PMIP_MAGO7
ID PMIP_MAGO7 Reviewed; 812 AA.
AC A4RF25; G4NBT3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 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: 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 STRING; 318829.MGG_00487T0; -.
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; VVYCDLF; -.
DR OrthoDB; 642479at2759; -.
DR Proteomes; UP000009058; Chromosome 5.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:EnsemblFungi.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
DR Gene3D; 1.10.1370.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
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; PTHR11804; 1.
DR Pfam; PF01432; Peptidase_M3; 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
