ID   PMIP_NEUCR              Reviewed;         805 AA.
AC   Q7SDD5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   16-JUN-2009, entry version 36.
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=oct-1; ORFNames=NCU02063;
OS   Neurospora crassa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   Neurospora.
OX   NCBI_TaxID=5141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   MEDLINE=22598136; PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
RA   Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA   Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA   Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA   Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA   Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA   Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA   Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
RA   Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; AABX02000003; EAA34783.1; -; Genomic_DNA.
DR   RefSeq; XP_964019.1; -.
DR   MEROPS; M03.006; -.
DR   GeneID; 3880168; -.
DR   KEGG; ncr:NCU02063; -.
DR   NMPDR; fig|5141.1.peg.7186; -.
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     25       Mitochondrion (Potential).
FT   CHAIN        26    805       Mitochondrial intermediate peptidase.
FT                                /FTId=PRO_0000338590.
FT   ACT_SITE    579    579       By similarity.
FT   METAL       578    578       Zinc; catalytic (By similarity).
FT   METAL       582    582       Zinc; catalytic (By similarity).
FT   METAL       585    585       Zinc; catalytic (By similarity).
SQ   SEQUENCE   805 AA;  91095 MW;  8F2F597AB9BD2130 CRC64;
     MIQPLVKASR PRLWVCSDCL LRRTLSPLLR QQRRRFTGFT AHAPKTLTGT IPVTHKNGDT
     KHDDSLLRSI FDSPETWKQF SGDKHGRNVG LFRNAYLTSP HGFLDFAHVS LGKARALVDK
     VLNAQSLDEY RAIVRHLDRL SDILCRVLDM ADFVRVTHPD QQIQRTASMA WDMMYEYMNQ
     LNTMTGLYDQ LVQAMDNPQV STTWSEEERM VAEVLKLDFA KSAVHLPKDA RDKFVHLSSA
     ISQTGTNFIQ HMEPKIPYTT VEKSRMMGMD PVEVKRMASM GKVYVQTLSP QASIALRTVR
     DDHARHQLFM ASRTASRRTV HTLEELMLLR GESAKLSGFE SYGHLVLHDR MMASTPESVR
     QFLQALSENT RPQAQQEVAD LTAAKRAHKG GDATLEPWDK DFYAESIRQA IKSRQKREDL
     SSYFSLGTVM QGLSRIFTRL YGIRFVPREP MPGETWHPDV RRLDVVSDVE GHVAVLYCDL
     FYRPLKSPNP AHFTLRCSRE LSPHEIAETA HTQAENPHVL IPSFESAEFA ANDGMAYSRS
     QDGAIKQLPT IALVCDFPQQ SHNRPALLSF FQLETLFHEM GHAIHSILAR TSFQNVSGTR
     CATDLAELPS TLMEYFAADP SVLALFARHY ETDNPLPYEW VDNKIREARR FEALDTENQI
     ILAMLDQELH SSKAVQGHID STEIFHSLQR QFSTAPPDPQ GTAWQGFFGH LVGYGSTYYS
     YLFDRVLAQR VWNVVFNSGQ GGAALQRENG ERLKENLLKW GGSKDPWKCL AGALKDERLE
     GGGEKAMKLV GSWGGQRGTK SDQAV
//