NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|169636415|ref|NP_000056|]
View 

complement component C6 precursor [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
MACPF smart00457
membrane-attack complex / perforin;
313-514 1.02e-59

membrane-attack complex / perforin;


:

Pssm-ID: 214671  Cd Length: 195  Bit Score: 202.28  E-value: 1.02e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415   313 FIRIHKVMKVLNFTTKAKDLHLSDVFLKALNHLPLEYNSALYSRIFDDFGTHYFTSGSLGGVYDLLYQFSSEELKNSGLT 392
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415   393 EEEAKHCVRIEtkkRVLFAKKTKVEHrCTTNKLSEKHEGSFiqGAEKSISLIRGGRSEYGAALAWEKGSSGLeekTFSEW 472
Cdd:smart00457  81 SEDISKCLAGS---SNSFAGSVSAEH-CLQSSSYIKYLSTS--LRRESHTQVLGGHVTVLCDLLRGPSSNSL---DFSDW 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 169636415   473 LESVKENPAVIDFELAPIVDLVRNIPCAVTKRNNLRKALQEY 514
Cdd:smart00457 152 AESVPNEPVLIDVSLAPIYELLPPNPELSQKREALRQALRSY 193
FIMAC smart00057
factor I membrane attack complex;
862-934 3.95e-20

factor I membrane attack complex;


:

Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 84.90  E-value: 3.95e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169636415   862 CGYDTCYDWEKCSASTskCVCLLPPQCFKGGnQLYCVKMGSStsEKTLNICEVGTIRCANRKMEILHPGKCLA 934
Cdd:smart00057   1 CAKGFCQLWQKCSAST--CVCKLPYECPKAG-TDVCVEDGRS--EKTLTYCKQGALRCLNQKYKFLHIGSCTA 68
FIMAC smart00057
factor I membrane attack complex;
768-839 2.83e-19

factor I membrane attack complex;


:

Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 82.59  E-value: 2.83e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169636415   768 KLKGHCQLGQKQSGSECICMSPEEdCSHHSEDLCVFDTDSndYFTSPACKFLAEKCLnNQQLHFLHIGSCQD 839
Cdd:smart00057   1 CAKGFCQLWQKCSASTCVCKLPYE-CPKAGTDVCVEDGRS--EKTLTYCKQGALRCL-NQKYKFLHIGSCTA 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
568-623 2.02e-10

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: 56.83  E-value: 2.02e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 169636415   568 WGCWSSWSTCDAT---YKRSRTRECNNPAPQRGGKRCEGEKRQEEDCtfsimenNGQPC 623
Cdd:smart00209   1 WSEWSEWSPCSVTcggGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC-------NEQPC 52
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
142-173 2.14e-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: 53.36  E-value: 2.14e-09
                         10        20        30
                 ....*....|....*....|....*....|..
gi 169636415 142 NKFRCDSGRCIARKLECNGENDCGDNSDERDC 173
Cdd:cd00112    4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
644-700 3.56e-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: 53.62  E-value: 3.56e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 169636415 644 CPQPVPPENGFIRNEKQLYLVGEDVEISCLTGFETVGYQYFRCLPDGTWRQGDVECQ 700
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
PHA02831 super family cl31511
EEV host range protein; Provisional
644-766 4.38e-09

EEV host range protein; Provisional


The actual alignment was detected with superfamily member PHA02831:

Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 58.47  E-value: 4.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415 644 CPQPVPPENGFIRNEKQLYLVGEDVEISC----LTGFETVGYQYFRCLpDGTWRQGDVECQRTECIKPVVQEVLtITPFQ 719
Cdd:PHA02831  78 CKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYSIVGNETVKCI-NKQWVPKYPVCKLIRCKYPALQNGF-LNVFE 155
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 169636415 720 RLYRIGESIELTCPKGFVVAGPSRYTCQGNS-WTPPISNsltCEKDTL 766
Cdd:PHA02831 156 KKFYYGDIVNFKCKKGFILLGSSVSTCDINSiWYPGIPK---CVKDKV 200
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
26-79 1.31e-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: 49.12  E-value: 1.31e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 169636415    26 HYAWTQWTSCSKTCNSGTQSRHRQIVVdkyYQENFCEQICSKQ--ETRECNWQRCP 79
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCS---PPPQNGGGPCTGEdvETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
85-133 7.48e-05

Thrombospondin type 1 domain;


:

Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 40.86  E-value: 7.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 169636415   85 GDFGPWSDCDPCIEKQSKVRSVLRPSQF-GGQPCTAPLVAFQPCiPSKLC 133
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFpGGEPCTGDDIETQAC-KMDKC 49
 
Name Accession Description Interval E-value
MACPF smart00457
membrane-attack complex / perforin;
313-514 1.02e-59

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 202.28  E-value: 1.02e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415   313 FIRIHKVMKVLNFTTKAKDLHLSDVFLKALNHLPLEYNSALYSRIFDDFGTHYFTSGSLGGVYDLLYQFSSEELKNSGLT 392
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415   393 EEEAKHCVRIEtkkRVLFAKKTKVEHrCTTNKLSEKHEGSFiqGAEKSISLIRGGRSEYGAALAWEKGSSGLeekTFSEW 472
Cdd:smart00457  81 SEDISKCLAGS---SNSFAGSVSAEH-CLQSSSYIKYLSTS--LRRESHTQVLGGHVTVLCDLLRGPSSNSL---DFSDW 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 169636415   473 LESVKENPAVIDFELAPIVDLVRNIPCAVTKRNNLRKALQEY 514
Cdd:smart00457 152 AESVPNEPVLIDVSLAPIYELLPPNPELSQKREALRQALRSY 193
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
294-514 2.25e-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: 188.00  E-value: 2.25e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415  294 NHNSAFKQAIQASHKKDSSFIRIHKVMKVLNFT-TKAKDLHLSDVFLKALNHLPLEYNSAL---YSRIFDDFGTHYFTSG 369
Cdd:pfam01823   4 SASSEFKKMSDKSKQKKKSLIISKSTCSLYQFTlKRSNKLQLSDEFLQALSDLPDNYDYAAkatYIQFFDKYGTHYITSV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415  370 SLGGVYDLLYQFSSEELKNSGLTEEEAKHCVRIEtkkrVLFAKKTKVEHRCTTNKLSEKHEGSFIQGAEKSISLIRGGRS 449
Cdd:pfam01823  84 TLGGKIVYVLKLDKSQLEDLKLKGEDVKICLSAS----AGASIGSVNLKGCSKNSSSTKEKKSFNQEIESSITLVIGGTP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169636415  450 EYGAAlawekgssglEEKTFSEWLESVKENPAVIDFELAPIVDLvrnIPCAVTKRNNLRKALQEY 514
Cdd:pfam01823 160 ESIDD----------DSKTYSDWAESVKDNPMPIDFELTPISEL---LKGVPLKKENLRKALEEY 211
FIMAC smart00057
factor I membrane attack complex;
862-934 3.95e-20

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 84.90  E-value: 3.95e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169636415   862 CGYDTCYDWEKCSASTskCVCLLPPQCFKGGnQLYCVKMGSStsEKTLNICEVGTIRCANRKMEILHPGKCLA 934
Cdd:smart00057   1 CAKGFCQLWQKCSAST--CVCKLPYECPKAG-TDVCVEDGRS--EKTLTYCKQGALRCLNQKYKFLHIGSCTA 68
FIMAC smart00057
factor I membrane attack complex;
768-839 2.83e-19

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 82.59  E-value: 2.83e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169636415   768 KLKGHCQLGQKQSGSECICMSPEEdCSHHSEDLCVFDTDSndYFTSPACKFLAEKCLnNQQLHFLHIGSCQD 839
Cdd:smart00057   1 CAKGFCQLWQKCSASTCVCKLPYE-CPKAGTDVCVEDGRS--EKTLTYCKQGALRCL-NQKYKFLHIGSCTA 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
568-623 2.02e-10

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: 56.83  E-value: 2.02e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 169636415   568 WGCWSSWSTCDAT---YKRSRTRECNNPAPQRGGKRCEGEKRQEEDCtfsimenNGQPC 623
Cdd:smart00209   1 WSEWSEWSPCSVTcggGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC-------NEQPC 52
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
142-173 2.14e-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: 53.36  E-value: 2.14e-09
                         10        20        30
                 ....*....|....*....|....*....|..
gi 169636415 142 NKFRCDSGRCIARKLECNGENDCGDNSDERDC 173
Cdd:cd00112    4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
644-700 3.56e-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: 53.62  E-value: 3.56e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 169636415 644 CPQPVPPENGFIRNEKQLYLVGEDVEISCLTGFETVGYQYFRCLPDGTWRQGDVECQ 700
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
142-173 3.74e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 52.64  E-value: 3.74e-09
                          10        20        30
                  ....*....|....*....|....*....|..
gi 169636415  142 NKFRCDSGRCIARKLECNGENDCGDNSDERDC 173
Cdd:pfam00057   6 NEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
PHA02831 PHA02831
EEV host range protein; Provisional
644-766 4.38e-09

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 58.47  E-value: 4.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415 644 CPQPVPPENGFIRNEKQLYLVGEDVEISC----LTGFETVGYQYFRCLpDGTWRQGDVECQRTECIKPVVQEVLtITPFQ 719
Cdd:PHA02831  78 CKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYSIVGNETVKCI-NKQWVPKYPVCKLIRCKYPALQNGF-LNVFE 155
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 169636415 720 RLYRIGESIELTCPKGFVVAGPSRYTCQGNS-WTPPISNsltCEKDTL 766
Cdd:PHA02831 156 KKFYYGDIVNFKCKKGFILLGSSVSTCDINSiWYPGIPK---CVKDKV 200
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
644-699 2.73e-08

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: 50.99  E-value: 2.73e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 169636415   644 CPQPVPPENGFIRNEKQLYLVGEDVEISCLTGFETVGYQYFRCLPDGTWRQGDVEC 699
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
142-170 7.50e-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: 49.17  E-value: 7.50e-08
                           10        20
                   ....*....|....*....|....*....
gi 169636415   142 NKFRCDSGRCIARKLECNGENDCGDNSDE 170
Cdd:smart00192   5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Sushi pfam00084
Sushi repeat (SCR repeat);
644-699 7.85e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.81  E-value: 7.85e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 169636415  644 CPQPVPPENGFIRNEKQLYLVGEDVEISCLTGFETVGYQYFRCLPDGTWRQGDVEC 699
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
26-79 1.31e-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: 49.12  E-value: 1.31e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 169636415    26 HYAWTQWTSCSKTCNSGTQSRHRQIVVdkyYQENFCEQICSKQ--ETRECNWQRCP 79
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCS---PPPQNGGGPCTGEdvETRACNEQPCP 53
PHA02927 PHA02927
secreted complement-binding protein; Provisional
644-755 1.55e-07

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 53.89  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415 644 CPQPVPPENGFIRNEKQLYLVGEDVEISCLTGFETVGYQYFRClPDGTWRQGDVeCQRTECIKPVVQEVLTITPFQRLYR 723
Cdd:PHA02927 148 CQSPPSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLC-SGGEWSDPPT-CQIVKCPHPTISNGYLSSGFKRSYS 225
                         90       100       110
                 ....*....|....*....|....*....|...
gi 169636415 724 IGESIELTCPKGFVVAGPSRYTCQ-GNSWTPPI 755
Cdd:PHA02927 226 YNDNVDFKCKYGYKLSGSSSSTCSpGNTWQPEL 258
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
28-78 7.36e-07

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: 46.89  E-value: 7.36e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 169636415   28 AWTQWTSCSKTCNSGTQSRHRQIVVdkyyQENFCEQIC-SKQETRECNWQRC 78
Cdd:pfam19028   5 EWSEWSECSVTCGGGVQTRTRTVIV----EPQNGGRPCpELLERRPCNLPPC 52
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
704-755 1.42e-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: 43.28  E-value: 1.42e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 169636415   704 CIKPVVQEVLTITPFQRLYRIGESIELTCPKGFVVAGPSRYTCQGN-SWTPPI 755
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENgTWSPPP 53
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
704-762 1.60e-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: 43.22  E-value: 1.60e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415 704 CIKPVVQEVLTITPFQRLYRIGESIELTCPKGFVVAGPSRYTCQGNS-WTPPIsnsLTCE 762
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPP---PTCE 57
TSP_1 pfam00090
Thrombospondin type 1 domain;
85-133 7.48e-05

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 40.86  E-value: 7.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 169636415   85 GDFGPWSDCDPCIEKQSKVRSVLRPSQF-GGQPCTAPLVAFQPCiPSKLC 133
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFpGGEPCTGDDIETQAC-KMDKC 49
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
29-80 1.51e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 45.34  E-value: 1.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 169636415  29 WTQWTSCSKTCNSGTQSRHRQIVVDKyyqenfceqiCSKQETRECNWQRCPI 80
Cdd:PTZ00441 243 WDEWTPCSVTCGKGTHSRSRPILHEG----------CTTHMVEECEEEECPV 284
Sushi pfam00084
Sushi repeat (SCR repeat);
722-754 8.93e-04

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 38.25  E-value: 8.93e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 169636415  722 YRIGESIELTCPKGFVVAGPSRYTCQGN-SWTPP 754
Cdd:pfam00084  19 YNYGASVSYECDPGYRLVGSPTITCQEDgTWSPP 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
571-623 4.93e-03

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: 36.10  E-value: 4.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 169636415  571 WSSWSTCDATY---KRSRTRECNNPaPQRGGKRCeGEKRQEEDCtfsimenNGQPC 623
Cdd:pfam19028   6 WSEWSECSVTCgggVQTRTRTVIVE-PQNGGRPC-PELLERRPC-------NLPPC 52
 
Name Accession Description Interval E-value
MACPF smart00457
membrane-attack complex / perforin;
313-514 1.02e-59

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 202.28  E-value: 1.02e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415   313 FIRIHKVMKVLNFTTKAKDLHLSDVFLKALNHLPLEYNSALYSRIFDDFGTHYFTSGSLGGVYDLLYQFSSEELKNSGLT 392
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415   393 EEEAKHCVRIEtkkRVLFAKKTKVEHrCTTNKLSEKHEGSFiqGAEKSISLIRGGRSEYGAALAWEKGSSGLeekTFSEW 472
Cdd:smart00457  81 SEDISKCLAGS---SNSFAGSVSAEH-CLQSSSYIKYLSTS--LRRESHTQVLGGHVTVLCDLLRGPSSNSL---DFSDW 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 169636415   473 LESVKENPAVIDFELAPIVDLVRNIPCAVTKRNNLRKALQEY 514
Cdd:smart00457 152 AESVPNEPVLIDVSLAPIYELLPPNPELSQKREALRQALRSY 193
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
294-514 2.25e-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: 188.00  E-value: 2.25e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415  294 NHNSAFKQAIQASHKKDSSFIRIHKVMKVLNFT-TKAKDLHLSDVFLKALNHLPLEYNSAL---YSRIFDDFGTHYFTSG 369
Cdd:pfam01823   4 SASSEFKKMSDKSKQKKKSLIISKSTCSLYQFTlKRSNKLQLSDEFLQALSDLPDNYDYAAkatYIQFFDKYGTHYITSV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415  370 SLGGVYDLLYQFSSEELKNSGLTEEEAKHCVRIEtkkrVLFAKKTKVEHRCTTNKLSEKHEGSFIQGAEKSISLIRGGRS 449
Cdd:pfam01823  84 TLGGKIVYVLKLDKSQLEDLKLKGEDVKICLSAS----AGASIGSVNLKGCSKNSSSTKEKKSFNQEIESSITLVIGGTP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169636415  450 EYGAAlawekgssglEEKTFSEWLESVKENPAVIDFELAPIVDLvrnIPCAVTKRNNLRKALQEY 514
Cdd:pfam01823 160 ESIDD----------DSKTYSDWAESVKDNPMPIDFELTPISEL---LKGVPLKKENLRKALEEY 211
FIMAC smart00057
factor I membrane attack complex;
862-934 3.95e-20

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 84.90  E-value: 3.95e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169636415   862 CGYDTCYDWEKCSASTskCVCLLPPQCFKGGnQLYCVKMGSStsEKTLNICEVGTIRCANRKMEILHPGKCLA 934
Cdd:smart00057   1 CAKGFCQLWQKCSAST--CVCKLPYECPKAG-TDVCVEDGRS--EKTLTYCKQGALRCLNQKYKFLHIGSCTA 68
FIMAC smart00057
factor I membrane attack complex;
768-839 2.83e-19

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 82.59  E-value: 2.83e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169636415   768 KLKGHCQLGQKQSGSECICMSPEEdCSHHSEDLCVFDTDSndYFTSPACKFLAEKCLnNQQLHFLHIGSCQD 839
Cdd:smart00057   1 CAKGFCQLWQKCSASTCVCKLPYE-CPKAGTDVCVEDGRS--EKTLTYCKQGALRCL-NQKYKFLHIGSCTA 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
568-623 2.02e-10

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: 56.83  E-value: 2.02e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 169636415   568 WGCWSSWSTCDAT---YKRSRTRECNNPAPQRGGKRCEGEKRQEEDCtfsimenNGQPC 623
Cdd:smart00209   1 WSEWSEWSPCSVTcggGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC-------NEQPC 52
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
142-173 2.14e-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: 53.36  E-value: 2.14e-09
                         10        20        30
                 ....*....|....*....|....*....|..
gi 169636415 142 NKFRCDSGRCIARKLECNGENDCGDNSDERDC 173
Cdd:cd00112    4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
644-700 3.56e-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: 53.62  E-value: 3.56e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 169636415 644 CPQPVPPENGFIRNEKQLYLVGEDVEISCLTGFETVGYQYFRCLPDGTWRQGDVECQ 700
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
142-173 3.74e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 52.64  E-value: 3.74e-09
                          10        20        30
                  ....*....|....*....|....*....|..
gi 169636415  142 NKFRCDSGRCIARKLECNGENDCGDNSDERDC 173
Cdd:pfam00057   6 NEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
PHA02831 PHA02831
EEV host range protein; Provisional
644-766 4.38e-09

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 58.47  E-value: 4.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415 644 CPQPVPPENGFIRNEKQLYLVGEDVEISC----LTGFETVGYQYFRCLpDGTWRQGDVECQRTECIKPVVQEVLtITPFQ 719
Cdd:PHA02831  78 CKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYSIVGNETVKCI-NKQWVPKYPVCKLIRCKYPALQNGF-LNVFE 155
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 169636415 720 RLYRIGESIELTCPKGFVVAGPSRYTCQGNS-WTPPISNsltCEKDTL 766
Cdd:PHA02831 156 KKFYYGDIVNFKCKKGFILLGSSVSTCDINSiWYPGIPK---CVKDKV 200
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
644-699 2.73e-08

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: 50.99  E-value: 2.73e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 169636415   644 CPQPVPPENGFIRNEKQLYLVGEDVEISCLTGFETVGYQYFRCLPDGTWRQGDVEC 699
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
142-170 7.50e-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: 49.17  E-value: 7.50e-08
                           10        20
                   ....*....|....*....|....*....
gi 169636415   142 NKFRCDSGRCIARKLECNGENDCGDNSDE 170
Cdd:smart00192   5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Sushi pfam00084
Sushi repeat (SCR repeat);
644-699 7.85e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.81  E-value: 7.85e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 169636415  644 CPQPVPPENGFIRNEKQLYLVGEDVEISCLTGFETVGYQYFRCLPDGTWRQGDVEC 699
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
26-79 1.31e-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: 49.12  E-value: 1.31e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 169636415    26 HYAWTQWTSCSKTCNSGTQSRHRQIVVdkyYQENFCEQICSKQ--ETRECNWQRCP 79
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCS---PPPQNGGGPCTGEdvETRACNEQPCP 53
PHA02927 PHA02927
secreted complement-binding protein; Provisional
644-755 1.55e-07

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 53.89  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415 644 CPQPVPPENGFIRNEKQLYLVGEDVEISCLTGFETVGYQYFRClPDGTWRQGDVeCQRTECIKPVVQEVLTITPFQRLYR 723
Cdd:PHA02927 148 CQSPPSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLC-SGGEWSDPPT-CQIVKCPHPTISNGYLSSGFKRSYS 225
                         90       100       110
                 ....*....|....*....|....*....|...
gi 169636415 724 IGESIELTCPKGFVVAGPSRYTCQ-GNSWTPPI 755
Cdd:PHA02927 226 YNDNVDFKCKYGYKLSGSSSSTCSpGNTWQPEL 258
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
28-78 7.36e-07

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: 46.89  E-value: 7.36e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 169636415   28 AWTQWTSCSKTCNSGTQSRHRQIVVdkyyQENFCEQIC-SKQETRECNWQRC 78
Cdd:pfam19028   5 EWSEWSECSVTCGGGVQTRTRTVIV----EPQNGGRPCpELLERRPCNLPPC 52
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
601-753 8.75e-06

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 48.93  E-value: 8.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415 601 CEGEKRQeedctFSIMENNGQPCINDDEEMKEVDLPEIEADSGCPQPVppengfirneKQLYLVGEDVEISCLTGFETVG 680
Cdd:PHA02954 101 CKDETKY-----FRCEEKNGNTSWNDTVTCPNAECQPLQLEHGSCQPV----------KEKYSFGEHITINCDVGYEVIG 165
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169636415 681 YQYFRCLPDgTWRQGDvECQRTECIKPVVQEVLTITPFQrlyrIGESIELTCPKGFVVAGPSRYTCQGNSWTP 753
Cdd:PHA02954 166 ASYISCTAN-SWNVIP-SCQQKCDIPSLSNGLISGSTFS----IGGVIHLSCKSGFTLTGSPSSTCIDGKWNP 232
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
704-755 1.42e-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: 43.28  E-value: 1.42e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 169636415   704 CIKPVVQEVLTITPFQRLYRIGESIELTCPKGFVVAGPSRYTCQGN-SWTPPI 755
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENgTWSPPP 53
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
704-762 1.60e-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: 43.22  E-value: 1.60e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415 704 CIKPVVQEVLTITPFQRLYRIGESIELTCPKGFVVAGPSRYTCQGNS-WTPPIsnsLTCE 762
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPP---PTCE 57
PHA02639 PHA02639
EEV host range protein; Provisional
644-761 2.15e-05

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 47.35  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415 644 CPQPVPPENGFIRNEKQLYLVGEDVEISCLTGFETVGYQYFRCLPD---GTWRQGDVECQRTECIKPVVQEVLTITPFQR 720
Cdd:PHA02639  22 CDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCIKDknnAIWSNKAPFCMLKECNDPPSIINGKIYNKRE 101
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 169636415 721 LYRIGESIELTCP--KG--FVVAGPSRYTC-QGNSWT--PPISNSLTC 761
Cdd:PHA02639 102 MYKVGDEIYYVCNehKGvqYSLVGNEKITCiQDKSWKpdPPICKMINC 149
PHA02817 PHA02817
EEV Host range protein; Provisional
648-755 3.79e-05

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 46.09  E-value: 3.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415 648 VPPE--NGFIRNEKQLYLVGEDVEISCltGFETVGYQY-------FRCLPDGTWRQGDVECQRTECIKPVVQE-VLTITP 717
Cdd:PHA02817  26 YPPSikNGYIYNKKTEYNIGSNVTFFC--GNNTRGVRYtlvgeknIICEKDGKWNKEFPVCKIIRCRFPALQNgFVNGIP 103
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 169636415 718 FQRLYRIGESIELTCPKGFVVAGPSRYTCQGNS-WTPPI 755
Cdd:PHA02817 104 DSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSsWIPKV 142
TSP_1 pfam00090
Thrombospondin type 1 domain;
85-133 7.48e-05

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 40.86  E-value: 7.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 169636415   85 GDFGPWSDCDPCIEKQSKVRSVLRPSQF-GGQPCTAPLVAFQPCiPSKLC 133
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFpGGEPCTGDDIETQAC-KMDKC 49
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
29-80 1.51e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 45.34  E-value: 1.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 169636415  29 WTQWTSCSKTCNSGTQSRHRQIVVDKyyqenfceqiCSKQETRECNWQRCPI 80
Cdd:PTZ00441 243 WDEWTPCSVTCGKGTHSRSRPILHEG----------CTTHMVEECEEEECPV 284
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
82-127 2.62e-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: 2.62e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 169636415   82 CLLGDFGPWSDCD-PC-IEKQSKVRSVLRPSQFGGQPCTaPLVAFQPC 127
Cdd:pfam19028   1 CVVSEWSEWSECSvTCgGGVQTRTRTVIVEPQNGGRPCP-ELLERRPC 47
TSP_1 pfam00090
Thrombospondin type 1 domain;
29-78 5.30e-04

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 38.55  E-value: 5.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 169636415   29 WTQWTSCSKTCNSGTQSRHRQIVVDKyYQENFCEQicSKQETRECNWQRC 78
Cdd:pfam00090   3 WSPWSPCSVTCGKGIQVRQRTCKSPF-PGGEPCTG--DDIETQACKMDKC 49
Sushi pfam00084
Sushi repeat (SCR repeat);
722-754 8.93e-04

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 38.25  E-value: 8.93e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 169636415  722 YRIGESIELTCPKGFVVAGPSRYTCQGN-SWTPP 754
Cdd:pfam00084  19 YNYGASVSYECDPGYRLVGSPTITCQEDgTWSPP 52
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
659-767 1.70e-03

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 41.61  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636415 659 KQLYLVGEDVEISCLTgfETvgyQYFRCLP---DGTWRQgDVECQRTECiKPVVQEVLTITPFQRLYRIGESIELTCPKG 735
Cdd:PHA02954  88 KPLYEVNSTITLICKD--ET---KYFRCEEkngNTSWND-TVTCPNAEC-QPLQLEHGSCQPVKEKYSFGEHITINCDVG 160
                         90       100       110
                 ....*....|....*....|....*....|..
gi 169636415 736 FVVAGPSRYTCQGNSWTPPISNSLTCEKDTLT 767
Cdd:PHA02954 161 YEVIGASYISCTANSWNVIPSCQQKCDIPSLS 192
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
571-623 4.93e-03

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: 36.10  E-value: 4.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 169636415  571 WSSWSTCDATY---KRSRTRECNNPaPQRGGKRCeGEKRQEEDCtfsimenNGQPC 623
Cdd:pfam19028   6 WSEWSECSVTCgggVQTRTRTVIVE-PQNGGRPC-PELLERRPC-------NLPPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
32-78 7.49e-03

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: 35.51  E-value: 7.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 169636415   32 WTSCSKTCNSGTQSRH---RQIVVDKYYQENFCEQICSKQETRECNWQRC 78
Cdd:pfam19030   6 WGECSVTCGGGVQTRLvqcVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH