07e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958749009  28 PWTHWSSCSKSCNSGTQSRQRQIVVNDYYRDNSCDQLctkQETRQCNVETC 78
Cdd:pfam19028   5 EWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPEL---LERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 568-612 6.27e-08

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 49.89  E-value: 6.27e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958749009  568 WGCWSSWSACNAA---YRRSRSRECNNPEPQRGGQRCEGKHWQEEDCT 612
Cdd:smart00209   1 WSEWSEWSPCSVTcggGVQTRTRSCCSPPPQNGGGPCTGEDVETRACN 48
PHA02831 super family cl31511
EEV host range protein; Provisional
 644-764 4.84e-07

EEV host range protein; Provisional


The actual alignment was detected with superfamily member PHA02831:

Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 52.30  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749009 644 CPQPPLPENAFVWNEKKLYSVGEEVEISC----LTGFKAVGYQYFRCLpDRTWRQGDVECQRTECLKPVVQDVLtISPFQ 719
Cdd:PHA02831   78 CKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYSIVGNETVKCI-NKQWVPKYPVCKLIRCKYPALQNGF-LNVFE 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958749009 720 SVYKIGESIELTCPRGFVVAGPSRYTCKGDS-WTPPIPNslsCEKD 764
Cdd:PHA02831  156 KKFYYGDIVNFKCKKGFILLGSSVSTCDINSiWYPGIPK---CVKD 198
TSP1_spondin super family cl46269
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 82-127 2.26e-04

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


The actual alignment was detected with superfamily member pfam19028:

Pssm-ID: 480609  Cd Length: 52  Bit Score: 39.57  E-value: 2.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958749009  82 CVLGDYGTWSDCD-PC-IRKQVKVRSVLRPSQFGGQPCTEPLVTfQPC 127
Cdd:pfam19028   1 CVVSEWSEWSECSvTCgGGVQTRTRTVIVEPQNGGRPCPELLER-RPC 47
 
Name Accession Description Interval E-value
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 292-514 3.28e-54

MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms transmembrane channels. These channels disrupt the phospholipid bilayer of target cells, leading to cell lysis and death. A number of proteins participate in the assembly of the MAC. Freshly activated C5b binds to C6 to form a C5b-6 complex, then to C7 forming the C5b-7 complex. The C5b-7 complex binds to C8, which is composed of three chains (alpha, beta, and gamma), thus forming the C5b-8 complex. C5b-8 subsequently binds to C9 and acts as a catalyst in the polymerization of C9. Active MAC has a subunit composition of C5b-C6-C7-C8-C9{n}. Perforin is a protein found in cytolytic T-cell and killer cells. In the presence of calcium, perforin polymerizes into transmembrane tubules and is capable of lysing, non-specifically, a variety of target cells. There are a number of regions of similarity in the sequences of complement components C6, C7, C8-alpha, C8-beta, C9 and perforin. The X-ray crystal structure of a MACPF domain reveals that it shares a common fold with bacterial cholesterol dependent cytolysins (pfam01289) such as perfringolysin O. Three key pieces of evidence suggests that MACPF domains and CDCs are homologous: Functional similarity (pore formation), conservation of three glycine residues at a hinge in both families and conservation of a complex core fold.


Pssm-ID: 460349  Cd Length: 211  Bit Score: 187.23  E-value: 3.28e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749009 292 NFQRNSGFKNAIEASHKKDSSFVRIHKVIKVLNFTMKTT-DLQLSDVFLKALIHLPLEYNFAL---YSRIFDDFGTHYFT 367
Cdd:pfam01823   2 SFSASSEFKKMSDKSKQKKKSLIISKSTCSLYQFTLKRSnKLQLSDEFLQALSDLPDNYDYAAkatYIQFFDKYGTHYIT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749009 368 SGSLGGKYDLLYQFSRQELQNSGLTEEETRNCVryetKKRFLFFTKTYKEDRCTTNRLSEKYKGSFLQGSEKSISLVQGG 447
Cdd:pfam01823  82 SVTLGGKIVYVLKLDKSQLEDLKLKGEDVKICL----SASAGASIGSVNLKGCSKNSSSTKEKKSFNQEIESSITLVIGG 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749009 448 RSqqaaalawekGSSGPEANVFSEWLESVKENPAVVDYELAPIIDLvrnIPCAVTKRNNLRKALQEY 514
Cdd:pfam01823 158 TP----------ESIDDDSKTYSDWAESVKDNPMPIDFELTPISEL---LKGVPLKKENLRKALEEY 211
MACPF smart00457
membrane-attack complex / perforin;
313-514 5.28e-50

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 174.93  E-value: 5.28e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749009  313 FVRIHKVIKVLNFTMKTTDLQLSDVFLKALIHLPLEYNFALYSRIFDDFGTHYFTSGSLGGKYDLLYQFSRQELQNSGLT 392
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749009  393 EEETRNCVRYETKkrflFFTKTYKEDRCTTNRLSEKYKGSFLqgSEKSISLVQGGRSQQAAALAWEKGSSGPEanvFSEW 472
Cdd:smart00457  81 SEDISKCLAGSSN----SFAGSVSAEHCLQSSSYIKYLSTSL--RRESHTQVLGGHVTVLCDLLRGPSSNSLD---FSDW 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958749009  473 LESVKENPAVVDYELAPIIDLVRNIPCAVTKRNNLRKALQEY 514
Cdd:smart00457 152 AESVPNEPVLIDVSLAPIYELLPPNPELSQKREALRQALRSY 193
FIMAC smart00057
factor I membrane attack complex;
862-934 4.43e-15

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 70.65  E-value: 4.43e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958749009  862 CGYDTCYDWEKCSAhtSNCVCLLPPQCPKdENQLHCVKMGSSMrgKTVNICTLGAVRCANRKVEILNPGRCLD 934
Cdd:smart00057   1 CAKGFCQLWQKCSA--STCVCKLPYECPK-AGTDVCVEDGRSE--KTLTYCKQGALRCLNQKYKFLHIGSCTA 68
FIMAC smart00057
factor I membrane attack complex;
768-839 1.49e-14

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 69.11  E-value: 1.49e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958749009  768 KSKGLCQPGQKQSGSECVCMSPEEdCSSYSEDLCIFDEGSsqYFTSSACKFLAEKCLNSnQFHFVHAGSCQE 839
Cdd:smart00057   1 CAKGFCQLWQKCSASTCVCKLPYE-CPKAGTDVCVEDGRS--EKTLTYCKQGALRCLNQ-KYKFLHIGSCTA 68
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 142-173 8.54e-10

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 54.52  E-value: 8.54e-10
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958749009 142 NKFLCDSGRCIPSKLECNGENDCGDNSDERNC 173
Cdd:cd00112     4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 644-700 5.93e-09

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: 52.85  E-value: 5.93e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749009 644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTGFKAVGYQYFRCLPDRTWRQGDVECQ 700
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
138-173 7.95e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.87  E-value: 7.95e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958749009 138 TDCK-NKFLCDSGRCIPSKLECNGENDCGDNSDERNC 173
Cdd:pfam00057   1 STCSpNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 28-78 3.07e-08

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 50.74  E-value: 3.07e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958749009  28 PWTHWSSCSKSCNSGTQSRQRQIVVNDYYRDNSCDQLctkQETRQCNVETC 78
Cdd:pfam19028   5 EWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPEL---LERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 568-612 6.27e-08

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 49.89  E-value: 6.27e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958749009  568 WGCWSSWSACNAA---YRRSRSRECNNPEPQRGGQRCEGKHWQEEDCT 612
Cdd:smart00209   1 WSEWSEWSPCSVTcggGVQTRTRSCCSPPPQNGGGPCTGEDVETRACN 48
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 142-170 8.85e-08

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 48.78  E-value: 8.85e-08
                           10        20
                   ....*....|....*....|....*....
gi 1958749009  142 NKFLCDSGRCIPSKLECNGENDCGDNSDE 170
Cdd:smart00192   5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Sushi pfam00084
Sushi repeat (SCR repeat);
644-699 9.28e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.42  E-value: 9.28e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749009 644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTGFKAVGYQYFRCLPDRTWRQGDVEC 699
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 644-699 1.26e-07

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: 49.06  E-value: 1.26e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749009  644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTGFKAVGYQYFRCLPDRTWRQGDVEC 699
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 26-79 1.49e-07

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 48.74  E-value: 1.49e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958749009   26 HYPWTHWSSCSKSCNSGTQSRQRQ-IVVNDYYRDNSCDQLctKQETRQCNVETCP 79
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRScCSPPPQNGGGPCTGE--DVETRACNEQPCP 53
PHA02831 PHA02831
EEV host range protein; Provisional
 644-764 4.84e-07

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 52.30  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749009 644 CPQPPLPENAFVWNEKKLYSVGEEVEISC----LTGFKAVGYQYFRCLpDRTWRQGDVECQRTECLKPVVQDVLtISPFQ 719
Cdd:PHA02831   78 CKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYSIVGNETVKCI-NKQWVPKYPVCKLIRCKYPALQNGF-LNVFE 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958749009 720 SVYKIGESIELTCPRGFVVAGPSRYTCKGDS-WTPPIPNslsCEKD 764
Cdd:PHA02831  156 KKFYYGDIVNFKCKKGFILLGSSVSTCDINSiWYPGIPK---CVKD 198
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 644-756 8.19e-07

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 51.58  E-value: 8.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749009 644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTGFKAVGYQYFRClPDRTWRQGDVeCQRTECLKPVVQDVLTISPFQSVYK 723
Cdd:PHA02927  148 CQSPPSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLC-SGGEWSDPPT-CQIVKCPHPTISNGYLSSGFKRSYS 225

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958749009 724 IGESIELTCPRGFVVAGPSRYTCK-GDSWTPPIP 756
Cdd:PHA02927  226 YNDNVDFKCKYGYKLSGSSSSTCSpGNTWQPELP 259
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 704-756 4.41e-05

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: 41.74  E-value: 4.41e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958749009  704 CLKPVVQDVLTISPFQSVYKIGESIELTCPRGFVVAGPSRYTCKGD-SWTPPIP 756
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENgTWSPPPP 54
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 704-756 4.96e-05

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: 41.68  E-value: 4.96e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958749009 704 CLKPVVQDVLTISPFQSVYKIGESIELTCPRGFVVAGPSRYTCKGDS-WTPPIP 756
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPPP 54
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 28-80 1.96e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 44.95  E-value: 1.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958749009  28 PWTHWSSCSKSCNSGTQSRQRQIVvndyyrdnscDQLCTKQETRQCNVETCPI 80
Cdd:PTZ00441  242 PWDEWTPCSVTCGKGTHSRSRPIL----------HEGCTTHMVEECEEEECPV 284
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 82-127 2.26e-04

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 39.57  E-value: 2.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958749009  82 CVLGDYGTWSDCD-PC-IRKQVKVRSVLRPSQFGGQPCTEPLVTfQPC 127
Cdd:pfam19028   1 CVVSEWSEWSECSvTCgGGVQTRTRTVIVEPQNGGRPCPELLER-RPC 47
Sushi pfam00084
Sushi repeat (SCR repeat);
715-756 5.91e-04

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 38.63  E-value: 5.91e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958749009 715 ISPFQSVYKIGESIELTCPRGFVVAGPSRYTCKGD-SWTPPIP 756
Cdd:pfam00084  12 VSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDgTWSPPFP 54
 
Name Accession Description Interval E-value
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 292-514 3.28e-54

MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms transmembrane channels. These channels disrupt the phospholipid bilayer of target cells, leading to cell lysis and death. A number of proteins participate in the assembly of the MAC. Freshly activated C5b binds to C6 to form a C5b-6 complex, then to C7 forming the C5b-7 complex. The C5b-7 complex binds to C8, which is composed of three chains (alpha, beta, and gamma), thus forming the C5b-8 complex. C5b-8 subsequently binds to C9 and acts as a catalyst in the polymerization of C9. Active MAC has a subunit composition of C5b-C6-C7-C8-C9{n}. Perforin is a protein found in cytolytic T-cell and killer cells. In the presence of calcium, perforin polymerizes into transmembrane tubules and is capable of lysing, non-specifically, a variety of target cells. There are a number of regions of similarity in the sequences of complement components C6, C7, C8-alpha, C8-beta, C9 and perforin. The X-ray crystal structure of a MACPF domain reveals that it shares a common fold with bacterial cholesterol dependent cytolysins (pfam01289) such as perfringolysin O. Three key pieces of evidence suggests that MACPF domains and CDCs are homologous: Functional similarity (pore formation), conservation of three glycine residues at a hinge in both families and conservation of a complex core fold.


Pssm-ID: 460349  Cd Length: 211  Bit Score: 187.23  E-value: 3.28e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749009 292 NFQRNSGFKNAIEASHKKDSSFVRIHKVIKVLNFTMKTT-DLQLSDVFLKALIHLPLEYNFAL---YSRIFDDFGTHYFT 367
Cdd:pfam01823   2 SFSASSEFKKMSDKSKQKKKSLIISKSTCSLYQFTLKRSnKLQLSDEFLQALSDLPDNYDYAAkatYIQFFDKYGTHYIT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749009 368 SGSLGGKYDLLYQFSRQELQNSGLTEEETRNCVryetKKRFLFFTKTYKEDRCTTNRLSEKYKGSFLQGSEKSISLVQGG 447
Cdd:pfam01823  82 SVTLGGKIVYVLKLDKSQLEDLKLKGEDVKICL----SASAGASIGSVNLKGCSKNSSSTKEKKSFNQEIESSITLVIGG 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749009 448 RSqqaaalawekGSSGPEANVFSEWLESVKENPAVVDYELAPIIDLvrnIPCAVTKRNNLRKALQEY 514
Cdd:pfam01823 158 TP----------ESIDDDSKTYSDWAESVKDNPMPIDFELTPISEL---LKGVPLKKENLRKALEEY 211
MACPF smart00457
membrane-attack complex / perforin;
313-514 5.28e-50

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 174.93  E-value: 5.28e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749009  313 FVRIHKVIKVLNFTMKTTDLQLSDVFLKALIHLPLEYNFALYSRIFDDFGTHYFTSGSLGGKYDLLYQFSRQELQNSGLT 392
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749009  393 EEETRNCVRYETKkrflFFTKTYKEDRCTTNRLSEKYKGSFLqgSEKSISLVQGGRSQQAAALAWEKGSSGPEanvFSEW 472
Cdd:smart00457  81 SEDISKCLAGSSN----SFAGSVSAEHCLQSSSYIKYLSTSL--RRESHTQVLGGHVTVLCDLLRGPSSNSLD---FSDW 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958749009  473 LESVKENPAVVDYELAPIIDLVRNIPCAVTKRNNLRKALQEY 514
Cdd:smart00457 152 AESVPNEPVLIDVSLAPIYELLPPNPELSQKREALRQALRSY 193
FIMAC smart00057
factor I membrane attack complex;
862-934 4.43e-15

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 70.65  E-value: 4.43e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958749009  862 CGYDTCYDWEKCSAhtSNCVCLLPPQCPKdENQLHCVKMGSSMrgKTVNICTLGAVRCANRKVEILNPGRCLD 934
Cdd:smart00057   1 CAKGFCQLWQKCSA--STCVCKLPYECPK-AGTDVCVEDGRSE--KTLTYCKQGALRCLNQKYKFLHIGSCTA 68
FIMAC smart00057
factor I membrane attack complex;
768-839 1.49e-14

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 69.11  E-value: 1.49e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958749009  768 KSKGLCQPGQKQSGSECVCMSPEEdCSSYSEDLCIFDEGSsqYFTSSACKFLAEKCLNSnQFHFVHAGSCQE 839
Cdd:smart00057   1 CAKGFCQLWQKCSASTCVCKLPYE-CPKAGTDVCVEDGRS--EKTLTYCKQGALRCLNQ-KYKFLHIGSCTA 68
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 142-173 8.54e-10

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 54.52  E-value: 8.54e-10
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958749009 142 NKFLCDSGRCIPSKLECNGENDCGDNSDERNC 173
Cdd:cd00112     4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 644-700 5.93e-09

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: 52.85  E-value: 5.93e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749009 644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTGFKAVGYQYFRCLPDRTWRQGDVECQ 700
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
138-173 7.95e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.87  E-value: 7.95e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958749009 138 TDCK-NKFLCDSGRCIPSKLECNGENDCGDNSDERNC 173
Cdd:pfam00057   1 STCSpNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 28-78 3.07e-08

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 50.74  E-value: 3.07e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958749009  28 PWTHWSSCSKSCNSGTQSRQRQIVVNDYYRDNSCDQLctkQETRQCNVETC 78
Cdd:pfam19028   5 EWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPEL---LERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 568-612 6.27e-08

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 49.89  E-value: 6.27e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958749009  568 WGCWSSWSACNAA---YRRSRSRECNNPEPQRGGQRCEGKHWQEEDCT 612
Cdd:smart00209   1 WSEWSEWSPCSVTcggGVQTRTRSCCSPPPQNGGGPCTGEDVETRACN 48
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 142-170 8.85e-08

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 48.78  E-value: 8.85e-08
                           10        20
                   ....*....|....*....|....*....
gi 1958749009  142 NKFLCDSGRCIPSKLECNGENDCGDNSDE 170
Cdd:smart00192   5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Sushi pfam00084
Sushi repeat (SCR repeat);
644-699 9.28e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.42  E-value: 9.28e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749009 644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTGFKAVGYQYFRCLPDRTWRQGDVEC 699
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 644-699 1.26e-07

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: 49.06  E-value: 1.26e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749009  644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTGFKAVGYQYFRCLPDRTWRQGDVEC 699
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 26-79 1.49e-07

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 48.74  E-value: 1.49e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958749009   26 HYPWTHWSSCSKSCNSGTQSRQRQ-IVVNDYYRDNSCDQLctKQETRQCNVETCP 79
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRScCSPPPQNGGGPCTGE--DVETRACNEQPCP 53
PHA02831 PHA02831
EEV host range protein; Provisional
 644-764 4.84e-07

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 52.30  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749009 644 CPQPPLPENAFVWNEKKLYSVGEEVEISC----LTGFKAVGYQYFRCLpDRTWRQGDVECQRTECLKPVVQDVLtISPFQ 719
Cdd:PHA02831   78 CKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYSIVGNETVKCI-NKQWVPKYPVCKLIRCKYPALQNGF-LNVFE 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958749009 720 SVYKIGESIELTCPRGFVVAGPSRYTCKGDS-WTPPIPNslsCEKD 764
Cdd:PHA02831  156 KKFYYGDIVNFKCKKGFILLGSSVSTCDINSiWYPGIPK---CVKD 198
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 644-756 8.19e-07

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 51.58  E-value: 8.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749009 644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTGFKAVGYQYFRClPDRTWRQGDVeCQRTECLKPVVQDVLTISPFQSVYK 723
Cdd:PHA02927  148 CQSPPSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLC-SGGEWSDPPT-CQIVKCPHPTISNGYLSSGFKRSYS 225

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958749009 724 IGESIELTCPRGFVVAGPSRYTCK-GDSWTPPIP 756
Cdd:PHA02927  226 YNDNVDFKCKYGYKLSGSSSSTCSpGNTWQPELP 259
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 659-756 3.38e-05

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 47.00  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749009 659 KKLYSVGEEVEISCLTGFKAVGYQYFRCLPDrTWRQGDvECQRtECLKPVVQDVLTISpfqSVYKIGESIELTCPRGFVV 738
Cdd:PHA02954  144 KEKYSFGEHITINCDVGYEVIGASYISCTAN-SWNVIP-SCQQ-KCDIPSLSNGLISG---STFSIGGVIHLSCKSGFTL 217

                          90
                  ....*....|....*...
gi 1958749009 739 AGPSRYTCKGDSWTPPIP 756
Cdd:PHA02954  218 TGSPSSTCIDGKWNPVLP 235
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 704-756 4.41e-05

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: 41.74  E-value: 4.41e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958749009  704 CLKPVVQDVLTISPFQSVYKIGESIELTCPRGFVVAGPSRYTCKGD-SWTPPIP 756
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENgTWSPPPP 54
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 704-756 4.96e-05

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: 41.68  E-value: 4.96e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958749009 704 CLKPVVQDVLTISPFQSVYKIGESIELTCPRGFVVAGPSRYTCKGDS-WTPPIP 756
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPPP 54
TSP_1 pfam00090
Thrombospondin type 1 domain;
28-78 5.74e-05

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 41.25  E-value: 5.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958749009  28 PWTHWSSCSKSCNSGTQSRQRQIVVNdyyrdNSCDQLCT--KQETRQCNVETC 78
Cdd:pfam00090   2 PWSPWSPCSVTCGKGIQVRQRTCKSP-----FPGGEPCTgdDIETQACKMDKC 49
PHA02817 PHA02817
EEV Host range protein; Provisional
 644-756 9.29e-05

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 44.93  E-value: 9.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749009 644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTG-----FKAVGYQYFRCLPDRTWRQGDVECQRTECLKPVVQD-VLTISP 717
Cdd:PHA02817   24 CCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRCRFPALQNgFVNGIP 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958749009 718 FQSVYKIGESIELTCPRGFVVAGPSRYTCK-GDSWTPPIP 756
Cdd:PHA02817  104 DSKKFYYESEVSFSCKPGFVLIGTKYSVCGiNSSWIPKVP 143
PHA02639 PHA02639
EEV host range protein; Provisional
 644-761 1.79e-04

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 44.65  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749009 644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTGFKAVGYQYFRCLPDRT---WRQGDVECQRTECLKPVVQDVLTISPFQS 720
Cdd:PHA02639   22 CDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCIKDKNnaiWSNKAPFCMLKECNDPPSIINGKIYNKRE 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958749009 721 VYKIGESIELTCPR----GFVVAGPSRYTCKGD-SWT--PPIPNSLSC 761
Cdd:PHA02639  102 MYKVGDEIYYVCNEhkgvQYSLVGNEKITCIQDkSWKpdPPICKMINC 149
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 28-80 1.96e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 44.95  E-value: 1.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958749009  28 PWTHWSSCSKSCNSGTQSRQRQIVvndyyrdnscDQLCTKQETRQCNVETCPI 80
Cdd:PTZ00441  242 PWDEWTPCSVTCGKGTHSRSRPIL----------HEGCTTHMVEECEEEECPV 284
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 82-127 2.26e-04

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 39.57  E-value: 2.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958749009  82 CVLGDYGTWSDCD-PC-IRKQVKVRSVLRPSQFGGQPCTEPLVTfQPC 127
Cdd:pfam19028   1 CVVSEWSEWSECSvTCgGGVQTRTRTVIVEPQNGGRPCPELLER-RPC 47
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 32-78 3.05e-04

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 39.36  E-value: 3.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958749009  32 WSSCSKSCNSGTQSRQ---RQIVVNDYYRDNSCDQLCTKQETRQCNVETC 78
Cdd:pfam19030   6 WGECSVTCGGGVQTRLvqcVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
Sushi pfam00084
Sushi repeat (SCR repeat);
715-756 5.91e-04

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 38.63  E-value: 5.91e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958749009 715 ISPFQSVYKIGESIELTCPRGFVVAGPSRYTCKGD-SWTPPIP 756
Cdd:pfam00084  12 VSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDgTWSPPFP 54
TSP_1 pfam00090
Thrombospondin type 1 domain;
85-128 4.68e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 35.86  E-value: 4.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958749009  85 GDYGTWSDCD-PCIrKQVKVRSVLRPSQF-GGQPCTEPLVTFQPCV 128
Cdd:pfam00090   1 SPWSPWSPCSvTCG-KGIQVRQRTCKSPFpGGEPCTGDDIETQACK 45
 
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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