ID   PMIP_NEOFI              Reviewed;         801 AA.
AC   A1DMR2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=NFIA_054290;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
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; DS027698; EAW16083.1; -; Genomic_DNA.
DR   RefSeq; XP_001257980.1; XM_001257979.1.
DR   AlphaFoldDB; A1DMR2; -.
DR   SMR; A1DMR2; -.
DR   STRING; 36630.CADNFIAP00004862; -.
DR   EnsemblFungi; EAW16083; EAW16083; NFIA_054290.
DR   GeneID; 4584495; -.
DR   KEGG; nfi:NFIA_054290; -.
DR   VEuPathDB; FungiDB:NFIA_054290; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   OMA; VVYCDLF; -.
DR   OrthoDB; 642479at2759; -.
DR   Proteomes; UP000006702; 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:0006879; P:cellular iron ion homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
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..42
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..801
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338589"
FT   ACT_SITE        566
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         569
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         572
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;  89774 MW;  906514456D11365F CRC64;
     MKDQLLVPLR RRPWTCRKCL QRLQLLPQHQ TRRSFETAAS PFPRQLDSLP ADYSRTKTVD
     DDTLRRVFDS QQFWREFSQQ RSAQPKPTGL VQNQYLTSPD GFRTFANVSL QKCQAIVSKV
     LAASTLEEYR TMARDLDRLS DLLCRVIDLS DFIRVIHPDP QVQEAATQAY ALMFEYMNVL
     NTTTGLNDQL KKAAANPEVT SQWSDEEKIV AQILIKDFSN SAIHMPPHER QRFVNLSNDI
     SQLGSSFVNG AEPAKSHVSV ATNNLRGLDP ILVQQIKRWN RTAAVPTTGM IPRLALRSVH
     DENVRREVYL ASRTSSKRQL HRLEELLLKR AELAKLSGYE SFAHMTLSDK MAKSPEAVSN
     FLTALVDSNR KLVREELSQL QAMKGAPLQP WDHAYYVHQR VMQYSQARRS RELSAVPEFF
     SLGTVMQGLS RLFDRLYGVR LVPQEPAPGE TWNPDVRRLD VVDESGRHIA VIYCDLFSRP
     NKHPNPAHFT LRCSREISTE EVAECASLDQ SSHPNDGMAT AVDPVTKTLR QLPTIALVCD
     FSEPGTNGGG RPSLLSEHSV RTLFHEMGHA VHSILGQTRL QSISGTRCAT DFAELPSVLM
     EHFATAPSVL ALYARHWRTD EPLSEGMIRS MERDRTAHGS IYGAVENEAQ ILMALVDQAY
     HSRPADGGRI DSTALYQQVS QQHSSLPEPA DVTPPTSWQG FFGHLYGYGA TYYSYIFDRA
     IANKLWVDVF GAGRQAVDRA AGERYKNEVL RWGGGRSGWE CVAGALGSAN ESNADGRLVE
     GGDEAMREVG RWGLGRDGVS G