ID   PMIP_COCIM              Reviewed;         795 AA.
AC   Q1E8M9; J3KIK8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=CIMG_01084;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
CC   -!- FUNCTION: Cleaves proteins, imported into the mitochondrion, to their
CC       mature size. While most mitochondrial precursor proteins are processed
CC       to the mature form in one step by mitochondrial processing peptidase
CC       (MPP), the sequential cleavage by MIP of an octapeptide after initial
CC       processing by MPP is a required step for a subgroup of nuclear-encoded
CC       precursor proteins destined for the matrix or the inner membrane (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal octapeptide as second stage of
CC         processing of some proteins imported into the mitochondrion.;
CC         EC=3.4.24.59;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M3 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GG704911; EAS35730.3; -; Genomic_DNA.
DR   RefSeq; XP_001247313.1; XM_001247312.1.
DR   AlphaFoldDB; Q1E8M9; -.
DR   SMR; Q1E8M9; -.
DR   STRING; 246410.Q1E8M9; -.
DR   EnsemblFungi; EAS35730; EAS35730; CIMG_01084.
DR   GeneID; 4567355; -.
DR   KEGG; cim:CIMG_01084; -.
DR   VEuPathDB; FungiDB:CIMG_01084; -.
DR   InParanoid; Q1E8M9; -.
DR   OMA; VVYCDLF; -.
DR   OrthoDB; 642479at2759; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1370.10; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804; PTHR11804; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW   Reference proteome; Transit peptide; Zinc.
FT   TRANSIT         1..22
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..795
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338579"
FT   ACT_SITE        562
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         561
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         565
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         568
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   795 AA;  89923 MW;  168DA75ECA56482F CRC64;
     MLKTLNRRSW TCRQCIRILR RNAETRRYFQ GASAASPLCQ HTVSSSTSDK ARDDQTLRLI
     FDSEPFWREF SQPKSSTSKR TGLLQNQYLT GPDGFLQFAQ VSLQKCQKIV AKVIAASTLE
     DYRGMVRDLD RLSDLLCRVI DMAEFMKLNH PSPQIQDAAT QAYALMFEYM NVLNTTPELD
     AQLKRASADL NVTSHWSPEE KVAARVLLKD FSQSAIHLPP KDRQKFVALS NEISQLGPMF
     VTNRQPETDH VTVDKNKLRG MDPSLIQQLQ RWRKVAVPMF GDIPRIALYS VHDEETRKEI
     YVTSRTSSKV QIRRLETLLQ KRAELAKLAG FPSYAHMTLS DKMAKTPEAV VNFLEALNAS
     NRGQVQDELS QLLALKQADV PSATQLQPWD HAYYVHQYSA RHSRVRRSRE STLLPAFFSI
     GTVIQGLSRL FTRLYGIRLV PTETLPGEIW NPDVRRLDVV DESDRRLAVI YCDLFTRPYK
     SPNPTHFTLR GSREISQAEI AECADLSSSL HPNDGMATTI KPETNKLYQL PTVALICDFD
     QSESRSTPSL LNEHNLETLF HEMGHAVHSV LARTDLQTIS GTRCATDFVE LPSVIMENFA
     TAPEVLALYA RHWETNEPLP EHMVKSMELN RQSRVSMHGG MDNEVQILMA LLDQAYHSSR
     PLEPNFDSTR IYHDVYSTHS SLPDPPGSRT SWQGYFAHLV GYGATYYSYL FDRAIANKVW
     SDVFKGGELS TNRDAGERFK NEVLRWGGGR DGWNCVAGLL GNNPANDNGK LAEGGEEAMR
     EVGRWGLGLM GTSEL