ID   PMIP_LEUGO              Reviewed;         760 AA.
AC   Q6VMB4;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 64.
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; Synonyms=MIP;
OS   Leucoagaricus gongylophorus (Leaf-cutting ant fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricaceae; Leucoagaricus.
OX   NCBI_TaxID=79220;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SAR 000701-1;
RX   PubMed=14761798; DOI=10.1016/j.fgb.2003.11.008;
RA   James T.Y., Kuees U., Rehner S.A., Vilgalys R.;
RT   "Evolution of the gene encoding mitochondrial intermediate peptidase and
RT   its cosegregation with the A mating-type locus of mushroom fungi.";
RL   Fungal Genet. Biol. 41:381-390(2004).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY338827; AAR22310.1; -; Genomic_DNA.
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   Gene3D; 1.10.1370.10; -; 2.
DR   Gene3D; 3.40.390.10; -; 1.
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; PTHR11804; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW   Transit peptide; Zinc.
FT   TRANSIT         1..19
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..760
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000343202"
FT   ACT_SITE        544
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         543
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         547
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   760 AA;  85580 MW;  66EDF1623874E4A1 CRC64;
     MLARSVRTLV VSPKTVFRFR GCLFEKHVST ASADDRAIVS LFDSPHAAFK YPSTISTGLF
     GHSQLSHPNA FISLAEATLV RAQLLTDRIL RARSSRDELL KVVKNLDRLS DMLCSVIDLA
     ELIRNAHPDR NWATAGHHVY EQLCEFMNVL NTHVGLYEVL KLVLADASIV KTLSPEAYQT
     ALIFWRDFEK SAINLPPEER QKFVSLSSDI LVLGREFLEN ANAPRPPASI KPEHMVGIKD
     KGLGVRLQLQ AQFTRRDLLV YPGSLQAQMI MRSAPDEEPR RRMYIAANSS TDQQIXTLER
     LLKTRAELAR LVGRSSFAHM TLDDKMAKTP ENVMNFLGAL IGQTRPFARR ALKTLSARKQ
     AHHGLSSLPT IQAWDRDFYC PPEPPAPPIP LPPLTLGTIF MGLSRLFKYL YGITLRPTEA
     QTGEVWHSDV HKLEVIDEDK GLIGWIYADL FARHGKSSGA AHYTVRCSRR TDLDDDLGDG
     GLTGHEELIQ QNLEFEKVKR HKIPNQDGVY QLPLVVLLCE FTRPSVLKGA TVLEWHDVMT
     LFHEMGHAML AMVGRTEYQN VSGTRCATDF VELPSILMEH FLSSPVVLSL FDLDGTHSLR
     QVGNTHEDPC HSIDTFSQII LASLDQIYHS PAVLDNSTFS TTDELENLTV SKGVIPHVPS
     TSFQTQFGHL FGYGATYYSY LFDRAIASRV WKKVFEKDPL KREVGEKYKL EVLRWGGGRD
     PWKMVSKLLD ASELEKGDAE AMREVGRWRI EDEVGLPGRH