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Conserved domains on  [gi|158261721|dbj|BAF83038|]
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unnamed protein product [Homo sapiens]

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
MACPF smart00457
membrane-attack complex / perforin;
250-450 7.80e-59

membrane-attack complex / perforin;


:

Pssm-ID: 214671  Cd Length: 195  Bit Score: 198.81  E-value: 7.80e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721   250 LLVVENTVEVAQFINNNPEfLQLAEPFWKELSHLPSLYDYSAYRRLIDQYGTHYLQSGSLGGEYRVLFYVDSEKLKQNDF 329
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDE-LPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721   330 NSVEEKKC-KSSGWHFVVKFSSHGCKELENALKAASGTQnnVLRGEPFIRGggaGFISGLSYLELDNPAgNKRRYSAWAE 408
Cdd:smart00457  80 TSEDISKClAGSSNSFAGSVSAEHCLQSSSYIKYLSTSL--RRESHTQVLG---GHVTVLCDLLRGPSS-NSLDFSDWAE 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 158261721   409 SVTNLPQVIKQKLTPLYELVKEVPCASVKKLYLKWALEEYLD 450
Cdd:smart00457 154 SVPNEPVLIDVSLAPIYELLPPNPELSQKREALRQALRSYLK 195
Kazal_3 pfam18434
Kazal-type serine protease inhibitor domain; Kazal domain found in factor I-like modules (FIMs) ...
 791-838 9.25e-23

Kazal-type serine protease inhibitor domain; Kazal domain found in factor I-like modules (FIMs) region on the carboxyl-terminal of complement component C7 proteins. Complement component C7 is a subunit of the membrane attack complex (MAC), a fundamental machinery in the mammalian innate immunity. KAZAL domains are common in serine protease inhibitors.


:

Pssm-ID: 436499  Cd Length: 50  Bit Score: 91.63  E-value: 9.25e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 158261721  791 CREASECEEEGFSICVEVNGK--EQTMSECEAGALRCRGQSISVTSIRPC 838
Cdd:pfam18434   1 CREASECEEGGISVCVEVNGGaaEQTMTECEAGVLRCRGESVTVVSIRPC 50
FIMAC smart00057
factor I membrane attack complex;
697-765 4.98e-21

factor I membrane attack complex;


:

Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 87.60  E-value: 4.98e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721   697 QAVPKCQRWEKLQNSRCVCKMPYECGP-SLDVCAQDERSkrILPLTVCKMHVLHCQGRNYTLTGRDSCTL 765
Cdd:smart00057   1 CAKGFCQLWQKCSASTCVCKLPYECPKaGTDVCVEDGRS--EKTLTYCKQGALRCLNQKYKFLHIGSCTA 68
PHA02817 super family cl31508
EEV Host range protein; Provisional
 571-683 2.79e-12

EEV Host range protein; Provisional


The actual alignment was detected with superfamily member PHA02817:

Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 67.27  E-value: 2.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721 571 CPSPPALKDGFVQDEGTMFPVGKNVVYTCNEG-----YSLIGNPVARCGEDLRWLVGEMHCQKIACVLPVLMDG-IQSHP 644
Cdd:PHA02817  24 CCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRCRFPALQNGfVNGIP 103

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 158261721 645 QKPFYTVGEKVTVSCSGGMSLEGPSAFLCGSSLKWSPEM 683
Cdd:PHA02817 104 DSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKV 142
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 503-545 3.79e-09

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: 53.36  E-value: 3.79e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 158261721   503 WSCWSSWSPCVQ----GKKTRSRECNNPPPSGGGRSCVGETTESTQC 545
Cdd:smart00209   1 WSEWSEWSPCSVtcggGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC 47
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 89-119 6.63e-06

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: 43.35  E-value: 6.63e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 158261721  89 FRCFSGQCISKSLVCNGDSDCdEDSADEDRC 119
Cdd:cd00112    6 FRCANGRCIPSSWVCDGEDDC-GDGSDEENC 35
 
Name Accession Description Interval E-value
MACPF smart00457
membrane-attack complex / perforin;
250-450 7.80e-59

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 198.81  E-value: 7.80e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721   250 LLVVENTVEVAQFINNNPEfLQLAEPFWKELSHLPSLYDYSAYRRLIDQYGTHYLQSGSLGGEYRVLFYVDSEKLKQNDF 329
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDE-LPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721   330 NSVEEKKC-KSSGWHFVVKFSSHGCKELENALKAASGTQnnVLRGEPFIRGggaGFISGLSYLELDNPAgNKRRYSAWAE 408
Cdd:smart00457  80 TSEDISKClAGSSNSFAGSVSAEHCLQSSSYIKYLSTSL--RRESHTQVLG---GHVTVLCDLLRGPSS-NSLDFSDWAE 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 158261721   409 SVTNLPQVIKQKLTPLYELVKEVPCASVKKLYLKWALEEYLD 450
Cdd:smart00457 154 SVPNEPVLIDVSLAPIYELLPPNPELSQKREALRQALRSYLK 195
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 243-448 5.98e-53

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: 183.38  E-value: 5.98e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721  243 HKGKSYQLLVVENTVEVAQFINNNPEFLQLAEPFWKELSHLPSLYDYSA---YRRLIDQYGTHYLQSGSLGGEYRVLFYV 319
Cdd:pfam01823  16 SKQKKKSLIISKSTCSLYQFTLKRSNKLQLSDEFLQALSDLPDNYDYAAkatYIQFFDKYGTHYITSVTLGGKIVYVLKL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721  320 DSEKLKQNDFNSVEEKKCKSSGWHFV-VKFSSHGCKELENALKAASGTQNNVLRGEPFIRGGgagfisglsylELDNPAG 398
Cdd:pfam01823  96 DKSQLEDLKLKGEDVKICLSASAGASiGSVNLKGCSKNSSSTKEKKSFNQEIESSITLVIGG-----------TPESIDD 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 158261721  399 NKRRYSAWAESVTNLPQVIKQKLTPLYELVKEVPcasVKKLYLKWALEEY 448
Cdd:pfam01823 165 DSKTYSDWAESVKDNPMPIDFELTPISELLKGVP---LKKENLRKALEEY 211
Kazal_3 pfam18434
Kazal-type serine protease inhibitor domain; Kazal domain found in factor I-like modules (FIMs) ...
 791-838 9.25e-23

Kazal-type serine protease inhibitor domain; Kazal domain found in factor I-like modules (FIMs) region on the carboxyl-terminal of complement component C7 proteins. Complement component C7 is a subunit of the membrane attack complex (MAC), a fundamental machinery in the mammalian innate immunity. KAZAL domains are common in serine protease inhibitors.


Pssm-ID: 436499  Cd Length: 50  Bit Score: 91.63  E-value: 9.25e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 158261721  791 CREASECEEEGFSICVEVNGK--EQTMSECEAGALRCRGQSISVTSIRPC 838
Cdd:pfam18434   1 CREASECEEGGISVCVEVNGGaaEQTMTECEAGVLRCRGESVTVVSIRPC 50
FIMAC smart00057
factor I membrane attack complex;
771-840 1.31e-21

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 89.14  E-value: 1.31e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721   771 KACGACPLWGKCDAESskCVCREASECEEEGFSICVEVNGKEQTMSECEAGALRCRGQSISVTSIRPCAA 840
Cdd:smart00057   1 CAKGFCQLWQKCSAST--CVCKLPYECPKAGTDVCVEDGRSEKTLTYCKQGALRCLNQKYKFLHIGSCTA 68
FIMAC smart00057
factor I membrane attack complex;
697-765 4.98e-21

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 87.60  E-value: 4.98e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721   697 QAVPKCQRWEKLQNSRCVCKMPYECGP-SLDVCAQDERSkrILPLTVCKMHVLHCQGRNYTLTGRDSCTL 765
Cdd:smart00057   1 CAKGFCQLWQKCSASTCVCKLPYECPKaGTDVCVEDGRS--EKTLTYCKQGALRCLNQKYKFLHIGSCTA 68
PHA02817 PHA02817
EEV Host range protein; Provisional
 571-683 2.79e-12

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 67.27  E-value: 2.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721 571 CPSPPALKDGFVQDEGTMFPVGKNVVYTCNEG-----YSLIGNPVARCGEDLRWLVGEMHCQKIACVLPVLMDG-IQSHP 644
Cdd:PHA02817  24 CCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRCRFPALQNGfVNGIP 103

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 158261721 645 QKPFYTVGEKVTVSCSGGMSLEGPSAFLCGSSLKWSPEM 683
Cdd:PHA02817 104 DSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKV 142
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 503-545 3.79e-09

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: 53.36  E-value: 3.79e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 158261721   503 WSCWSSWSPCVQ----GKKTRSRECNNPPPSGGGRSCVGETTESTQC 545
Cdd:smart00209   1 WSEWSEWSPCSVtcggGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC 47
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 571-627 8.89e-09

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


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 52.08  E-value: 8.89e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 158261721 571 CPSPPALKDGFVQDEGTMFPVGKNVVYTCNEGYSLIGNPVARCGEDLRWLVGEMHCQ 627
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 571-626 1.02e-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: 52.14  E-value: 1.02e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 158261721   571 CPSPPALKDGFVQDEGTMFPVGKNVVYTCNEGYSLIGNPVARCGEDLRWLVGEMHC 626
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
571-626 6.67e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.81  E-value: 6.67e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 158261721  571 CPSPPALKDGFVQDEGTMFPVGKNVVYTCNEGYSLIGNPVARCGEDLRWLVGEMHC 626
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 89-119 6.63e-06

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: 43.35  E-value: 6.63e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 158261721  89 FRCFSGQCISKSLVCNGDSDCdEDSADEDRC 119
Cdd:cd00112    6 FRCANGRCIPSSWVCDGEDDC-GDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 89-116 1.05e-04

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: 39.92  E-value: 1.05e-04
                           10        20
                   ....*....|....*....|....*...
gi 158261721    89 FRCFSGQCISKSLVCNGDSDCdEDSADE 116
Cdd:smart00192   7 FQCDNGRCIPSSWVCDGVDDC-GDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
89-119 1.35e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 39.92  E-value: 1.35e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 158261721   89 FRCFSGQCISKSLVCNGDSDCdEDSADEDRC 119
Cdd:pfam00057   8 FQCGSGECIPRSWVCDGDPDC-GDGSDEENC 37
PTZ00482 PTZ00482
membrane-attack complex/perforin (MACPF) Superfamily; Provisional
 290-430 1.47e-04

membrane-attack complex/perforin (MACPF) Superfamily; Provisional


Pssm-ID: 240433 [Multi-domain]  Cd Length: 844  Bit Score: 45.63  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721 290 SAYRRLIDQYGTHYLQSGSLGGEYRVLFYVDS---EKLKQNDFNSVEEKKCKSSGwhfvvkFSSHGCKELENALKAASGT 366
Cdd:PTZ00482 427 PIWISFFEQYGTHIIMELQLGGKITKQVTVKNssvEQMKKDGVSVKAQVKAQFGF------ASAGGSTNVSSDNSSASNE 500

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158261721 367 QNNVLRGEPFIRGGgagfisglsyleldNPAGN---KRRYSAWAESVTNLPQVIKQKLTPLYELVKE 430
Cdd:PTZ00482 501 YSYNMSEQLLVIGG--------------NPIKDvtkEENLAEWSKTVSTLPMPINIELLPISTLFPS 553
 
Name Accession Description Interval E-value
MACPF smart00457
membrane-attack complex / perforin;
250-450 7.80e-59

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 198.81  E-value: 7.80e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721   250 LLVVENTVEVAQFINNNPEfLQLAEPFWKELSHLPSLYDYSAYRRLIDQYGTHYLQSGSLGGEYRVLFYVDSEKLKQNDF 329
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDE-LPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721   330 NSVEEKKC-KSSGWHFVVKFSSHGCKELENALKAASGTQnnVLRGEPFIRGggaGFISGLSYLELDNPAgNKRRYSAWAE 408
Cdd:smart00457  80 TSEDISKClAGSSNSFAGSVSAEHCLQSSSYIKYLSTSL--RRESHTQVLG---GHVTVLCDLLRGPSS-NSLDFSDWAE 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 158261721   409 SVTNLPQVIKQKLTPLYELVKEVPCASVKKLYLKWALEEYLD 450
Cdd:smart00457 154 SVPNEPVLIDVSLAPIYELLPPNPELSQKREALRQALRSYLK 195
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 243-448 5.98e-53

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: 183.38  E-value: 5.98e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721  243 HKGKSYQLLVVENTVEVAQFINNNPEFLQLAEPFWKELSHLPSLYDYSA---YRRLIDQYGTHYLQSGSLGGEYRVLFYV 319
Cdd:pfam01823  16 SKQKKKSLIISKSTCSLYQFTLKRSNKLQLSDEFLQALSDLPDNYDYAAkatYIQFFDKYGTHYITSVTLGGKIVYVLKL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721  320 DSEKLKQNDFNSVEEKKCKSSGWHFV-VKFSSHGCKELENALKAASGTQNNVLRGEPFIRGGgagfisglsylELDNPAG 398
Cdd:pfam01823  96 DKSQLEDLKLKGEDVKICLSASAGASiGSVNLKGCSKNSSSTKEKKSFNQEIESSITLVIGG-----------TPESIDD 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 158261721  399 NKRRYSAWAESVTNLPQVIKQKLTPLYELVKEVPcasVKKLYLKWALEEY 448
Cdd:pfam01823 165 DSKTYSDWAESVKDNPMPIDFELTPISELLKGVP---LKKENLRKALEEY 211
Kazal_3 pfam18434
Kazal-type serine protease inhibitor domain; Kazal domain found in factor I-like modules (FIMs) ...
 791-838 9.25e-23

Kazal-type serine protease inhibitor domain; Kazal domain found in factor I-like modules (FIMs) region on the carboxyl-terminal of complement component C7 proteins. Complement component C7 is a subunit of the membrane attack complex (MAC), a fundamental machinery in the mammalian innate immunity. KAZAL domains are common in serine protease inhibitors.


Pssm-ID: 436499  Cd Length: 50  Bit Score: 91.63  E-value: 9.25e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 158261721  791 CREASECEEEGFSICVEVNGK--EQTMSECEAGALRCRGQSISVTSIRPC 838
Cdd:pfam18434   1 CREASECEEGGISVCVEVNGGaaEQTMTECEAGVLRCRGESVTVVSIRPC 50
FIMAC smart00057
factor I membrane attack complex;
771-840 1.31e-21

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 89.14  E-value: 1.31e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721   771 KACGACPLWGKCDAESskCVCREASECEEEGFSICVEVNGKEQTMSECEAGALRCRGQSISVTSIRPCAA 840
Cdd:smart00057   1 CAKGFCQLWQKCSAST--CVCKLPYECPKAGTDVCVEDGRSEKTLTYCKQGALRCLNQKYKFLHIGSCTA 68
FIMAC smart00057
factor I membrane attack complex;
697-765 4.98e-21

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 87.60  E-value: 4.98e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721   697 QAVPKCQRWEKLQNSRCVCKMPYECGP-SLDVCAQDERSkrILPLTVCKMHVLHCQGRNYTLTGRDSCTL 765
Cdd:smart00057   1 CAKGFCQLWQKCSASTCVCKLPYECPKaGTDVCVEDGRS--EKTLTYCKQGALRCLNQKYKFLHIGSCTA 68
PHA02817 PHA02817
EEV Host range protein; Provisional
 571-683 2.79e-12

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 67.27  E-value: 2.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721 571 CPSPPALKDGFVQDEGTMFPVGKNVVYTCNEG-----YSLIGNPVARCGEDLRWLVGEMHCQKIACVLPVLMDG-IQSHP 644
Cdd:PHA02817  24 CCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRCRFPALQNGfVNGIP 103

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 158261721 645 QKPFYTVGEKVTVSCSGGMSLEGPSAFLCGSSLKWSPEM 683
Cdd:PHA02817 104 DSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKV 142
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 571-690 4.32e-11

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 64.29  E-value: 4.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721 571 CPSPPALKDGFVQDEGTMFPVGKNVVYTCNEGYSLIGNPVARC--GEdlrWlVGEMHCQKIACVLPVLMDGIQSHPQKPF 648
Cdd:PHA02927 148 CQSPPSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLCsgGE---W-SDPPTCQIVKCPHPTISNGYLSSGFKRS 223

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 158261721 649 YTVGEKVTVSCSGGMSLEGPSAFLCGSSLKWSPEMknARCVQ 690
Cdd:PHA02927 224 YSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPEL--PKCVR 263
PHA02639 PHA02639
EEV host range protein; Provisional
 571-692 1.21e-10

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 63.53  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721 571 CPSPPALKDGFVQDEGTMFPVGKNVVYTCNE----GYSLIGNPVARCGEDLRWLVGEMHCQKIACVLPVLMDG-IQSHPQ 645
Cdd:PHA02639  85 CNDPPSIINGKIYNKREMYKVGDEIYYVCNEhkgvQYSLVGNEKITCIQDKSWKPDPPICKMINCRFPALQNGyINGIPS 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 158261721 646 KPFYTVGEKVTVSCSGGMSLEGPSAFLCGSSLKWSPEMKNarCVQKE 692
Cdd:PHA02639 165 NKKFYYKTRVGFSCKSGFDLVGEKYSTCNINATWFPSIPT--CVRNK 209
PHA02831 PHA02831
EEV host range protein; Provisional
 571-690 1.22e-10

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 63.09  E-value: 1.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721 571 CPSPPALKDGFVQDEGTMFPVGKNVVYTCN----EGYSLIGNPVARCgEDLRWLVGEMHCQKIACVLPVLMDGIQSHPQK 646
Cdd:PHA02831  78 CKDPVTILNGYIKNKKDQYSFGDSVTYACKvnklEKYSIVGNETVKC-INKQWVPKYPVCKLIRCKYPALQNGFLNVFEK 156

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 158261721 647 PFYtVGEKVTVSCSGGMSLEGPSAFLCGSSLKWSPEMknARCVQ 690
Cdd:PHA02831 157 KFY-YGDIVNFKCKKGFILLGSSVSTCDINSIWYPGI--PKCVK 197
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 571-688 5.38e-10

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 60.82  E-value: 5.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721 571 CPSPPALKDGFVQDEGTMFpvGKNVVYTCNEGYSLIGNPVARC----GEDLRWLVGEMHCQKIACVLPVLMDGIQSHPQK 646
Cdd:PHA02927  86 CPSPRDIDNGQLDIGGVDF--GSSITYSCNSGYQLIGESKSYCelgsTGSMVWNPEAPICESVKCQSPPSISNGRHNGYE 163

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 158261721 647 PFYTVGEKVTVSCSGGMSLEGPSAFLCgSSLKWS--PEMKNARC 688
Cdd:PHA02927 164 DFYTDGSVVTYSCNSGYSLIGNSGVLC-SGGEWSdpPTCQIVKC 206
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 503-545 3.79e-09

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: 53.36  E-value: 3.79e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 158261721   503 WSCWSSWSPCVQ----GKKTRSRECNNPPPSGGGRSCVGETTESTQC 545
Cdd:smart00209   1 WSEWSEWSPCSVtcggGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC 47
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 571-627 8.89e-09

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


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 52.08  E-value: 8.89e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 158261721 571 CPSPPALKDGFVQDEGTMFPVGKNVVYTCNEGYSLIGNPVARCGEDLRWLVGEMHCQ 627
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 571-626 1.02e-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: 52.14  E-value: 1.02e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 158261721   571 CPSPPALKDGFVQDEGTMFPVGKNVVYTCNEGYSLIGNPVARCGEDLRWLVGEMHC 626
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
571-626 6.67e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.81  E-value: 6.67e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 158261721  571 CPSPPALKDGFVQDEGTMFPVGKNVVYTCNEGYSLIGNPVARCGEDLRWLVGEMHC 626
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02639 PHA02639
EEV host range protein; Provisional
 566-705 5.45e-06

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 49.28  E-value: 5.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721 566 VPTEFCPSPPALKDGFVQDEGTMFPVGKNVVYTCNEGYSLIGNPVARCGEDLR---WLVGEMHCQKIACVLPVLMDGIQS 642
Cdd:PHA02639  17 VKSIYCDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCIKDKNnaiWSNKAPFCMLKECNDPPSIINGKI 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158261721 643 HPQKPFYTVGEKVTVSCSG----GMSLEGPSAFLCGSSLKWSPE-----MKNARCVQKENPLTQAVPKCQRW 705
Cdd:PHA02639  97 YNKREMYKVGDEIYYVCNEhkgvQYSLVGNEKITCIQDKSWKPDppickMINCRFPALQNGYINGIPSNKKF 168
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 89-119 6.63e-06

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: 43.35  E-value: 6.63e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 158261721  89 FRCFSGQCISKSLVCNGDSDCdEDSADEDRC 119
Cdd:cd00112    6 FRCANGRCIPSSWVCDGEDDC-GDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 89-116 1.05e-04

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: 39.92  E-value: 1.05e-04
                           10        20
                   ....*....|....*....|....*...
gi 158261721    89 FRCFSGQCISKSLVCNGDSDCdEDSADE 116
Cdd:smart00192   7 FQCDNGRCIPSSWVCDGVDDC-GDGSDE 33
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 631-683 1.23e-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 [Multi-domain]  Cd Length: 56  Bit Score: 40.59  E-value: 1.23e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 158261721   631 CVLPVLMDGIQSHPQKPFYTVGEKVTVSCSGGMSLEGPSAFLCGSSLKWSPEM 683
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPP 53
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
89-119 1.35e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 39.92  E-value: 1.35e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 158261721   89 FRCFSGQCISKSLVCNGDSDCdEDSADEDRC 119
Cdd:pfam00057   8 FQCGSGECIPRSWVCDGDPDC-GDGSDEENC 37
PTZ00482 PTZ00482
membrane-attack complex/perforin (MACPF) Superfamily; Provisional
 290-430 1.47e-04

membrane-attack complex/perforin (MACPF) Superfamily; Provisional


Pssm-ID: 240433 [Multi-domain]  Cd Length: 844  Bit Score: 45.63  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158261721 290 SAYRRLIDQYGTHYLQSGSLGGEYRVLFYVDS---EKLKQNDFNSVEEKKCKSSGwhfvvkFSSHGCKELENALKAASGT 366
Cdd:PTZ00482 427 PIWISFFEQYGTHIIMELQLGGKITKQVTVKNssvEQMKKDGVSVKAQVKAQFGF------ASAGGSTNVSSDNSSASNE 500

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158261721 367 QNNVLRGEPFIRGGgagfisglsyleldNPAGN---KRRYSAWAESVTNLPQVIKQKLTPLYELVKE 430
Cdd:PTZ00482 501 YSYNMSEQLLVIGG--------------NPIKDvtkEENLAEWSKTVSTLPMPINIELLPISTLFPS 553
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 631-683 1.86e-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 [Multi-domain]  Cd Length: 57  Bit Score: 40.14  E-value: 1.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 158261721 631 CVLPVLMDGIQSHPQKPFYTVGEKVTVSCSGGMSLEGPSAFLCGSSLKWSPEM 683
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPP 53
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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