ID B3S3T1_TRIAD Unreviewed; 311 AA.
AC B3S3T1;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Metalloendopeptidase OMA1, mitochondrial {ECO:0000256|ARBA:ARBA00040360};
DE AltName: Full=Overlapping with the m-AAA protease 1 homolog {ECO:0000256|ARBA:ARBA00042978};
GN ORFNames=TRIADDRAFT_28764 {ECO:0000313|EMBL:EDV22520.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV22520.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV22520.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV22520.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003983};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}.
CC -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|ARBA:ARBA00038233, ECO:0000256|RuleBase:RU003983}.
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DR EMBL; DS985249; EDV22520.1; -; Genomic_DNA.
DR RefSeq; XP_002115064.1; XM_002115028.1.
DR AlphaFoldDB; B3S3T1; -.
DR STRING; 10228.B3S3T1; -.
DR EnsemblMetazoa; TriadT28764; TriadP28764; TriadG28764.
DR GeneID; 6756095; -.
DR KEGG; tad:TRIADDRAFT_28764; -.
DR CTD; 6756095; -.
DR eggNOG; KOG2661; Eukaryota.
DR HOGENOM; CLU_029002_6_0_1; -.
DR InParanoid; B3S3T1; -.
DR OMA; THNERSE; -.
DR OrthoDB; 5490879at2759; -.
DR PhylomeDB; B3S3T1; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR CDD; cd07331; M48C_Oma1_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003983};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT TRANSMEM 34..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 99..289
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDV22520.1"
SQ SEQUENCE 311 AA; 36001 MW; 256071D3D3DFF049 CRC64;
FCIPYFRIAK YWWNKLPTHK KHNYKRMLKR HQQVVYIIAL FGTGAGIYYI YNHIESVPLT
GRTRLMMLSH EHLQELGKML YDEQIQANGE HLLPTTSSQY HRVKSVVSRL IKNNGDIPQI
NTLHWEINII DSNEVNAFVL PDGQIFVYKG MLSTLGNDDA LAFLLGHEMA HALLSHAAEQ
LSFFNIFDLL AAVSLGLVWA LMPTDVVAAV THWFHNSIAS ICLHRPYSRK LEVEADLIGS
NLATKACYDV RAATYFWEML ANKDPSNAEL EWLSTHPSHQ KRADLIKERM TEVEYYTHLL
EYKVQKQRIY K
//