ID   PMIP_ASPFU              Reviewed;         801 AA.
AC   Q4WMU9;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=AFUA_6G08640;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000006; EAL88715.1; -; Genomic_DNA.
DR   RefSeq; XP_750753.1; XM_745660.1.
DR   AlphaFoldDB; Q4WMU9; -.
DR   SMR; Q4WMU9; -.
DR   STRING; 746128.CADAFUBP00007267; -.
DR   MEROPS; M03.006; -.
DR   EnsemblFungi; EAL88715; EAL88715; AFUA_6G08640.
DR   GeneID; 3508040; -.
DR   KEGG; afm:AFUA_6G08640; -.
DR   VEuPathDB; FungiDB:Afu6g08640; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   InParanoid; Q4WMU9; -.
DR   OMA; VVYCDLF; -.
DR   OrthoDB; 642479at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IBA:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..801
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338571"
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;  89695 MW;  93D0BDC76A499FE0 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
     HFATVPSVLA LYARHWRTDE PLSEGMIRSM ERDRTAHGSI YGAVENEAQI LMALVDQAYH
     SRPADGGRID STALYQQVSQ QHSSLPEPAD ATTPPTSWQG FFGHLYGYGA TYYSYIFDRA
     IANKLWVDVF GAGRHAVDRA AGERYKNEVL RWGGGRSGWE CVAGALGSAN ESNADGRLVE
     GGDQAMREVG RWGLGRDGVS G