ID   A0A091J1V8_EGRGA        Unreviewed;       472 AA.
AC   A0A091J1V8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
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};
DE   Flags: Fragment;
GN   ORFNames=Z169_03047 {ECO:0000313|EMBL:KFP13813.1};
OS   Egretta garzetta (Little egret).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX   NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP13813.1, ECO:0000313|Proteomes:UP000053119};
RN   [1] {ECO:0000313|EMBL:KFP13813.1, ECO:0000313|Proteomes:UP000053119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP13813.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KK501293; KFP13813.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091J1V8; -.
DR   STRING; 188379.A0A091J1V8; -.
DR   MEROPS; M48.017; -.
DR   Proteomes; UP000053119; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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};
KW   Membrane {ECO:0000256|SAM:Phobius};
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   Reference proteome {ECO:0000313|Proteomes:UP000053119};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        156..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          224..412
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
FT   REGION          448..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         472
FT                   /evidence="ECO:0000313|EMBL:KFP13813.1"
SQ   SEQUENCE   472 AA;  53688 MW;  4864D15F7C76E1C3 CRC64;
     MNIICGLKLP GRNCIFFHLA SLTKHGKCNN LYSSRGLRCL LNVPNTEVYK NAHHSSGRLC
     FQSSLPLGEK ITSLQISSVG QLLHNFSAWN IQIIRSFHTT PSVQAAPVPL FWIIVKPAQK
     LFAIILGRSI RNWWKALPPN KRELFKESAR KNKWKILLGV SSLGVLFVVF YFTHLEETPI
     TGRARLLVFG KEHFRELSQM EYDMWMEEFK SKMLPETDAR YQVVERVVGH LSESNKDIPQ
     VSVLKWVIHV VDEPGVNAFV LPNGQVFVFT GLLNAVSDIH QLSFILGHEI AHAVLEHAVK
     KASLVHFLDF LSLIFLTMIW AICPRDSLAV VGQWIQSKLQ EFVFDRPYSR TLEAEADKVG
     LQFAAKACVD VRASSVFWQQ MELAETIQGQ PKLPEWLSTH PSHENRAEHL DRLIPEALKI
     RESCNCPSLS GPDPRLIFKL NMQHLLESSK DQEPPNSTKQ DLSKQKLDVP HT
//