ID   PMIP_CANGA              Reviewed;         761 AA.
AC   Q6FW88;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 35.
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; OrderedLocusNames=CAGL0D02112g;
OS   Candida glabrata (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   mitosporic Nakaseomyces.
OX   NCBI_TaxID=5478;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380950; CAG58417.1; -; Genomic_DNA.
DR   RefSeq; XP_445506.1; -.
DR   MEROPS; M03.006; -.
DR   GeneID; 2887167; -.
DR   KEGG; cgr:CAGL0D02112g; -.
DR   HOGENOM; Q6FW88; -.
DR   OMA; Q6FW88; AMGERYR.
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     37       Mitochondrion (Potential).
FT   CHAIN        38    761       Mitochondrial intermediate peptidase.
FT                                /FTId=PRO_0000338577.
FT   ACT_SITE    548    548       By similarity.
FT   METAL       547    547       Zinc; catalytic (By similarity).
FT   METAL       551    551       Zinc; catalytic (By similarity).
FT   METAL       554    554       Zinc; catalytic (By similarity).
SQ   SEQUENCE   761 AA;  87333 MW;  89CA8567A26EC72E CRC64;
     MLIQKILLNK EISRLPRILS ILNYTGLRWL SGSSGRNTTE LQRIFDDSKY WQSLSENTTQ
     YTKETGLFKN PYLTSTDGLR QFSHDSLHKA HKLAEILRNS VSKEEKVHYI MNLDQLSDTL
     CRVIDLCEFL RSAHPDQSYV EAAQMCHEEM FEFMNVLNTD VVLCNKLKEV LEDPEILKVL
     SEEERKVGEI LLDDFEKSGI YMKAGIREQF IELSQQISVI GQEFINNTDY VAKEFIKVKR
     DEMDKSGISP LLTARLNRDL TGKYYKIPTY GQIPLQILKS CPDEDIRKEV WAALHNCPKA
     QIQRLNQLVR LRVILSNLLG KQSYSDYQLD NKMAGSPENV KGFIKTLMNV TKPLAARELE
     FIARDKLNAP DSRHMSDNEI LSIVKPWDKN YFSSKYDSDN EMAMIRDEQL RYYFSLGNVI
     NGLSELFKRI YGITLQPSRT ENGETWSPDV RRLDVISEEE GLVGVIYCDL FERVGKISNP
     AHFTVCCSRQ VYPDENDFTT IQTGQNSDGT VFQLPVISLV CNFSTVALPN GNRTCFLHMN
     EIETLFHEMG HAMHSMLGRT RLQNISGTRC ATDFVELPSI LMEHFARDIR VLRTIGSHYE
     TSEPAPEALL NDYLDKTQFL QHCETYSQAK MAMLDQKLHG SFSLSDIERI DSAKIYQKLE
     TRLQVLADDE SNWCGRFGHL FGYGATYYSY LFDRAIASKV WDSLFKDDPF NRTGGEKFKE
     RVLKWGGLKN PWSCIADVLE KPDLAKGGAE AMTYIGDSED L
//