ID   PMIP_ASPCL              Reviewed;         801 AA.
AC   A1CTP5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, 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=ACLA_083770;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027060; EAW06682.1; -; Genomic_DNA.
DR   RefSeq; XP_001268108.1; XM_001268107.1.
DR   AlphaFoldDB; A1CTP5; -.
DR   SMR; A1CTP5; -.
DR   STRING; 344612.A1CTP5; -.
DR   EnsemblFungi; EAW06682; EAW06682; ACLA_083770.
DR   GeneID; 4700295; -.
DR   KEGG; act:ACLA_083770; -.
DR   VEuPathDB; FungiDB:ACLA_083770; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   OMA; ALMFEYM; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000006701; 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   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_0000338569"
FT   REGION          31..54
FT                   /note="Disordered"
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   801 AA;  89815 MW;  38B5273FF01FD833 CRC64;
     MKPQLLTPLR RRPWTCRQCL QRLQRLQQQT RRSFETAASP APGHTQVDYI PADASQSKKV
     DDETIRRVFD SQHFWREFSQ RRSTQSKPTG LVQNQYLTSP DGFRTFANVS LQKCQAIVSK
     VLAASTLEEY RTMARDLDRL SDLLCRVIDL SDFIRVIHPD PRVQEAATQA YALMFEYMNV
     LNTTTGLNDQ LKKAVANPEV ASHWTEEEKI VAQILIKDFS NSAILMPPQE RQRFVNLSND
     ISQLGSSFVN SPEPAKSQVV VNANSLRGLD PMLVQQIKRW NRTASVPTTG MIPRLALRSV
     HDESVRREVY LASRTSSARQ LHRLEELLLK RAELAKLSGY SSFGHMTLSD KMAKSPEAVS
     NFLTSLVDSN RTLVREELLQ LRNMKGSPLQ PWDHAYYVHK RVMQYSQSRR SRELSAVPEF
     FSLGTVMQGL SRLFDRLYGV RLVPQEAAPG ETWNPDVRRL DVVDEADRHI AVIYCDLFSR
     PNKHPNPAHF TLRCSREISA TEVAECASLD QSSHPNDGMA TAVDPTTKTL RQLPTIALVC
     DFAEPAAHGG RPSLLSEHSV RTLFHEMGHA LHSILGQTRL QSISGTRCAT DFAELPSVLM
     EHFATAPSVL SLYARHWETD EPLSERMIQS MERDRTAHGS IYGAVENEAQ ILMALVDQEY
     HSRPADGGRI DSTALYHEVA QRHSSLPDPA ETAPPTSWQG FFGHLYGYGA TYYSYIFDRA
     IANKLWADVF GAGRAAVDRA AGERYKTEVL RWGGGRNGWQ CVAGVLGPSN ASNADGRLVE
     GGDEAMREVG RWGLGRDGVS G
//