ID   PMIP_BOTFB              Reviewed;         762 AA.
AC   A6SHZ5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   22-FEB-2023, entry version 74.
DE   RecName: Full=Mitochondrial intermediate peptidase;
DE            Short=MIP;
DE            EC=3.4.24.59;
DE   AltName: Full=Octapeptidyl aminopeptidase;
DE   Flags: Fragment;
GN   Name=oct1; ORFNames=BC1G_12067;
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10;
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=EDN33764.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CH476940; EDN33764.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001549090.1; XM_001549040.1.
DR   AlphaFoldDB; A6SHZ5; -.
DR   SMR; A6SHZ5; -.
DR   GeneID; 5429605; -.
DR   KEGG; bfu:BCIN_11g05560; -.
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; Zinc.
FT   CHAIN           <1..762
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338575"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT   BINDING         550
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   NON_TER         1
SQ   SEQUENCE   762 AA;  85181 MW;  383090D54BF577B9 CRC64;
     RRLATASTQY RESRPVPVDN SAPGAKRDDR TLRQIFDSPN FWAEFSQSSK QSYNRPAVGL
     FQNRYLVNPQ GFEVFANTSL RKAQRIVDKV LSASTVEEYR HVARELDRLS DLLCRVIDLS
     DFVRATHPNA AIQAAASRAY AKMFEYMNIL NTTTGLDKQL EIAMATPEIV AGWTEEEVVV
     ADILRKDFAK SAIDLPRAQR ERFVALSQEI SEIGPEFVDY MTPAKPYLTF ESSKLKGMDP
     VLVRQYTTWG QTKIPTIGGA AAAAIRSVQN EDVRKEIFMA TRTASRNTVY KLEELMRKRA
     ELAKLSRYES YSHLALGDKM AKSPASVSQF LEALSKDNNQ IVEGEVSELL KFKMSNSHGS
     SPGLQPWDKD YYMSQILASV RSHSRNSDFL SAYFSLGTVM QGLSRLFTRL YGVRLAPHET
     MPGETWNSDV RRLDVISETD GHVAVLYCDL FSRPGKSPNP AHFTLRCSRE ITTPELEEAS
     SLSQNGLFKT NEEAANDGMA TSRASGVLKQ LPTIALICDF VTMSGKSSRP ALLSFNEVQT
     LFHEMGHAIH SILGRTSLQN VSGTRCATDF AELPSVLMEH FAADPSVLSL FARHYETDQP
     LPYEMVAEKL ALDKRFEGSD TENQIILSML DLAYHSDLPL SPSFSSTQIY HSLQQKHGAL
     PVDPPGTCWQ GFFGHLFGYG STYYSYLFDR VLARRIWQVV FKDGEAGGSI QRDNGEKMKE
     EVLKWGGGRD PWKCLAGVLD DGRVENGDEK AMAIVGSWGV KE
//