ID   PMIP_CHAGB              Reviewed;         778 AA.
AC   Q2HFL8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
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=CHGG_00986;
OS   Chaetomium globosum (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae;
OC   Chaetomium.
OX   NCBI_TaxID=38033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / IFO 6347 / NRRL 1970;
RA   Birren B.W., Lander E.S., Galagan J.E., Devon K., Nusbaum C.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Kodira C.D.,
RA   Yandava C., Zeng Q., Alvarado L., Oleary S., Untereiner W.;
RT   "Annotation of the Chaetomium globosum CBS 148.51 genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; CH408029; EAQ92751.1; -; Genomic_DNA.
DR   RefSeq; XP_001220207.1; -.
DR   GeneID; 4386396; -.
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    778       Mitochondrial intermediate peptidase.
FT                                /FTId=PRO_0000338578.
FT   ACT_SITE    558    558       By similarity.
FT   METAL       557    557       Zinc; catalytic (By similarity).
FT   METAL       561    561       Zinc; catalytic (By similarity).
FT   METAL       564    564       Zinc; catalytic (By similarity).
SQ   SEQUENCE   778 AA;  87685 MW;  77933C763AF2F3D9 CRC64;
     MIRTVTRPRQ WQRWVYSSCL LQRAVPPAAA RQQPRFTTSH KANHFGYHQP IAPVTHAPIT
     REDDFVLRSV FDYPQFWQDF TSVPGGIPVG LFRNSFLKEP RGMLTFAYVS LKKARAVVAK
     VLAASSVTEY RLIVRDLDRL SDILCRVLDM ADFVRVTHPD PEIQQNASKA WESVYEYMNE
     LNTMTGLHDQ LATAMANPDV TVVWSEEEKT VAEVLKLDFT KSAVSLPQKY RDRFVQLSSE
     ISAVGSAFVQ EMAPEQETVV LPSSDLRGMD PVRARDLTRR GKVYLPTLSG EAVMALRTVH
     DADARKHIFY ASRTASRRSV QMLEYLMRLR SELASLSGFE SYGHLALRDR MMAKSPEAVD
     QFLRALVESN RPKAMQEMAE LLAEKQKAYP QTNSLDPWDK DYYSDIIRRP LRVAGRQGDL
     LSSYFSLGVP LVGETWHPDV RRLDVVSDTD GHVAVLYCDL FTRPNKSPNP AHFTLRCSRE
     IFASEMEEVW EQTQQSNQKS MFGSPELAAT DGMTFSRHGD SIKQLPTIAL VCDFPQPSKH
     GDQPALLSFL QLETLFHEMG HAIHSVLART SFQTVAGTRC ATDLAELPST LMEFFAADAA
     VLGQFARHHE TNEPLPYRMV AQKARQTRRF EALDTENQIV TAMFDQALHS PRAGEPGFDP
     TAIFHALQRT HSCAPPDPPG TSWPGFFGHL SGYGSVYYSY LFDRVLAQRV WDVVFKAGER
     RAALSRENGE KLKQSLLKWG GARDPWKCLA EALDDDRLAE GGEEAMALVG SWGSTKPR
//