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Conserved domains on  [gi|28570180|ref|NP_788263|]
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complement component C6 precursor [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 8.66e-50

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: 307781  Cd Length: 207  Bit Score: 176.42  E-value: 8.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28570180   292 NFQRNSGFKNAIEASHKKDSSFVRIHKVIKVLNFTMKTT-DLQLSDVFLKALIHLPLEYNFAL---YSRIFDDFGTHYFT 367
Cdd:pfam01823   2 SFSASSEFKKLSDKLKQKKNSFIISKSYCSLYQFTLSRSnKLKLSDDFLKALNALPDNYDSANedtYIQFFDKYGTHVIT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28570180   368 SGSLGGKYDLLYQFSRQELQNSGLTEEETrncvryeTKKRFLFFTKTYKEDRCTTNRLSEKYKGSFLQGSEKSISLVQGG 447
Cdd:pfam01823  82 SVTLGGKIVYILKLDKSELEKLKLKGSDC-------LSASAGASIGSVSVKGCKKNSSNTKEKKSSSQEIESSITIVLGG 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28570180   448 RSqqaaalawekGSSGPEANVFSEWLESVKENPAVVDYELAPIIDLVRNIPcavtKRNNLRKALQEY 514
Cdd:pfam01823 155 TP----------PSNDDDPETYSKWAESVKDNPMPIKFELLPISELLKEVP----KKENLKKALEEY 207
FIMAC super family cl20168
factor I membrane attack complex;
862-934 3.11e-14

factor I membrane attack complex;


The actual alignment was detected with superfamily member smart00057:

Pssm-ID: 214493  Cd Length: 68  Bit Score: 70.65  E-value: 3.11e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28570180    862 CGYDTCYDWEKCSAhtSNCVCLLPPQCPKdENQLHCVKMGSSMrgKTVNICTLGAVRCANRKVEILNPGRCLD 934
Cdd:smart00057   1 CAKGFCQLWQKCSA--STCVCKLPYECPK-AGTDVCVEDGRSE--KTLTYCKQGALRCLNQKYKFLHIGSCTA 68
FIMAC super family cl20168
factor I membrane attack complex;
768-839 1.02e-13

factor I membrane attack complex;


The actual alignment was detected with superfamily member smart00057:

Pssm-ID: 214493  Cd Length: 68  Bit Score: 69.11  E-value: 1.02e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28570180    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 1.55e-09

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: 56.06  E-value: 1.55e-09
                        10        20        30
                ....*....|....*....|....*....|..
gi 28570180 142 NKFLCDSGRCIPSKLKCNGENDCGDNSDERNC 173
Cdd:cd00112   4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
644-700 3.02e-08

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: 52.85  E-value: 3.02e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 28570180 644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTGFKAVGYQYFRCLPDRTWRQGDVECQ 700
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
568-612 3.09e-07

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


:

Pssm-ID: 214559  Cd Length: 53  Bit Score: 49.89  E-value: 3.09e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 28570180    568 WGCWSSWSACNAA---YRRSRSRECNNPEPQRGGQRCEGKHWQEEDCT 612
Cdd:smart00209   1 WSEWSEWSPCSVTcggGVQTRTRSCCSPPPQNGGGPCTGEDVETRACN 48
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
26-79 7.04e-07

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


:

Pssm-ID: 214559  Cd Length: 53  Bit Score: 48.74  E-value: 7.04e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28570180     26 HYPWTHWSSCSKSCNSGTQSRQRQ-IVVNDYYRDNSCDQLctKQETRQCNVETCP 79
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRScCSPPPQNGGGPCTGE--DVETRACNEQPCP 53
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
704-756 1.57e-04

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


:

Pssm-ID: 214478  Cd Length: 56  Bit Score: 41.74  E-value: 1.57e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 28570180    704 CLKPVVQDVLTISPFQSVYKIGESIELTCPRGFVVAGPSRYTCKGD-SWTPPIP 756
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENgTWSPPPP 54
 
Name Accession Description Interval E-value
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
292-514 8.66e-50

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: 307781  Cd Length: 207  Bit Score: 176.42  E-value: 8.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28570180   292 NFQRNSGFKNAIEASHKKDSSFVRIHKVIKVLNFTMKTT-DLQLSDVFLKALIHLPLEYNFAL---YSRIFDDFGTHYFT 367
Cdd:pfam01823   2 SFSASSEFKKLSDKLKQKKNSFIISKSYCSLYQFTLSRSnKLKLSDDFLKALNALPDNYDSANedtYIQFFDKYGTHVIT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28570180   368 SGSLGGKYDLLYQFSRQELQNSGLTEEETrncvryeTKKRFLFFTKTYKEDRCTTNRLSEKYKGSFLQGSEKSISLVQGG 447
Cdd:pfam01823  82 SVTLGGKIVYILKLDKSELEKLKLKGSDC-------LSASAGASIGSVSVKGCKKNSSNTKEKKSSSQEIESSITIVLGG 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28570180   448 RSqqaaalawekGSSGPEANVFSEWLESVKENPAVVDYELAPIIDLVRNIPcavtKRNNLRKALQEY 514
Cdd:pfam01823 155 TP----------PSNDDDPETYSKWAESVKDNPMPIKFELLPISELLKEVP----KKENLKKALEEY 207
MACPF smart00457
membrane-attack complex / perforin;
313-514 2.24e-49

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 174.93  E-value: 2.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28570180    313 FVRIHKVIKVLNFTMKTTDLQLSDVFLKALIHLPLEYNFALYSRIFDDFGTHYFTSGSLGGKYDLLYQFSRQELQNSGLT 392
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28570180    393 EEETRNCVRYETKkrflFFTKTYKEDRCTTNRLSEKYKGSFLqgSEKSISLVQGGRSQQAAALAWEKGSSGPEanvFSEW 472
Cdd:smart00457  81 SEDISKCLAGSSN----SFAGSVSAEHCLQSSSYIKYLSTSL--RRESHTQVLGGHVTVLCDLLRGPSSNSLD---FSDW 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 28570180    473 LESVKENPAVVDYELAPIIDLVRNIPCAVTKRNNLRKALQEY 514
Cdd:smart00457 152 AESVPNEPVLIDVSLAPIYELLPPNPELSQKREALRQALRSY 193
FIMAC smart00057
factor I membrane attack complex;
862-934 3.11e-14

factor I membrane attack complex;


Pssm-ID: 214493  Cd Length: 68  Bit Score: 70.65  E-value: 3.11e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28570180    862 CGYDTCYDWEKCSAhtSNCVCLLPPQCPKdENQLHCVKMGSSMrgKTVNICTLGAVRCANRKVEILNPGRCLD 934
Cdd:smart00057   1 CAKGFCQLWQKCSA--STCVCKLPYECPK-AGTDVCVEDGRSE--KTLTYCKQGALRCLNQKYKFLHIGSCTA 68
FIMAC smart00057
factor I membrane attack complex;
768-839 1.02e-13

factor I membrane attack complex;


Pssm-ID: 214493  Cd Length: 68  Bit Score: 69.11  E-value: 1.02e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28570180    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 1.55e-09

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: 56.06  E-value: 1.55e-09
                        10        20        30
                ....*....|....*....|....*....|..
gi 28570180 142 NKFLCDSGRCIPSKLKCNGENDCGDNSDERNC 173
Cdd:cd00112   4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
644-700 3.02e-08

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: 52.85  E-value: 3.02e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 28570180 644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTGFKAVGYQYFRCLPDRTWRQGDVECQ 700
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
138-173 3.42e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 278486  Cd Length: 37  Bit Score: 52.25  E-value: 3.42e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 28570180   138 TDCK-NKFLCDSGRCIPSKLKCNGENDCGDNSDERNC 173
Cdd:pfam00057   1 STCSpNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
142-170 1.44e-07

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: 50.32  E-value: 1.44e-07
                           10        20
                   ....*....|....*....|....*....
gi 28570180    142 NKFLCDSGRCIPSKLKCNGENDCGDNSDE 170
Cdd:smart00192   5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
568-612 3.09e-07

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


Pssm-ID: 214559  Cd Length: 53  Bit Score: 49.89  E-value: 3.09e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 28570180    568 WGCWSSWSACNAA---YRRSRSRECNNPEPQRGGQRCEGKHWQEEDCT 612
Cdd:smart00209   1 WSEWSEWSPCSVTcggGVQTRTRSCCSPPPQNGGGPCTGEDVETRACN 48
PHA02831 PHA02831
EEV host range protein; Provisional
644-764 4.61e-07

EEV host range protein; Provisional


Pssm-ID: 165176  Cd Length: 268  Bit Score: 52.30  E-value: 4.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28570180  644 CPQPPLPENAFVWNEKKLYSVGEEVEISC----LTGFKAVGYQYFRCLpDRTWRQGDVECQRTECLKPVVQDVLtISPFQ 719
Cdd:PHA02831  78 CKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYSIVGNETVKCI-NKQWVPKYPVCKLIRCKYPALQNGF-LNVFE 155
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 28570180  720 SVYKIGESIELTCPRGFVVAGPSRYTCKGDS-WTPPIPNslsCEKD 764
Cdd:PHA02831 156 KKFYYGDIVNFKCKKGFILLGSSVSTCDINSiWYPGIPK---CVKD 198
Sushi pfam00084
Sushi repeat (SCR repeat);
644-699 4.62e-07

Sushi repeat (SCR repeat);


Pssm-ID: 306569  Cd Length: 56  Bit Score: 49.43  E-value: 4.62e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 28570180   644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTGFKAVGYQYFRCLPDRTWRQGDVEC 699
Cdd:pfam00084   1 CPPPPDLPNGSVSATKNEYNYGAKVEYECDPGYRLVGNPVITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
644-699 5.83e-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  Cd Length: 56  Bit Score: 49.06  E-value: 5.83e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 28570180    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 7.04e-07

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


Pssm-ID: 214559  Cd Length: 53  Bit Score: 48.74  E-value: 7.04e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28570180     26 HYPWTHWSSCSKSCNSGTQSRQRQ-IVVNDYYRDNSCDQLctKQETRQCNVETCP 79
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRScCSPPPQNGGGPCTGE--DVETRACNEQPCP 53
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
704-756 1.57e-04

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478  Cd Length: 56  Bit Score: 41.74  E-value: 1.57e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 28570180    704 CLKPVVQDVLTISPFQSVYKIGESIELTCPRGFVVAGPSRYTCKGD-SWTPPIP 756
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENgTWSPPPP 54
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
28-80 1.67e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420  Cd Length: 576  Bit Score: 44.95  E-value: 1.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 28570180   28 PWTHWSSCSKSCNSGTQSRQRQIVvndyyrdnscDQLCTKQETRQCNVETCPI 80
Cdd:PTZ00441 242 PWDEWTPCSVTCGKGTHSRSRPIL----------HEGCTTHMVEECEEEECPV 284
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
704-756 1.70e-04

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: 41.68  E-value: 1.70e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 28570180 704 CLKPVVQDVLTISPFQSVYKIGESIELTCPRGFVVAGPSRYTCKGDS-WTPPIP 756
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPPP 54
TSP_1 pfam00090
Thrombospondin type 1 domain;
28-78 4.14e-04

Thrombospondin type 1 domain;


Pssm-ID: 306574  Cd Length: 49  Bit Score: 40.50  E-value: 4.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 28570180    28 PWTHWSSCSKSCNSGTQSRQRQIVVNdyyrdNSCDQLCT--KQETRQCNVETC 78
Cdd:pfam00090   2 PWSPWSPCSVTCGKGIRVRQRTCKSP-----FPGGEPCTgdAIETEACKMDKC 49
Sushi pfam00084
Sushi repeat (SCR repeat);
704-756 1.15e-03

Sushi repeat (SCR repeat);


Pssm-ID: 306569  Cd Length: 56  Bit Score: 39.41  E-value: 1.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 28570180   704 CLKPVVQDVLTISPFQSVYKIGESIELTCPRGFVVAGPSRYTCKGD-SWTPPIP 756
Cdd:pfam00084   1 CPPPPDLPNGSVSATKNEYNYGAKVEYECDPGYRLVGNPVITCQEDgTWSPPFP 54
 
Name Accession Description Interval E-value
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
292-514 8.66e-50

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: 307781  Cd Length: 207  Bit Score: 176.42  E-value: 8.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28570180   292 NFQRNSGFKNAIEASHKKDSSFVRIHKVIKVLNFTMKTT-DLQLSDVFLKALIHLPLEYNFAL---YSRIFDDFGTHYFT 367
Cdd:pfam01823   2 SFSASSEFKKLSDKLKQKKNSFIISKSYCSLYQFTLSRSnKLKLSDDFLKALNALPDNYDSANedtYIQFFDKYGTHVIT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28570180   368 SGSLGGKYDLLYQFSRQELQNSGLTEEETrncvryeTKKRFLFFTKTYKEDRCTTNRLSEKYKGSFLQGSEKSISLVQGG 447
Cdd:pfam01823  82 SVTLGGKIVYILKLDKSELEKLKLKGSDC-------LSASAGASIGSVSVKGCKKNSSNTKEKKSSSQEIESSITIVLGG 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28570180   448 RSqqaaalawekGSSGPEANVFSEWLESVKENPAVVDYELAPIIDLVRNIPcavtKRNNLRKALQEY 514
Cdd:pfam01823 155 TP----------PSNDDDPETYSKWAESVKDNPMPIKFELLPISELLKEVP----KKENLKKALEEY 207
MACPF smart00457
membrane-attack complex / perforin;
313-514 2.24e-49

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 174.93  E-value: 2.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28570180    313 FVRIHKVIKVLNFTMKTTDLQLSDVFLKALIHLPLEYNFALYSRIFDDFGTHYFTSGSLGGKYDLLYQFSRQELQNSGLT 392
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28570180    393 EEETRNCVRYETKkrflFFTKTYKEDRCTTNRLSEKYKGSFLqgSEKSISLVQGGRSQQAAALAWEKGSSGPEanvFSEW 472
Cdd:smart00457  81 SEDISKCLAGSSN----SFAGSVSAEHCLQSSSYIKYLSTSL--RRESHTQVLGGHVTVLCDLLRGPSSNSLD---FSDW 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 28570180    473 LESVKENPAVVDYELAPIIDLVRNIPCAVTKRNNLRKALQEY 514
Cdd:smart00457 152 AESVPNEPVLIDVSLAPIYELLPPNPELSQKREALRQALRSY 193
FIMAC smart00057
factor I membrane attack complex;
862-934 3.11e-14

factor I membrane attack complex;


Pssm-ID: 214493  Cd Length: 68  Bit Score: 70.65  E-value: 3.11e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28570180    862 CGYDTCYDWEKCSAhtSNCVCLLPPQCPKdENQLHCVKMGSSMrgKTVNICTLGAVRCANRKVEILNPGRCLD 934
Cdd:smart00057   1 CAKGFCQLWQKCSA--STCVCKLPYECPK-AGTDVCVEDGRSE--KTLTYCKQGALRCLNQKYKFLHIGSCTA 68
FIMAC smart00057
factor I membrane attack complex;
768-839 1.02e-13

factor I membrane attack complex;


Pssm-ID: 214493  Cd Length: 68  Bit Score: 69.11  E-value: 1.02e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28570180    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 1.55e-09

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: 56.06  E-value: 1.55e-09
                        10        20        30
                ....*....|....*....|....*....|..
gi 28570180 142 NKFLCDSGRCIPSKLKCNGENDCGDNSDERNC 173
Cdd:cd00112   4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
644-700 3.02e-08

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: 52.85  E-value: 3.02e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 28570180 644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTGFKAVGYQYFRCLPDRTWRQGDVECQ 700
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
138-173 3.42e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 278486  Cd Length: 37  Bit Score: 52.25  E-value: 3.42e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 28570180   138 TDCK-NKFLCDSGRCIPSKLKCNGENDCGDNSDERNC 173
Cdd:pfam00057   1 STCSpNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
142-170 1.44e-07

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: 50.32  E-value: 1.44e-07
                           10        20
                   ....*....|....*....|....*....
gi 28570180    142 NKFLCDSGRCIPSKLKCNGENDCGDNSDE 170
Cdd:smart00192   5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
568-612 3.09e-07

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


Pssm-ID: 214559  Cd Length: 53  Bit Score: 49.89  E-value: 3.09e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 28570180    568 WGCWSSWSACNAA---YRRSRSRECNNPEPQRGGQRCEGKHWQEEDCT 612
Cdd:smart00209   1 WSEWSEWSPCSVTcggGVQTRTRSCCSPPPQNGGGPCTGEDVETRACN 48
PHA02831 PHA02831
EEV host range protein; Provisional
644-764 4.61e-07

EEV host range protein; Provisional


Pssm-ID: 165176  Cd Length: 268  Bit Score: 52.30  E-value: 4.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28570180  644 CPQPPLPENAFVWNEKKLYSVGEEVEISC----LTGFKAVGYQYFRCLpDRTWRQGDVECQRTECLKPVVQDVLtISPFQ 719
Cdd:PHA02831  78 CKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYSIVGNETVKCI-NKQWVPKYPVCKLIRCKYPALQNGF-LNVFE 155
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 28570180  720 SVYKIGESIELTCPRGFVVAGPSRYTCKGDS-WTPPIPNslsCEKD 764
Cdd:PHA02831 156 KKFYYGDIVNFKCKKGFILLGSSVSTCDINSiWYPGIPK---CVKD 198
Sushi pfam00084
Sushi repeat (SCR repeat);
644-699 4.62e-07

Sushi repeat (SCR repeat);


Pssm-ID: 306569  Cd Length: 56  Bit Score: 49.43  E-value: 4.62e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 28570180   644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTGFKAVGYQYFRCLPDRTWRQGDVEC 699
Cdd:pfam00084   1 CPPPPDLPNGSVSATKNEYNYGAKVEYECDPGYRLVGNPVITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
644-699 5.83e-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  Cd Length: 56  Bit Score: 49.06  E-value: 5.83e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 28570180    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 7.04e-07

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


Pssm-ID: 214559  Cd Length: 53  Bit Score: 48.74  E-value: 7.04e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28570180     26 HYPWTHWSSCSKSCNSGTQSRQRQ-IVVNDYYRDNSCDQLctKQETRQCNVETCP 79
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRScCSPPPQNGGGPCTGE--DVETRACNEQPCP 53
PHA02927 PHA02927
secreted complement-binding protein; Provisional
644-756 7.65e-07

secreted complement-binding protein; Provisional


Pssm-ID: 222943  Cd Length: 263  Bit Score: 51.58  E-value: 7.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28570180  644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTGFKAVGYQYFRClPDRTWRQGDVeCQRTECLKPVVQDVLTISPFQSVYK 723
Cdd:PHA02927 148 CQSPPSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLC-SGGEWSDPPT-CQIVKCPHPTISNGYLSSGFKRSYS 225
                         90       100       110
                 ....*....|....*....|....*....|....
gi 28570180  724 IGESIELTCPRGFVVAGPSRYTCK-GDSWTPPIP 756
Cdd:PHA02927 226 YNDNVDFKCKYGYKLSGSSSSTCSpGNTWQPELP 259
PHA02639 PHA02639
EEV host range protein; Provisional
644-756 2.76e-06

EEV host range protein; Provisional


Pssm-ID: 165022  Cd Length: 295  Bit Score: 50.05  E-value: 2.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28570180  644 CPQPPLPENAFVWNEKKLYSVGEEVEISCL----TGFKAVGYQYFRCLPDRTWRQGDVECQRTECLKPVVQD-VLTISPF 718
Cdd:PHA02639  85 CNDPPSIINGKIYNKREMYKVGDEIYYVCNehkgVQYSLVGNEKITCIQDKSWKPDPPICKMINCRFPALQNgYINGIPS 164
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 28570180  719 QSVYKIGESIELTCPRGFVVAGPSRYTCK-GDSWTPPIP 756
Cdd:PHA02639 165 NKKFYYKTRVGFSCKSGFDLVGEKYSTCNiNATWFPSIP 203
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
659-756 3.06e-05

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263  Cd Length: 317  Bit Score: 47.00  E-value: 3.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28570180  659 KKLYSVGEEVEISCLTGFKAVGYQYFRCLPDrTWRQGDvECQRtECLKPVVQDVLTISpfqSVYKIGESIELTCPRGFVV 738
Cdd:PHA02954 144 KEKYSFGEHITINCDVGYEVIGASYISCTAN-SWNVIP-SCQQ-KCDIPSLSNGLISG---STFSIGGVIHLSCKSGFTL 217
                         90
                 ....*....|....*...
gi 28570180  739 AGPSRYTCKGDSWTPPIP 756
Cdd:PHA02954 218 TGSPSSTCIDGKWNPVLP 235
PHA02817 PHA02817
EEV Host range protein; Provisional
644-756 8.52e-05

EEV Host range protein; Provisional


Pssm-ID: 165167  Cd Length: 225  Bit Score: 44.93  E-value: 8.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28570180  644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTG-----FKAVGYQYFRCLPDRTWRQGDVECQRTECLKPVVQD-VLTISP 717
Cdd:PHA02817  24 CCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRCRFPALQNgFVNGIP 103
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 28570180  718 FQSVYKIGESIELTCPRGFVVAGPSRYTCK-GDSWTPPIP 756
Cdd:PHA02817 104 DSKKFYYESEVSFSCKPGFVLIGTKYSVCGiNSSWIPKVP 143
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
704-756 1.57e-04

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478  Cd Length: 56  Bit Score: 41.74  E-value: 1.57e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 28570180    704 CLKPVVQDVLTISPFQSVYKIGESIELTCPRGFVVAGPSRYTCKGD-SWTPPIP 756
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENgTWSPPPP 54
PHA02639 PHA02639
EEV host range protein; Provisional
644-761 1.61e-04

EEV host range protein; Provisional


Pssm-ID: 165022  Cd Length: 295  Bit Score: 44.65  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28570180  644 CPQPPLPENAFVWNEKKLYSVGEEVEISCLTGFKAVGYQYFRCLPDRT---WRQGDVECQRTECLKPVVQDVLTISPFQS 720
Cdd:PHA02639  22 CDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCIKDKNnaiWSNKAPFCMLKECNDPPSIINGKIYNKRE 101
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 28570180  721 VYKIGESIELTCPR----GFVVAGPSRYTCKGD-SWT--PPIPNSLSC 761
Cdd:PHA02639 102 MYKVGDEIYYVCNEhkgvQYSLVGNEKITCIQDkSWKpdPPICKMINC 149
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
28-80 1.67e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420  Cd Length: 576  Bit Score: 44.95  E-value: 1.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 28570180   28 PWTHWSSCSKSCNSGTQSRQRQIVvndyyrdnscDQLCTKQETRQCNVETCPI 80
Cdd:PTZ00441 242 PWDEWTPCSVTCGKGTHSRSRPIL----------HEGCTTHMVEECEEEECPV 284
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
704-756 1.70e-04

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: 41.68  E-value: 1.70e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 28570180 704 CLKPVVQDVLTISPFQSVYKIGESIELTCPRGFVVAGPSRYTCKGDS-WTPPIP 756
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPPP 54
TSP_1 pfam00090
Thrombospondin type 1 domain;
28-78 4.14e-04

Thrombospondin type 1 domain;


Pssm-ID: 306574  Cd Length: 49  Bit Score: 40.50  E-value: 4.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 28570180    28 PWTHWSSCSKSCNSGTQSRQRQIVVNdyyrdNSCDQLCT--KQETRQCNVETC 78
Cdd:pfam00090   2 PWSPWSPCSVTCGKGIRVRQRTCKSP-----FPGGEPCTgdAIETEACKMDKC 49
Sushi pfam00084
Sushi repeat (SCR repeat);
704-756 1.15e-03

Sushi repeat (SCR repeat);


Pssm-ID: 306569  Cd Length: 56  Bit Score: 39.41  E-value: 1.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 28570180   704 CLKPVVQDVLTISPFQSVYKIGESIELTCPRGFVVAGPSRYTCKGD-SWTPPIP 756
Cdd:pfam00084   1 CPPPPDLPNGSVSATKNEYNYGAKVEYECDPGYRLVGNPVITCQEDgTWSPPFP 54
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • 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, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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