ID   PMIP_PHANO              Reviewed;         790 AA.
AC   Q0TXL7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   24-JAN-2024, entry version 92.
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=SNOG_15771;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(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}.
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DR   EMBL; CH445364; EAT76866.2; -; Genomic_DNA.
DR   RefSeq; XP_001805910.1; XM_001805858.1.
DR   AlphaFoldDB; Q0TXL7; -.
DR   SMR; Q0TXL7; -.
DR   STRING; 321614.Q0TXL7; -.
DR   EnsemblFungi; SNOT_15771; SNOT_15771; SNOG_15771.
DR   GeneID; 5982840; -.
DR   KEGG; pno:SNOG_15771; -.
DR   VEuPathDB; FungiDB:JI435_157710; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   InParanoid; Q0TXL7; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IBA:GO_Central.
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..790
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338591"
FT   ACT_SITE        571
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"
FT   BINDING         574
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         577
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   790 AA;  89067 MW;  3E8AFBC2E8963A45 CRC64;
     MLKRLARNNS SPWICSRCLQ QSQRQRRFNS TFAATATARD HAPSALYGLS ASGKTDDDAL
     RKVFDNASFW ESFKRGTSNK KPSGIIGNKY LTHPDGFIDF VTVTIQRCNG VVEKVSRAET
     IEDFKYMVKD LDKLSDLLCR VIDLADFVRS THPNRQFQIM AVKAYHTVFQ YMNQLNTTPV
     LYDQLKKASD IPEVFESWTE EERIVARILM EDFARFGIGL DDATRQKLVD LSGEIAEVGS
     QFVEGMSPET PTLKFESKRL KGLDPNLAKA LTKWGETRIS TMHHEAQAVL RFVDDAEVRR
     ETYSAVRTAG SSTIARLEKM LKLRAELAQL SGYETFSHMT LENKMAKTPE AVNTFLKALY
     EDSRPSVLAD LHELMELKRG DAHQDNFPNR MNAWDKFYYT QKMLSTMEGA YKQRTADSLS
     AYFSVGTVLQ GISRLFDRLY GVRLVPQETQ PGEVWEDGVR RLDVISDTEG HIAVLYCDLF
     SRPGKTPNPA HFTLRCSREI LPAELEEMQH MPHRFSSPIE AATDGMSVSY NASRNSYFQL
     PTIALICDFS KPSSPRPTLL NIHDVRTLFH EMGHALHSIL GRTALQNVSG TRCATDIAEL
     PSVLMEHFAF DPSVLALYAR HWDTNAPLPL ALLENRLAID NRNGYSELES QILLAMLDQA
     YHSNLPLDPA FNSTSVYHNT YTRFASVPEP AGTRWQGFFG HLFGYGATYY SYLFDRAIAS
     RIWKGVFNEG RDGGSLDREK GELYKNEVLR WGGGRDGWVC LAGVLRDGKV GEGGEGAMRE
     VGKWGIDAGK
//