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   16-JUN-2009, entry version 24.
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 (Septoria nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Phaeosphaeriaceae;
OC   Phaeosphaeria.
OX   NCBI_TaxID=13684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15;
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
RT   and EST analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- FUNCTION: Cleaves proteins, imported into the mitochondrion, to
CC       their mature size. While most mitochondrial precursor proteins are
CC       processed to the mature form in one step by mitochondrial
CC       processing peptidase (MPP), the sequential cleavage by MIP of an
CC       octapeptide after initial processing by MPP is a required step for
CC       a subgroup of nuclear-encoded precursor proteins destined for the
CC       matrix or the inner membrane (By similarity).
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal octapeptide as second
CC       stage of processing of some proteins imported into the
CC       mitochondrion.
CC   -!- COFACTOR: Binds 1 zinc ion (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
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DR   EMBL; CH445364; EAT76866.2; -; Genomic_DNA.
DR   RefSeq; XP_001805910.1; -.
DR   MEROPS; M03.006; -.
DR   GeneID; 5982840; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR001567; Pept_M3A_M3B.
DR   InterPro; IPR006025; Pept_M_Zn_BS.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Metal-binding; Metalloprotease;
KW   Mitochondrion; Protease; Transit peptide; Zinc.
FT   TRANSIT       1     29       Mitochondrion (Potential).
FT   CHAIN        30    790       Mitochondrial intermediate peptidase.
FT                                /FTId=PRO_0000338591.
FT   ACT_SITE    571    571       By similarity.
FT   METAL       570    570       Zinc; catalytic (By similarity).
FT   METAL       574    574       Zinc; catalytic (By similarity).
FT   METAL       577    577       Zinc; catalytic (By similarity).
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
//