ID   PMIP_USTMA              Reviewed;         863 AA.
AC   Q4PBS8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   16-JUN-2009, entry version 28.
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=UM02435;
OS   Ustilago maydis (Smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=5270;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T.,
RA   Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O.,
RA   Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J.,
RA   Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J.,
RA   Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W.,
RA   Guzman P., Farman M.L., Stajich J.E., Sentandreu R.,
RA   Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA   Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M.,
RA   Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA   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.,
RA   Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W.,
RA   Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K.,
RA   Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen
RT   Ustilago maydis.";
RL   Nature 444:97-101(2006).
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; AACP01000083; EAK83473.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_758582.1; -.
DR   MEROPS; M03.006; -.
DR   GeneID; 3630533; -.
DR   KEGG; uma:UM02435.1; -.
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     40       Mitochondrion (Potential).
FT   CHAIN        41    863       Mitochondrial intermediate peptidase.
FT                                /FTId=PRO_0000338595.
FT   ACT_SITE    645    645       By similarity.
FT   METAL       644    644       Zinc; catalytic (By similarity).
FT   METAL       648    648       Zinc; catalytic (By similarity).
FT   METAL       651    651       Zinc; catalytic (By similarity).
SQ   SEQUENCE   863 AA;  95030 MW;  88FF232FA6308458 CRC64;
     MSRLPTLLSN ISAPAASKAL DRYESKRIHS RSFSSSLAAQ RVQRPTSAGP ILTNPISDHE
     KDNDELRSLF DAPPTSSSAN HLRSSGPSTG LFEIPSLTSP QNFLVLAQQT LARAQLLVDR
     IDRAGSADAS TAQGIKELKE VVRNLDRLSD LLCGVIDMAE LVRNAHPDPE WAEAANAAYE
     YLCGYMNVLN THTGLYSVLK NILSIKEVAE TLSKEATAVA QVFLRDFEKS GIHLPPAERE
     RFVQLSDEIL VLGRGFLQDI AGNDASDDFA RIASAQADAD KSDMVGLPTH WLEDVNPTIL
     KAVRASAITD TDGLLTFSAA DQPWVFQTLL KYAPDERARK VAFRAANYGS QAQVQRLERL
     LKARAELATL TGASSYAEMA LGDKMAKEPQ NVEEFLRALT KHHRPRASHD LDKLRRLKHN
     ATVSEPAQNT RQSTFNTNST LPEFAPWDRD MYTEQHFRSA SLSNVQPLSP YLSVGSVFAG
     LSRLFSALYG IRFRASMVAP GEVWSEGAGD VMKVEVLDES EGARGTSGSA EGLIGTIYAD
     LWSREGKPGG AAHYTVRCSR RVDKDDEAGD FTYGRAEDGR VVRPQDLGGE GCGNPLQAPT
     FEQRERPGRY QLPVVVLMCD FARPGNANQG PCLLGWHEVE TLFHEMGHAI HSMIGRTSYH
     NVSGTRCATD FVELPSILME HFVSSPQVVH LLARHHSTGA SLPFEHLSSH LAASKSLEGL
     DTYHQILLAR LDQLYHSQLA ASPSFSSTTT YSDLDRQMHL PGAPNLSYTE GAHPQVRFGH
     LFGYGSTYYS YLLDRVIASK VWNHLFANNP LDRYAGQVFK NQCLKYGGGK DPWHILADVL
     NEDSVRQGDS RAMQQVGKWG IEC
//