PMIP_ASPCL
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 03-AUG-2022, entry version 86.
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; 5057.CADACLAP00007518; -.
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; VVYCDLF; -.
DR OrthoDB; 642479at2759; -.
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: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..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
