ID   PMIP_ASPFC              Reviewed;         801 AA.
AC   B0Y7Q2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-MAY-2023, entry version 76.
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=AFUB_074600;
OS   Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS   fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 144.89 / FGSC A1163 / CEA10;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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DR   EMBL; DS499599; EDP49433.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y7Q2; -.
DR   SMR; B0Y7Q2; -.
DR   EnsemblFungi; EDP49433; EDP49433; AFUB_074600.
DR   VEuPathDB; FungiDB:AFUB_074600; -.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   PhylomeDB; B0Y7Q2; -.
DR   Proteomes; UP000001699; 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   CDD; cd06457; M3A_MIP; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR033851; M3A_MIP.
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:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW   Transit peptide; Zinc.
FT   TRANSIT         1..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..801
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338570"
FT   ACT_SITE        565
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         564
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"
FT   BINDING         571
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   801 AA;  89667 MW;  4EAE66D5ECCD8269 CRC64;
     MKDQLLVPLR RRPWTCQKCL QRLQLPRHQT RRSFETAASP FPRPLDSLPA DYARTKTVDD
     DTLRRVFDSQ QFWREFSQQR AAQPKPTGLV QNQYLTSPDG FRTFANVSLQ KCQAIVSKVL
     AASTLEEYRT MARDLDRLSD LLCRVIDLSD FIRVIHPDPQ VQEAATQAYA LMFEYMNVLN
     TTTGLNDQLK KAAANPEVTS QWSDEEKIVA QILIKDFSNS AIHMPPHERQ RFVNLSNDIS
     QLGSSFVNGA EPAKSHVSVA TNNLRGLDPI LVQQIKRWNR TAAVPTTGMI PRLALRSVHD
     ENVRREVYLA SRTSSKRQLH RLEELLLKRA ELAKLSGYES FAHMTLSDKM AKSPEAVSNF
     LTALVESNRK LVREELSQLQ VMKGAPLQPW DHAYYVHQRV LQYSQARRSR ELSAVPEFFS
     LGTVMQGLSR LFDRLYGVRL VPQEPAPGET WNPDVRRLDV VDEAGRHIAV IYCDLFSRPN
     KHPNPAHFTL RCSREISAEE VAECASLDQS SHPNDGMATA VDPVTQTLRQ LPTIALVCDF
     PEPGTNGGGR PSLLSEHSVR TLFHEMGHAV HSILGQTRLQ SISGTRCATD FAELPSVLME
     HFATAPSVLA LYARHWRTDE PLSEGMIRSM ERDRTAHGSI YGAVENEAQI LMALVDQAYH
     SRPADGGRID STALYQQVSQ QHSSLPEPAD ATTPPTSWQG FFGHLYGYGA TYYSYIFDRA
     IANKLWVDVF GAGRHAVDRA AGERYKNEVL RWGGGRSGWE CVAGALGSAN ESNADGRLVE
     GGDQAMREVG RWGLGRDGVS G
//