ID   PMIP_PYRO7              Reviewed;         812 AA.
AC   A4RF25; G4NBT3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   02-SEP-2026, entry version 102.
DE   RecName: Full=Mitochondrial intermediate peptidase;
DE            Short=MIP;
DE            EC=3.4.24.59;
DE   AltName: Full=Octapeptidyl aminopeptidase;
DE   Flags: Precursor;
GN   Name=OCT1; ORFNames=MGG_00487;
OS   Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Magnaporthe 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: Cleaves proteins, imported into the mitochondrion, to their
CC       mature size. While most mitochondrial precursor proteins are processed
CC       to the mature form in one step by mitochondrial processing peptidase
CC       (MPP), the sequential cleavage by MIP of an octapeptide after initial
CC       processing by MPP is a required step for a subgroup of nuclear-encoded
CC       precursor proteins destined for the matrix or the inner membrane (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal octapeptide as second stage of
CC         processing of some proteins imported into the mitochondrion.;
CC         EC=3.4.24.59;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M3 family. {ECO:0000305}.
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DR   EMBL; CM001235; EHA48991.1; -; Genomic_DNA.
DR   RefSeq; XP_003718575.1; XM_003718527.1.
DR   AlphaFoldDB; A4RF25; -.
DR   SMR; A4RF25; -.
DR   FunCoup; A4RF25; 653.
DR   STRING; 242507.A4RF25; -.
DR   EnsemblFungi; MGG_00487T0; MGG_00487T0; MGG_00487.
DR   GeneID; 2674708; -.
DR   KEGG; mgr:MGG_00487; -.
DR   VEuPathDB; FungiDB:MGG_00487; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   InParanoid; A4RF25; -.
DR   OMA; ALMFEYM; -.
DR   OrthoDB; 17530at2759; -.
DR   Proteomes; UP000009058; Chromosome 5.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006518; P:peptide metabolic process; IEA:TreeGrafter.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd06457; M3A_MIP; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR033851; M3A_MIP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW   Reference proteome; Transit peptide; Zinc.
FT   TRANSIT         1..35
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..812
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338587"
FT   REGION          518..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        588
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         587
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         591
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         594
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   812 AA;  90362 MW;  ADBC3C60189F33E9 CRC64;
     MLKLLRPRPW VCNSCLNRVA FPKPYPVGSR STRWLSTAQS AAPAVSIPPV NPVPADHTTS
     GTHDDALLGK IFDCSSAWRD FSARSAKFPT ENAGLFRNAY LTSPDGFLTF AQSSLSKASA
     IVNRVLGAST IEEYKTIVRD LDRLSDLLCR VIDLSDFVRV THPDVRIQRA ASEAWYMVYQ
     YMNQLNTMTG LNDQLGKAME NSDVTKTWSE EEMAVAQLLK LDFMKSAVNL PQAARDRFVD
     LSQRISEIGS DFVNEMAPEQ RRVVLPSSKF QGMDPQIARR FTKHGYMQLP TMSGEAAAAL
     RTVHDEETRK AVYLAIRTAS SRSVGLLEAL LKHRAELADL AGFESYGHMT LRDRMMAKTP
     ESINKFLVEL SKNNAPRVLQ EVDSLLQEKK TLLASPSATL NPWDREYYIQ RIRNAQGKNV
     KHDNFFASYF SVGRVMQGLS RLFTRLYGIR FVPRETLPGE KWHPDVRRLD VVSDTDGHVA
     VLYCDLFYRE DKSPNPAHFT IRCSRAISED EISEAAVSTS EGGPAFGSPE SAANDGMAAS
     RGASGGPLKQ LPTIALVCDF PQRDNPLSGS KSKPASLTFA SLETLFHEMG HAIHSVLART
     SFQNVAGTRC ATDLAELPST LMEYFASDPS VLSLFARHAE TDEPLDYDLL AERVRSRGRF
     EGCDTDYQII LAMLDQAYHS PLASSESFDT TRAYHDLQRE HSPLGPDPSS TRWQGFFGHL
     FGYGSTYYSY LFDQVLAERA WKKVFSSGQD GAALSREAGE HLKESLLKWG GSREPWRCVS
     DVLRDERIAG GGEEAMALVG SWGTSNKSTM KH
//