ID   PMIP_SCLS1              Reviewed;         785 AA.
AC   A7E7L8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   03-AUG-2022, entry version 75.
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=SS1G_01296;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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   -!- SEQUENCE CAUTION:
CC       Sequence=EDN96370.1; Type=Erroneous initiation; Evidence={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; CH476622; EDN96370.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001597102.1; XM_001597052.1.
DR   AlphaFoldDB; A7E7L8; -.
DR   SMR; A7E7L8; -.
DR   STRING; 665079.A7E7L8; -.
DR   GeneID; 5493674; -.
DR   KEGG; ssl:SS1G_01296; -.
DR   VEuPathDB; FungiDB:sscle_01g009890; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   InParanoid; A7E7L8; -.
DR   Proteomes; UP000001312; 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   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   Gene3D; 1.10.1370.10; -; 1.
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   Reference proteome; Transit peptide; Zinc.
FT   TRANSIT         1..27
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..785
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338594"
FT   REGION          26..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        567
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         566
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"
FT   BINDING         573
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   785 AA;  87723 MW;  22354DF6D7047D4F CRC64;
     MLKAVMPRPW VCSRCVKRQI QSSRGLATAS TQYREPRPVP TDHSAPGAKH DDRTLRQIFD
     SPDFWADFSQ SSKQSYYRPG VGLFQNRYLV NPQGFEVFAN TSLRKAQRIV DKVLKASTVE
     EYRHVARDLD RLSDLLCRVI DLSDFVRATH PNAAIQAAAS RAYAKMFEYM NILNTTTGLD
     KQLEVAMGTP EIVAGWTEEE VVVADILKKD FAKSAIDLPR AQREKFVALS QEISEIGPDF
     VDYMTPAKSY LTFESSKLKG MDPVLVREHT TWGQTKIPTI GGAAAAAIRT VQNEEVRREI
     FMATRTASRN TVHKLEELMR KRAELAKLSR YESYSQLALG DKMAKSPASV TQFLEALAKD
     NNKIVQGEVS ELLKFKFSNP NASSPGLQPW DKDYYMSRIL ASVRSHSRNS DFLSAYFSLG
     TVMQGLSRLF TRLYGVRLAP HETMPGETWN SDVRRLDVIS ETDGHVAVLY CDLFSRPGKS
     PNPAHFTLRC SREITTAELE EASMLSQNGL FKTDEEAAND GMATSKSSGV LKQLPTIALI
     CDFVTMSGKS SRPALLSFNE VQTLFHEMGH AIHSILGRTS LQNVSGTRCA TDFAELPSVL
     MEHFAADPSV LSLFARHYET DQQLPYEMVA EKLALDKRFE GSDTENQIIL SMLDLAYHSD
     LPLSPTFNST EIYHSLQQKH GALPVDPPGT CWQGFFGHLF GYGSTYYSYL FDRVLARRIW
     QVVFQGGEAG GSVHRGNGEK MKEEVLKWGG GRDPWKCLAG VLDDGRVENG DEKAMAIVGS
     WGVKE