ID   A0A3B3RSS1_9TELE        Unreviewed;       491 AA.
AC   A0A3B3RSS1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
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};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000021554.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000021554.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBUNIT: Homooligomer. {ECO:0000256|ARBA:ARBA00011182}.
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}.
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DR   AlphaFoldDB; A0A3B3RSS1; -.
DR   STRING; 1676925.ENSPKIP00000021554; -.
DR   Ensembl; ENSPKIT00000002194.1; ENSPKIP00000021554.1; ENSPKIG00000005899.1.
DR   GeneTree; ENSGT00390000007027; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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};
KW   Membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          346..417
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
FT   REGION          447..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   491 AA;  55279 MW;  77A6F560B5026547 CRC64;
     MFRFRVACLL RKPCNVSVLT GRAAPPGTEW RNYATGFCHA VPSGALRRRC AISTRCPAPP
     GTEWRNYAVC RTAPSGALWR HCAAITCRSV PSGAVRSKCT VFTRRSSPIG GELRHCTMGT
     CHLSTPIRHV PAIACQLLHT SSSCRAMPAP LLWLLVKPAQ RLVVIILGRS IGKWWRSLPP
     NRKEFLRQEA WRRRWYLAAV VSALLTLLAT FGLTHLDESP ITGRVRLLVF SREQFMELAN
     LTAEEMMEEF KESIISLEDP RHKAVEMVVK HLAQRNQDIA EMASMPWSVH VLDHPSTNAF
     VLPVSSVAFY QAISCVNDIQ LWEKNYIYIS CLHLMFSILF ECQLITVLLF DHPYSRKLET
     EADEVGLQLA AKACADVRGL PLFWQQMERE EQQNGNLELP EWLSTHPSHR NRSSRMERLI
     PQALELRASC NCPALPRLPP QLVVSGSVRP LEDGEGKQNA VTAKDPDHPP HPRCQRPLPH
     TGGQIPTRGR A
//