ID   PMIP_ASPTN              Reviewed;         802 AA.
AC   Q0CI79;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   02-SEP-2026, 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=ATEG_06605;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- SEQUENCE CAUTION:
CC       Sequence=EAU33149.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAU33149.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CH476602; EAU33149.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001215783.1; XM_001215783.1.
DR   AlphaFoldDB; Q0CI79; -.
DR   SMR; Q0CI79; -.
DR   STRING; 341663.Q0CI79; -.
DR   EnsemblFungi; EAU33149; EAU33149; ATEG_06605.
DR   GeneID; 4322361; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   OrthoDB; 17530at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006518; P:peptide metabolic process; IEA:TreeGrafter.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd06457; M3A_MIP; 1.
DR   FunFam; 3.40.390.10:FF:000029; Mitochondrial intermediate peptidase 1; 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   Reference proteome; Transit peptide; Zinc.
FT   TRANSIT         1..24
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..802
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338574"
FT   REGION          28..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   802 AA;  89472 MW;  3E92F4BA281CEB5F CRC64;
     MGGPKLLMPL RPRPWTCRTC LQRLHSARRS LKTAASPSPQ STSFEYNRSA HNTQKSTTDD
     ETLRRVFDSP SFWKEFSQRS SLHTKPTGLV QNQYLTSPEG FRTFANVSLH KCQAIVHKVL
     AASTLEEYRD MARDLDRLSD LLCRVIDLSD FIRVIHPDPQ VQEAATQAYA LMFDYMNVLN
     TTTGLNDQLK KAAANPDVTS HWSAEEKIVA QILIKDFSNS AIHMPPNERQ RFVNLSNEIS
     QLGSNFVNAA EPAKSHVVVG TNSLRGLDPL LVQQIKRWNR TASVPTMGMI PRLVLRSVHD
     EGVRKDVYLA TRTSSSRQIK RLEQLLAKRA ELAQLSGYAS FGHMTLSDKM AKSPEAVSNF
     LTSLVGSNRQ FVHEELAQLQ GMKGSSPLQA WDHAYYVHQR VMQYSQSRRS RELSIVPEFF
     SLGTVMQGLS RLFNRLYGVR LVPQETAPGE TWNPDVRRLD VVDEAERHIA VIYCDLFSRP
     NKHPNPAHFT LRCSREISNQ EVAECASMDQ SAHPNDGMAT AVDPQSKTLR QLPTIALVCD
     FPDPPATSAG RPSLLSEHSV RTLFHEMGHA LHSILGQTRL QSISGTRCAT DFAELPSVLM
     ERFATAPEVL SMYARHWQTD QPLSENMMRS MEQDRTAHGS IYGAVENEAQ ILMALVDQAY
     HSVPAEAAGK IDSTAIYHQV SQAHSSLPEP SDTQPPTSWQ GFFGHLYGYG ATYYSYIFDR
     AIANKLWEDV FQSGQASVDR NAGERYKNEV LRWGGGRNGW DCVAGVLGSG NPSNADGRLV
     EGGDDAMREV GRWGLGRDGV SG
//