ID   PMIP_ASPTN              Reviewed;         802 AA.
AC   Q0CI79;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
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=ATEG_06605;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae;
OC   mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
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., Larson L., Luoma S.,
RA   White J., Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C.,
RA   Denning D.W., Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-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.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAU33149.1; Type=Erroneous gene model prediction;
CC       Sequence=EAU33149.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; CH476602; EAU33149.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001215783.1; -.
DR   MEROPS; M03.006; -.
DR   GeneID; 4322361; -.
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     24       Mitochondrion (Potential).
FT   CHAIN        25    802       Mitochondrial intermediate peptidase.
FT                                /FTId=PRO_0000338574.
FT   ACT_SITE    566    566       By similarity.
FT   METAL       565    565       Zinc; catalytic (By similarity).
FT   METAL       569    569       Zinc; catalytic (By similarity).
FT   METAL       572    572       Zinc; catalytic (By similarity).
SQ   SEQUENCE   802 AA;  89472 MW;  3E92F4BA281CEB5F CRC64;
     MGGPKLLMPL RPRPWTCRTC LQRLHSARRS LKTAASPSPQ STSFEYNRSA HNTQKSTTDD
     ETLRRVFDSP SFWKEFSQRS SLHTKPTGLV QNQYLTSPEG FRTFANVSLH KCQAIVHKVL
     AASTLEEYRD MARDLDRLSD LLCRVIDLSD FIRVIHPDPQ VQEAATQAYA LMFDYMNVLN
     TTTGLNDQLK KAAANPDVTS HWSAEEKIVA QILIKDFSNS AIHMPPNERQ RFVNLSNEIS
     QLGSNFVNAA EPAKSHVVVG TNSLRGLDPL LVQQIKRWNR TASVPTMGMI PRLVLRSVHD
     EGVRKDVYLA TRTSSSRQIK RLEQLLAKRA ELAQLSGYAS FGHMTLSDKM AKSPEAVSNF
     LTSLVGSNRQ FVHEELAQLQ GMKGSSPLQA WDHAYYVHQR VMQYSQSRRS RELSIVPEFF
     SLGTVMQGLS RLFNRLYGVR LVPQETAPGE TWNPDVRRLD VVDEAERHIA VIYCDLFSRP
     NKHPNPAHFT LRCSREISNQ EVAECASMDQ SAHPNDGMAT AVDPQSKTLR QLPTIALVCD
     FPDPPATSAG RPSLLSEHSV RTLFHEMGHA LHSILGQTRL QSISGTRCAT DFAELPSVLM
     ERFATAPEVL SMYARHWQTD QPLSENMMRS MEQDRTAHGS IYGAVENEAQ ILMALVDQAY
     HSVPAEAAGK IDSTAIYHQV SQAHSSLPEP SDTQPPTSWQ GFFGHLYGYG ATYYSYIFDR
     AIANKLWEDV FQSGQASVDR NAGERYKNEV LRWGGGRNGW DCVAGVLGSG NPSNADGRLV
     EGGDDAMREV GRWGLGRDGV SG
//