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ATP23_MAGO7
ID   ATP23_MAGO7             Reviewed;         273 AA.
AC   A4RF31; G4NBU0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Mitochondrial inner membrane protease ATP23;
DE            EC=3.4.24.-;
GN   Name=ATP23; ORFNames=MGG_00480;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- FUNCTION: Has a dual role in the assembly of mitochondrial ATPase. Acts
CC       as a protease that removes N-terminal residues of mitochondrial ATPase
CC       CF(0) subunit 6 at the intermembrane space side. Also involved in the
CC       correct assembly of the membrane-embedded ATPase CF(0) particle,
CC       probably mediating association of subunit 6 with the subunit 9 ring (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC       protein; Intermembrane side. Note=Associates loosely with the inner
CC       membrane. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M76 family. {ECO:0000305}.
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DR   EMBL; CM001235; EHA48998.1; -; Genomic_DNA.
DR   RefSeq; XP_003718582.1; XM_003718534.1.
DR   AlphaFoldDB; A4RF31; -.
DR   STRING; 318829.MGG_00480T0; -.
DR   MEROPS; M76.002; -.
DR   PRIDE; A4RF31; -.
DR   EnsemblFungi; MGG_00480T0; MGG_00480T0; MGG_00480.
DR   GeneID; 2674715; -.
DR   KEGG; mgr:MGG_00480; -.
DR   VEuPathDB; FungiDB:MGG_00480; -.
DR   eggNOG; KOG3314; Eukaryota.
DR   HOGENOM; CLU_079125_0_0_1; -.
DR   InParanoid; A4RF31; -.
DR   OMA; VDHLACT; -.
DR   OrthoDB; 1288109at2759; -.
DR   Proteomes; UP000009058; Chromosome 5.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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; IPR019165; Peptidase_M76_ATP23.
DR   PANTHER; PTHR21711; PTHR21711; 1.
DR   Pfam; PF09768; Peptidase_M76; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Membrane; Metal-binding; Metalloprotease; Mitochondrion;
KW   Mitochondrion inner membrane; Protease; Reference proteome.
FT   CHAIN           1..273
FT                   /note="Mitochondrial inner membrane protease ATP23"
FT                   /id="PRO_0000330066"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         170
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   273 AA;  31660 MW;  DEB457D990FBE0C3 CRC64;
     MASPQDNTPS GATPKPQTHE ETPDQVKLRI NGGERLNIRK NNPAETGFDP ATSKWVNYFK
     VLTGSMTKEG QFHYREHLYR TNEERDLRRC EEQRDWLFRY SPVVRYMRDQ IRLLGGELDA
     DNVVCRRCPS RLTADGRILG QAGGFSPQHG ILVCANSIRD RKHLEDTLAH EMVHAYDHLR
     WQVDFVGEKD LRHAACTEIR ASMLSGECRW TREAFGRGNW TVTQQFQNCV RSRAIMSVRA
     RARCRDTEHA TKVVNQVWDS CFSDTRPFDE IYK
 
 
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