ID   PMIP_USTMA              Reviewed;         889 AA.
AC   Q4PBS8; A0A0D1E1U7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 3.
DT   03-AUG-2022, entry version 95.
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=UMAG_02435;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003144; KIS69921.1; -; Genomic_DNA.
DR   RefSeq; XP_011388723.1; XM_011390421.1.
DR   AlphaFoldDB; Q4PBS8; -.
DR   SMR; Q4PBS8; -.
DR   STRING; 5270.UM02435P0; -.
DR   EnsemblFungi; KIS69921; KIS69921; UMAG_02435.
DR   GeneID; 23563181; -.
DR   KEGG; uma:UMAG_02435; -.
DR   VEuPathDB; FungiDB:UMAG_02435; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   InParanoid; Q4PBS8; -.
DR   OMA; VVYCDLF; -.
DR   OrthoDB; 642479at2759; -.
DR   Proteomes; UP000000561; Chromosome 5.
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..30
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..889
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338595"
FT   REGION          60..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        671
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         670
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         674
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         677
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   889 AA;  97799 MW;  7376E7069CBE7367 CRC64;
     MASTSKNAQR AAASVAHSYH VCLARRMSRL PTLLSNISAP AASKALDRYE SKRIHSRSFS
     SSLAAQRVQR PTSAGPILTN PISDHEKDND ELRSLFDAPP TSSSANHLRS SGPSTGLFEI
     PSLTSPQNFL VLAQQTLARA QLLVDRIDRA GSADASTAQG IKELKEVVRN LDRLSDLLCG
     VIDMAELVRN AHPDPEWAEA ANAAYEYLCG YMNVLNTHTG LYSVLKNILS IKEVAETLSK
     EATAVAQVFL RDFEKSGIHL PPAERERFVQ LSDEILVLGR GFLQDIAGND ASDDFARIAS
     AQADADKSDM VGLPTHWLED VNPTILKAVR ASAITDTDGL LTFSAADQPW VFQTLLKYAP
     DERARKVAFR AANYGSQAQV QRLERLLKAR AELATLTGAS SYAEMALGDK MAKEPQNVEE
     FLRALTKHHR PRASHDLDKL RRLKHNATVS EPAQNTRQST FNTNSTLPEF APWDRDMYTE
     QHFRSASLSN VQPLSPYLSV GSVFAGLSRL FSALYGIRFR ASMVAPGEVW SEGAGDVMKV
     EVLDESEGAR GTSGSAEGLI GTIYADLWSR EGKPGGAAHY TVRCSRRVDK DDEAGDFTYG
     RAEDGRVVRP QDLGGEGCGN PLQAPTFEQR ERPGRYQLPV VVLMCDFARP GNANQGPCLL
     GWHEVETLFH EMGHAIHSMI GRTSYHNVSG TRCATDFVEL PSILMEHFVS SPQVVHLLAR
     HHSTGASLPF EHLSSHLAAS KSLEGLDTYH QILLARLDQL YHSQLAASPS FSSTTTYSDL
     DRQMHLPGAP NLSYTEGAHP QVRFGHLFGY GSTYYSYLLD RVIASKVWNH LFANNPLDRY
     AGQVFKNQCL KYGGGKDPWH ILADVLNEDS VRQGDSRAMQ QVGKWGIEC