ID   PMIP_CHAGB              Reviewed;         778 AA.
AC   Q2HFL8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   24-JAN-2024, 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=CHGG_00986;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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; CH408029; EAQ92751.1; -; Genomic_DNA.
DR   RefSeq; XP_001220207.1; XM_001220206.1.
DR   AlphaFoldDB; Q2HFL8; -.
DR   SMR; Q2HFL8; -.
DR   STRING; 306901.Q2HFL8; -.
DR   GeneID; 4386396; -.
DR   VEuPathDB; FungiDB:CHGG_00986; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   InParanoid; Q2HFL8; -.
DR   OMA; ALMFEYM; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000001056; 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..37
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..778
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338578"
FT   ACT_SITE        558
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         557
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         561
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         564
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   778 AA;  87685 MW;  77933C763AF2F3D9 CRC64;
     MIRTVTRPRQ WQRWVYSSCL LQRAVPPAAA RQQPRFTTSH KANHFGYHQP IAPVTHAPIT
     REDDFVLRSV FDYPQFWQDF TSVPGGIPVG LFRNSFLKEP RGMLTFAYVS LKKARAVVAK
     VLAASSVTEY RLIVRDLDRL SDILCRVLDM ADFVRVTHPD PEIQQNASKA WESVYEYMNE
     LNTMTGLHDQ LATAMANPDV TVVWSEEEKT VAEVLKLDFT KSAVSLPQKY RDRFVQLSSE
     ISAVGSAFVQ EMAPEQETVV LPSSDLRGMD PVRARDLTRR GKVYLPTLSG EAVMALRTVH
     DADARKHIFY ASRTASRRSV QMLEYLMRLR SELASLSGFE SYGHLALRDR MMAKSPEAVD
     QFLRALVESN RPKAMQEMAE LLAEKQKAYP QTNSLDPWDK DYYSDIIRRP LRVAGRQGDL
     LSSYFSLGVP LVGETWHPDV RRLDVVSDTD GHVAVLYCDL FTRPNKSPNP AHFTLRCSRE
     IFASEMEEVW EQTQQSNQKS MFGSPELAAT DGMTFSRHGD SIKQLPTIAL VCDFPQPSKH
     GDQPALLSFL QLETLFHEMG HAIHSVLART SFQTVAGTRC ATDLAELPST LMEFFAADAA
     VLGQFARHHE TNEPLPYRMV AQKARQTRRF EALDTENQIV TAMFDQALHS PRAGEPGFDP
     TAIFHALQRT HSCAPPDPPG TSWPGFFGHL SGYGSVYYSY LFDRVLAQRV WDVVFKAGER
     RAALSRENGE KLKQSLLKWG GARDPWKCLA EALDDDRLAE GGEEAMALVG SWGSTKPR
//