ID   PMIP_PICGU              Reviewed;         786 AA.
AC   A5DI46;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   24-JAN-2024, entry version 82.
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=PGUG_02947;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC   Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH408157; EDK38849.2; -; Genomic_DNA.
DR   RefSeq; XP_001485218.1; XM_001485168.1.
DR   AlphaFoldDB; A5DI46; -.
DR   SMR; A5DI46; -.
DR   STRING; 294746.A5DI46; -.
DR   GeneID; 5127052; -.
DR   KEGG; pgu:PGUG_02947; -.
DR   VEuPathDB; FungiDB:PGUG_02947; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   InParanoid; A5DI46; -.
DR   OMA; ALMFEYM; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
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..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..786
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338592"
FT   ACT_SITE        568
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         567
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         571
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         574
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   786 AA;  90517 MW;  784FAB0D1430E2E3 CRC64;
     MSSILLRSYR HHAKVWTRPS SKSSFIRSLA SRSNPTSSFE HVRRVFDDDK YYQDFNNGTL
     SRKIFSGPRT GLFKNEKLTT PQGLIDFSGQ CLTEAQTLVD TMIREAETSD QGKIHYIRRL
     DQLSDILCRV IDVAEFIRVA HPNSKWTHAA QQTHELMFEY MNQLNTNVQL HTILGNILAD
     KSITSKLSSE EIMVGEYLKQ DFERSGIYME PHTRENFVAL TQEISVLGSH FNNGIHELKD
     YWCEISQQEY EAIDNADLKR EIRRFQQKSP RSSRNSVYIP LAGSLPYSIL QRCSMESVRR
     KVWIALHNAS EEQISTLNLF LKYRATLSKM LGYESFAHYQ LEHKMAKNPE NVLTFLENLQ
     RKMVDGENSG LISELESLYA MSNHWKPGAS KSDIIHAIQP WDRDYLLHKL QEEKKETQLD
     DNISEYLSVG TIMSGLSQLF HSIYSIELLP EPSASGETWA SQVRKIKVFD NETQSTLGFL
     YLDFWSPNVL PSHFTIVCSR QLNKDLGEKV EVMKPLVQLD ETESHQLPVI SLVCNFHQGN
     SFIGRFAGLE TSKPTLLTLD QVDTIFHEMG HAMHSMIGRT KLQNLSGTRC STDFVELPSV
     LMESFSKDPR VLGRIARHYS TNELLPHDIL AKHQHYRNVL ENSETYMQSK MAMLDQVLHG
     KSIVKQLEMA RDDIDSTTMY HSLEKELKVF SDQWSTWHGK FPHLFSYGAV YFSYLFDRAI
     AEKIWKSLFQ NDPWSREAGT TYKEAILKWG GTRDPWHCLA DALSNQELSK GDEKAMRIIG
     GETKDL
//