ID   PMIP_LODEL              Reviewed;         811 AA.
AC   A5E4V6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-MAY-2023, entry version 83.
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=LELG_04645;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC   NRRL YB-4239;
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; CH981530; EDK46464.1; -; Genomic_DNA.
DR   RefSeq; XP_001523832.1; XM_001523782.1.
DR   AlphaFoldDB; A5E4V6; -.
DR   SMR; A5E4V6; -.
DR   STRING; 379508.A5E4V6; -.
DR   GeneID; 5231285; -.
DR   KEGG; lel:LELG_04645; -.
DR   VEuPathDB; FungiDB:LELG_04645; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   InParanoid; A5E4V6; -.
DR   OMA; ALMFEYM; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000001996; 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; 2.
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..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..811
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338586"
FT   REGION          423..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..450
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        594
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         593
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         597
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         600
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   811 AA;  91934 MW;  E9995C8F9BF12958 CRC64;
     MRSGSRLSNY LVRLSGRVSF TQKRSLTNVK LPSNVNYERL KAAFDSDEHT LNGKNNNNEG
     KLFSKTALFQ GQKDGSASTG LFKNSYLTSP QGLVQFSKKS KLQAQTLVDE MTRDVLTHQG
     KLDYIKKLDQ LSDILCRTID VAEFIRVVHD DQKWVDAAQQ THEIIFEYMN QLNTNVELYA
     NLVKILEDKD LISQLSDEEI KVGEYLRQDF ERSGIHMDPQ SRDQFVSLTQ EISIMGSHFN
     NESSSLKSDW ISITSNEFSA IEDRFIQSEV MRASALYPGK KESGTYYIPL ASAIPYRIMI
     QCGSGNLRKK MWIGLHEASD EQVQVLNHFV AYRALLAKML GYDSYAHYQL EHKMAKKPEN
     VLSFLTNLQE NLKNSQVLKE LRALSALQQG YSLLSDEELI RQIKPWDRDF LLKSFEAKKL
     SSTENGEKAS TDTSTSTTTS TTTTDSTTTT ATFSNSTDSV AIKRLCEYFS IGTVIAGLSK
     LFSALYNISF VVEPTVKGEV WNEKRVRKLN VLNNSNGETM GYLYLDFCSP KVFPSHFTVV
     CLRQLNKAES VSEHGDMVQL SKDYQLPVVA LVCNFTSGNP TLLSLDQVDT IFHEMGHAMH
     SMIGRTQLHN LSGTRCATDF VEIPSVLMES FSKDPRVLSE IGCHYRTGEP VPINLLEQAQ
     SQRSALEACE TFVQSKMAML DQELHSKEIV ELLRQGLEAI NSTEIYHQVE RDLEIFADEW
     STWHGKFPHL FSYGAVYYSY LLDRAIANVL WQKLFAKDPW SRDAGIKYKE EILKWGGTKD
     PWACLADALQ MEELRKGDAH AMQIIGENSK L
//