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Conserved domains on  [gi|172045784|sp|Q9WV57|]
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RecName: Full=Macrophage-expressed gene 1 protein; Short=Macrophage gene 1 protein; Short=Mpg-1; AltName: Full=Perforin-2; Short=P-2; Contains: RecName: Full=Macrophage-expressed gene 1 protein, processed form; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MPEG1_P2 cd22579
P2 domain of macrophage-expressed gene 1 protein (MPEG1) and similar proteins; ...
347-627 2.25e-158

P2 domain of macrophage-expressed gene 1 protein (MPEG1) and similar proteins; Macrophage-expressed gene 1 protein (MPEG1), also called perforin-2 (P-2) or macrophage gene 1 protein (Mpg-1), is a pore-forming, antibacterial protein with broad-spectrum activity. It is a major antibacterial effector protein of the innate immune system in phagocytic as well as tissue forming cells. It plays an essential role in intracellular defense of parenchymal cells and phagocytes against pathogenic bacteria by inserting into the bacterial surface to form pores. This model corresponds to a unique membrane bound P2 domain of MPEG1, which helps to stabilize the pre-pore state by swapping between monomers and enables MPEG1 to bind its targeted membrane.


:

Pssm-ID: 439345  Cd Length: 287  Bit Score: 459.04  E-value: 2.25e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784 347 HPGCTNVDSPNFNFQANMEDDSCDAKVTNFTFGGLYQECTELSGDA--LCQNLEQKNLLTGDFSCPSGYTPVHLLSqthe 424
Cdd:cd22579    1 HPGCTDPDSPNFNFQANVDDGSCEGPATNFTFGGVYQTCTGLSGDAgdLCQGLTQKNPLTGDFSCPAGYEPVLLLS---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784 425 EGYSRLECKKKCTLKIFCKTVCEDVFRVAKAQFRAYWCVATGQVPDNSGLLFGGLFTDKSINPMTNAQSCPAGYIPLNLF 504
Cdd:cd22579   77 GGYSVTECRKVCHSCWLFFTCCHDECAVSYATYTTYWCAATGPVPQNSGYLFGGLYTSKTVNPVTGSQSCPPYFYPLKLG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784 505 ESLKVCVSLDYELGYKFSVPFGGFFSCIMGNPLVNS---------DTAKDIGAPSLKKCPGGFSQHLAVISDGCQVSYCV 575
Cdd:cd22579  157 SDLKVCVSDDYELGSRYSVPFGGFFSCQSGNPLAGSlksnsagslKGYQDGPSSWPKRCPPGYSQHLATISDGCQVNYCV 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 172045784 576 KAGIFTGGSLLPVRLPPYTKPPLMSQVATNTVIVTSSETaRSWIKDPQTNQW 627
Cdd:cd22579  237 KAGSLSGGSLPPIRRPPFTPPPLLSVNATNTVLISGSGG-QSWVKNGSSNQW 287
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
125-341 5.96e-38

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: 140.23  E-value: 5.96e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784  125 VNGKFSTEFQRM--KTLQVKDQAVTTRVQVRNRIYTVKNSPTSELSFGFTNALMDICDQLEKNQTKMAtylaELLVLNYG 202
Cdd:pfam01823   1 GSFSASSEFKKMsdKSKQKKKSLIISKSTCSLYQFTLKRSNKLQLSDEFLQALSDLPDNYDYAAKATY----IQFFDKYG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784  203 THVITSVDAGAALVQEDHIRSSFLLDNQNSENT----VTASAGIAFLNiVNFKVETDHTSQTLLTKSYLSNRTNSRVQSF 278
Cdd:pfam01823  77 THYITSVTLGGKIVYVLKLDKSQLEDLKLKGEDvkicLSASAGASIGS-VNLKGCSKNSSSTKEKKSFNQEIESSITLVI 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 172045784  279 GGIPF---YPGITLETWQKGITNHLVAIDRAGLPLHFFIKPdklpglpgglVKKLSKTVETAVRHY 341
Cdd:pfam01823 156 GGTPEsidDDSKTYSDWAESVKDNPMPIDFELTPISELLKG----------VPLKKENLRKALEEY 211
 
Name Accession Description Interval E-value
MPEG1_P2 cd22579
P2 domain of macrophage-expressed gene 1 protein (MPEG1) and similar proteins; ...
347-627 2.25e-158

P2 domain of macrophage-expressed gene 1 protein (MPEG1) and similar proteins; Macrophage-expressed gene 1 protein (MPEG1), also called perforin-2 (P-2) or macrophage gene 1 protein (Mpg-1), is a pore-forming, antibacterial protein with broad-spectrum activity. It is a major antibacterial effector protein of the innate immune system in phagocytic as well as tissue forming cells. It plays an essential role in intracellular defense of parenchymal cells and phagocytes against pathogenic bacteria by inserting into the bacterial surface to form pores. This model corresponds to a unique membrane bound P2 domain of MPEG1, which helps to stabilize the pre-pore state by swapping between monomers and enables MPEG1 to bind its targeted membrane.


Pssm-ID: 439345  Cd Length: 287  Bit Score: 459.04  E-value: 2.25e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784 347 HPGCTNVDSPNFNFQANMEDDSCDAKVTNFTFGGLYQECTELSGDA--LCQNLEQKNLLTGDFSCPSGYTPVHLLSqthe 424
Cdd:cd22579    1 HPGCTDPDSPNFNFQANVDDGSCEGPATNFTFGGVYQTCTGLSGDAgdLCQGLTQKNPLTGDFSCPAGYEPVLLLS---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784 425 EGYSRLECKKKCTLKIFCKTVCEDVFRVAKAQFRAYWCVATGQVPDNSGLLFGGLFTDKSINPMTNAQSCPAGYIPLNLF 504
Cdd:cd22579   77 GGYSVTECRKVCHSCWLFFTCCHDECAVSYATYTTYWCAATGPVPQNSGYLFGGLYTSKTVNPVTGSQSCPPYFYPLKLG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784 505 ESLKVCVSLDYELGYKFSVPFGGFFSCIMGNPLVNS---------DTAKDIGAPSLKKCPGGFSQHLAVISDGCQVSYCV 575
Cdd:cd22579  157 SDLKVCVSDDYELGSRYSVPFGGFFSCQSGNPLAGSlksnsagslKGYQDGPSSWPKRCPPGYSQHLATISDGCQVNYCV 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 172045784 576 KAGIFTGGSLLPVRLPPYTKPPLMSQVATNTVIVTSSETaRSWIKDPQTNQW 627
Cdd:cd22579  237 KAGSLSGGSLPPIRRPPFTPPPLLSVNATNTVLISGSGG-QSWVKNGSSNQW 287
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
125-341 5.96e-38

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: 140.23  E-value: 5.96e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784  125 VNGKFSTEFQRM--KTLQVKDQAVTTRVQVRNRIYTVKNSPTSELSFGFTNALMDICDQLEKNQTKMAtylaELLVLNYG 202
Cdd:pfam01823   1 GSFSASSEFKKMsdKSKQKKKSLIISKSTCSLYQFTLKRSNKLQLSDEFLQALSDLPDNYDYAAKATY----IQFFDKYG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784  203 THVITSVDAGAALVQEDHIRSSFLLDNQNSENT----VTASAGIAFLNiVNFKVETDHTSQTLLTKSYLSNRTNSRVQSF 278
Cdd:pfam01823  77 THYITSVTLGGKIVYVLKLDKSQLEDLKLKGEDvkicLSASAGASIGS-VNLKGCSKNSSSTKEKKSFNQEIESSITLVI 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 172045784  279 GGIPF---YPGITLETWQKGITNHLVAIDRAGLPLHFFIKPdklpglpgglVKKLSKTVETAVRHY 341
Cdd:pfam01823 156 GGTPEsidDDSKTYSDWAESVKDNPMPIDFELTPISELLKG----------VPLKKENLRKALEEY 211
MACPF smart00457
membrane-attack complex / perforin;
146-343 1.35e-35

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 133.33  E-value: 1.35e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784   146 VTTRVQVRNRIYTVKNsPTSELSFGFTNALMDICDQLEKNqtkmatyLAELLVLNYGTHVITSVDAGAALVQEDHI-RSS 224
Cdd:smart00457   2 LVARDTVRNRLYSVKL-DELPLALEFLKALRDLPDTYNRG-------AYARFIDDYGTHYITSATLGGEYSLLLVLdKES 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784   225 FLLDNQNSENTVTASAGiaFLNIVNFKVETDHTSQTLLTKSYLSNRT--NSRVQSFGG-IPFYP---------GITLETW 292
Cdd:smart00457  74 LERKGLTSEDISKCLAG--SSNSFAGSVSAEHCLQSSSYIKYLSTSLrrESHTQVLGGhVTVLCdllrgpssnSLDFSDW 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 172045784   293 QKGITNHLVAIDRAGLPLHFFIKPDKlpglpggLVKKLSKTVETAVRHYYT 343
Cdd:smart00457 152 AESVPNEPVLIDVSLAPIYELLPPNP-------ELSQKREALRQALRSYLK 195
 
Name Accession Description Interval E-value
MPEG1_P2 cd22579
P2 domain of macrophage-expressed gene 1 protein (MPEG1) and similar proteins; ...
347-627 2.25e-158

P2 domain of macrophage-expressed gene 1 protein (MPEG1) and similar proteins; Macrophage-expressed gene 1 protein (MPEG1), also called perforin-2 (P-2) or macrophage gene 1 protein (Mpg-1), is a pore-forming, antibacterial protein with broad-spectrum activity. It is a major antibacterial effector protein of the innate immune system in phagocytic as well as tissue forming cells. It plays an essential role in intracellular defense of parenchymal cells and phagocytes against pathogenic bacteria by inserting into the bacterial surface to form pores. This model corresponds to a unique membrane bound P2 domain of MPEG1, which helps to stabilize the pre-pore state by swapping between monomers and enables MPEG1 to bind its targeted membrane.


Pssm-ID: 439345  Cd Length: 287  Bit Score: 459.04  E-value: 2.25e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784 347 HPGCTNVDSPNFNFQANMEDDSCDAKVTNFTFGGLYQECTELSGDA--LCQNLEQKNLLTGDFSCPSGYTPVHLLSqthe 424
Cdd:cd22579    1 HPGCTDPDSPNFNFQANVDDGSCEGPATNFTFGGVYQTCTGLSGDAgdLCQGLTQKNPLTGDFSCPAGYEPVLLLS---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784 425 EGYSRLECKKKCTLKIFCKTVCEDVFRVAKAQFRAYWCVATGQVPDNSGLLFGGLFTDKSINPMTNAQSCPAGYIPLNLF 504
Cdd:cd22579   77 GGYSVTECRKVCHSCWLFFTCCHDECAVSYATYTTYWCAATGPVPQNSGYLFGGLYTSKTVNPVTGSQSCPPYFYPLKLG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784 505 ESLKVCVSLDYELGYKFSVPFGGFFSCIMGNPLVNS---------DTAKDIGAPSLKKCPGGFSQHLAVISDGCQVSYCV 575
Cdd:cd22579  157 SDLKVCVSDDYELGSRYSVPFGGFFSCQSGNPLAGSlksnsagslKGYQDGPSSWPKRCPPGYSQHLATISDGCQVNYCV 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 172045784 576 KAGIFTGGSLLPVRLPPYTKPPLMSQVATNTVIVTSSETaRSWIKDPQTNQW 627
Cdd:cd22579  237 KAGSLSGGSLPPIRRPPFTPPPLLSVNATNTVLISGSGG-QSWVKNGSSNQW 287
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
125-341 5.96e-38

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: 140.23  E-value: 5.96e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784  125 VNGKFSTEFQRM--KTLQVKDQAVTTRVQVRNRIYTVKNSPTSELSFGFTNALMDICDQLEKNQTKMAtylaELLVLNYG 202
Cdd:pfam01823   1 GSFSASSEFKKMsdKSKQKKKSLIISKSTCSLYQFTLKRSNKLQLSDEFLQALSDLPDNYDYAAKATY----IQFFDKYG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784  203 THVITSVDAGAALVQEDHIRSSFLLDNQNSENT----VTASAGIAFLNiVNFKVETDHTSQTLLTKSYLSNRTNSRVQSF 278
Cdd:pfam01823  77 THYITSVTLGGKIVYVLKLDKSQLEDLKLKGEDvkicLSASAGASIGS-VNLKGCSKNSSSTKEKKSFNQEIESSITLVI 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 172045784  279 GGIPF---YPGITLETWQKGITNHLVAIDRAGLPLHFFIKPdklpglpgglVKKLSKTVETAVRHY 341
Cdd:pfam01823 156 GGTPEsidDDSKTYSDWAESVKDNPMPIDFELTPISELLKG----------VPLKKENLRKALEEY 211
MACPF smart00457
membrane-attack complex / perforin;
146-343 1.35e-35

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 133.33  E-value: 1.35e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784   146 VTTRVQVRNRIYTVKNsPTSELSFGFTNALMDICDQLEKNqtkmatyLAELLVLNYGTHVITSVDAGAALVQEDHI-RSS 224
Cdd:smart00457   2 LVARDTVRNRLYSVKL-DELPLALEFLKALRDLPDTYNRG-------AYARFIDDYGTHYITSATLGGEYSLLLVLdKES 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045784   225 FLLDNQNSENTVTASAGiaFLNIVNFKVETDHTSQTLLTKSYLSNRT--NSRVQSFGG-IPFYP---------GITLETW 292
Cdd:smart00457  74 LERKGLTSEDISKCLAG--SSNSFAGSVSAEHCLQSSSYIKYLSTSLrrESHTQVLGGhVTVLCdllrgpssnSLDFSDW 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 172045784   293 QKGITNHLVAIDRAGLPLHFFIKPDKlpglpggLVKKLSKTVETAVRHYYT 343
Cdd:smart00457 152 AESVPNEPVLIDVSLAPIYELLPPNP-------ELSQKREALRQALRSYLK 195
 
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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