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Conserved domains on  [gi|2512653539|pdb|8B6W|U]
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Chain U, Mpf2Ba1

Protein Classification

MACPF domain-containing protein( domain architecture ID 1760)

MACPF (MAC/Perforin) domain-containing protein may facilitate membrane insertion and pore formation; similar to Phyllodiscus semoni DELTA-alicitoxin-Pse2a that causes lethal toxicity to the shrimp Palaemon paucidence, and hemolytic activity toward sheep red blood cells

Gene Ontology:  GO:0051205

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MACPF super family cl46582
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 90-266 2.20e-11

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.


The actual alignment was detected with superfamily member pfam01823:

Pssm-ID: 460349  Cd Length: 211  Bit Score: 63.19  E-value: 2.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8B6W_U         90 FSGSLSTDFD--SNSLRNAENEFTRIQQSINLWSLRLPsvKSLRELMLPHMRQQLDELNVN-DPKAISRY---FDRVGSH 163
Cdd:pfam01823   1 GSFSASSEFKkmSDKSKQKKKSLIISKSTCSLYQFTLK--RSNKLQLSDEFLQALSDLPDNyDYAAKATYiqfFDKYGTH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8B6W_U        164 FLTGIVMGGRAIL--------ASSTNKLRVKRDYSVSVVAKASYEGLTGQLSAEAKAKYGESiSSFTQYSNTHQ-EVRGG 234
Cdd:pfam01823  79 YITSVTLGGKIVYvlkldksqLEDLKLKGEDVKICLSASAGASIGSVNLKGCSKNSSSTKEK-KSFNQEIESSItLVIGG 157

                         170       180       190
                  ....*....|....*....|....*....|..
8B6W_U        235 DGakahGVFSGKKEDFQAWVDSVSASPDFVDF 266
Cdd:pfam01823 158 TP----ESIDDDSKTYSDWAESVKDNPMPIDF 185
 
Name Accession Description Interval E-value
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 90-266 2.20e-11

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: 63.19  E-value: 2.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8B6W_U         90 FSGSLSTDFD--SNSLRNAENEFTRIQQSINLWSLRLPsvKSLRELMLPHMRQQLDELNVN-DPKAISRY---FDRVGSH 163
Cdd:pfam01823   1 GSFSASSEFKkmSDKSKQKKKSLIISKSTCSLYQFTLK--RSNKLQLSDEFLQALSDLPDNyDYAAKATYiqfFDKYGTH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8B6W_U        164 FLTGIVMGGRAIL--------ASSTNKLRVKRDYSVSVVAKASYEGLTGQLSAEAKAKYGESiSSFTQYSNTHQ-EVRGG 234
Cdd:pfam01823  79 YITSVTLGGKIVYvlkldksqLEDLKLKGEDVKICLSASAGASIGSVNLKGCSKNSSSTKEK-KSFNQEIESSItLVIGG 157

                         170       180       190
                  ....*....|....*....|....*....|..
8B6W_U        235 DGakahGVFSGKKEDFQAWVDSVSASPDFVDF 266
Cdd:pfam01823 158 TP----ESIDDDSKTYSDWAESVKDNPMPIDF 185
MACPF smart00457
membrane-attack complex / perforin;
149-266 8.01e-08

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 52.44  E-value: 8.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8B6W_U         149 DPKAISRYFDRVGSHFLTGIVMGGRAILASSTNKLRVKRDY----SVSVVAKASYEGLTGQLSAEAKAKYGESI--SSFT 222
Cdd:smart00457  38 NRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGltseDISKCLAGSSNSFAGSVSAEHCLQSSSYIkyLSTS 117

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
8B6W_U         223 QYSNTHQEVRGGD---GAKAHGVFSGKKEDFQAWVDSVSASPDFVDF 266
Cdd:smart00457 118 LRRESHTQVLGGHvtvLCDLLRGPSSNSLDFSDWAESVPNEPVLIDV 164
 
Name Accession Description Interval E-value
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 90-266 2.20e-11

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: 63.19  E-value: 2.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8B6W_U         90 FSGSLSTDFD--SNSLRNAENEFTRIQQSINLWSLRLPsvKSLRELMLPHMRQQLDELNVN-DPKAISRY---FDRVGSH 163
Cdd:pfam01823   1 GSFSASSEFKkmSDKSKQKKKSLIISKSTCSLYQFTLK--RSNKLQLSDEFLQALSDLPDNyDYAAKATYiqfFDKYGTH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8B6W_U        164 FLTGIVMGGRAIL--------ASSTNKLRVKRDYSVSVVAKASYEGLTGQLSAEAKAKYGESiSSFTQYSNTHQ-EVRGG 234
Cdd:pfam01823  79 YITSVTLGGKIVYvlkldksqLEDLKLKGEDVKICLSASAGASIGSVNLKGCSKNSSSTKEK-KSFNQEIESSItLVIGG 157

                         170       180       190
                  ....*....|....*....|....*....|..
8B6W_U        235 DGakahGVFSGKKEDFQAWVDSVSASPDFVDF 266
Cdd:pfam01823 158 TP----ESIDDDSKTYSDWAESVKDNPMPIDF 185
MACPF smart00457
membrane-attack complex / perforin;
149-266 8.01e-08

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 52.44  E-value: 8.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8B6W_U         149 DPKAISRYFDRVGSHFLTGIVMGGRAILASSTNKLRVKRDY----SVSVVAKASYEGLTGQLSAEAKAKYGESI--SSFT 222
Cdd:smart00457  38 NRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGltseDISKCLAGSSNSFAGSVSAEHCLQSSSYIkyLSTS 117

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
8B6W_U         223 QYSNTHQEVRGGD---GAKAHGVFSGKKEDFQAWVDSVSASPDFVDF 266
Cdd:smart00457 118 LRRESHTQVLGGHvtvLCDLLRGPSSNSLDFSDWAESVPNEPVLIDV 164
 
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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