ID   PMIP_ASPOR              Reviewed;         800 AA.
AC   Q2UN31;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-MAY-2023, entry version 95.
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=AO090001000525;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(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; AP007154; BAE57034.1; -; Genomic_DNA.
DR   RefSeq; XP_001819036.1; XM_001818984.1.
DR   AlphaFoldDB; Q2UN31; -.
DR   SMR; Q2UN31; -.
DR   STRING; 510516.Q2UN31; -.
DR   EnsemblFungi; BAE57034; BAE57034; AO090001000525.
DR   GeneID; 5991007; -.
DR   KEGG; aor:AO090001000525; -.
DR   VEuPathDB; FungiDB:AO090001000525; -.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   OMA; ALMFEYM; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000006564; Chromosome 2.
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..23
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..800
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338573"
FT   REGION          27..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        564
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         563
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
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         570
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   800 AA;  89243 MW;  474F93077541B66F CRC64;
     MAGHMLMPLR RRPWTCRACL QRLQQPRRSL ETAASPSSQS DVYDYAPTNH STQKKSNDET
     LRRVFDSQPF WREFSQRSAT QSKPTGLVQN QYLTNPDGFR AFANVSLQRC QAIVAKVLAA
     STLEEYRDMA RDLDRLSDLL CRVIDLSDFI RVIHPDPRVQ EAATQAYALM FEYMNVLNTT
     TGLNDQLKKA ASNPDVTSYW SEEEKIVAQI LIKDFSNSAI HMPPNERQRF VNLSNDISQL
     GSNFVNSAEP AKSQVVVGAN SLRGLDPILV QQIRRWNRTA SVPTTGMIPR LALRSVHDEG
     VRREVYLATR TSSSRQLHRL EELLSKRAEL AQLSGHASFG HMTLSDKMAK SPEAVSNFLT
     ALVGSNREYV QEELSKLQAM KGGSPLQPWD HAYYVHQRVL QYSQSRRSRE LSAVPEFFSL
     GTVMQGLSRL FDRLYGVRLV PQETAAGETW NPDVRRLDVV DEAERHIAVI YCDLFSRPNK
     HPNPAHFTLR CAREISSEEV AECATMDHSA HPNDGMATAV DPQSKTLRQL PTIALVCDFA
     EPPATGAGRP SLLSEHSVRT LFHEMGHALH SILGQTRLQS ISGTRCATDF AELPSVLMER
     FATEPAVLSM YARHWQTDQP LSESMMLSME KDRLAHGSIY GAVENEAQIL MALVDQAYHS
     IPADKAGQID STAIYHQVSS AHSTLPDPTD SRPPTSWQGF FGHLYGYGAT YYSYIFDRAI
     ANKIWEDVFQ AGKAAVDREA GERYKNEVLR WGGGRNGWDC VAGVLGSANA ANANGRLAEG
     GDEAMREVGR WGLGRDGVSG
//