ID   PMIP_MALGO              Reviewed;         806 AA.
AC   A8QB25;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   22-FEB-2023, entry version 67.
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=MGL_3874;
OS   Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=425265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4612 / CBS 7966;
RX   PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA   Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA   Kronstad J.W., DeAngelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA   Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA   Chu L., Sears R., Yuan B., Dawson T.L. Jr.;
RT   "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT   virulence traits shared with plant and human fungal pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDP41872.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AAYY01000015; EDP41872.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001729086.1; XM_001729034.1.
DR   AlphaFoldDB; A8QB25; -.
DR   SMR; A8QB25; -.
DR   STRING; 425265.A8QB25; -.
DR   GeneID; 5853393; -.
DR   KEGG; mgl:MGL_3874; -.
DR   InParanoid; A8QB25; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000008837; 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..806
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338588"
FT   ACT_SITE        582
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         581
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         585
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         588
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   806 AA;  90373 MW;  C7156509B4D06706 CRC64;
     MLSRHLTVLR SACRVSHDLR VPSTQAVRKS AWSVCYSRRP LHISRSDAAS TAALDMGVAP
     AVEKDHEILK ELLDTRHSSG HVLSQGVPTG LFQIDHLRTP SDFLLLAQRT LIRCQLLVQR
     IARAIGNPSE LARVVRNLDR LSDMLCGVID MAELVRHAHP DQGWANAAND AYEYLCNYMN
     VLNTHTELYD ALRCVMETKD IYHSLSQEAQ AVAHIFMRDF EKSGIHLPPH ERNRFVELSD
     QIMILGRAFL QDMSTGTSDT IVEFPTDLLD GMDTSIFAQN LFRLRPSKSI PVVPGSWELH
     YISKYAPNPQ ARRLAYMISY TGRTQPVAVL EQLLHARYEL AKLTGKQSFA EMTLVDKMAG
     TPEHVLRFLR LLADAQRPVA QRMIAEFGQL KHALEGSSQV EIWDREYYAD AYLQRHHPSQ
     LAPLSPYLSL GSIFTGLSRL FYLLYGIHFR AAETLPGEVW HPDVLKLEVV DETESSVIGL
     IYCDLYTRDG KPPSAAHYTV RCSRRIDLDD THLDMELGAS ADLPPVADTE HLLGVKGATG
     FGRPGRFQQP VVVLMTDFAP PNIGHGGACL LRWHDVETLF HEMGHAIHSM IGRTEFHNVS
     GTRCATDFVE LPSILMEHFL TDPSVVALTA HHHRTGSPLP YVQLQKHLAT QRSLDALDTH
     QQILLASLDQ RYHSERAGAP TFSSSQELES LQADMGLFPP VSNATWQGQF GHLFGYGATY
     YSYLFDRAIA ARVWEQVFAK KPLSREAGER FKMEVLRHGG GKSPWEMLSR LLHEDKIADG
     NAGAMEAIGR WGLGQNQSNE TISAHL
//