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PMIP_ASHGO
ID   PMIP_ASHGO              Reviewed;         776 AA.
AC   Q753X4;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 113.
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; OrderedLocusNames=AFR198W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53569.1; -; Genomic_DNA.
DR   RefSeq; NP_985745.1; NM_211099.1.
DR   AlphaFoldDB; Q753X4; -.
DR   SMR; Q753X4; -.
DR   STRING; 33169.AAS53569; -.
DR   MEROPS; M03.006; -.
DR   PRIDE; Q753X4; -.
DR   EnsemblFungi; AAS53569; AAS53569; AGOS_AFR198W.
DR   GeneID; 4622005; -.
DR   KEGG; ago:AGOS_AFR198W; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   InParanoid; Q753X4; -.
DR   OMA; VVYCDLF; -.
DR   Proteomes; UP000000591; Chromosome VI.
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..28
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..776
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338568"
FT   REGION          48..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        568
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         567
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"
FT   BINDING         574
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   776 AA;  88597 MW;  78E4201F03A2B72F CRC64;
     MFVRFYKRLD RQYIQSQRRW ILSSNKCLLQ GNKNATISPL RRAFDDQDHW EESQAQNTSS
     EQDNKGKNSS YFWSRSKATA PQVAHTGLFQ NPYLNSPEGL RKFANKSLTE ATALVRNLRE
     DSSQEGLVRY IIRLDQLSDI LCRVIDLCEF LRAAHPDEQF VAAAQECHEQ MFEIMNILNT
     DVVLCKRLKQ VLSDENISSK LSSEEIRVGH ILLEDFEKAG AYASPEVRKQ FIQLSQNISI
     IGQDFINNTE SLSSSYIKIP CKDLESSGTS HLVLRQLTKD TMGNNYKIPT SGYAPYTLLN
     ACPSEAIRRQ VWTAMFSCSE KQVKRLKSLL QLRRKLANIM GATDYVSYQL EGKMAKSPEN
     VKNFLNTLVD HTKPLAAGEL EELAKLKRNV ENLSETNTLK LMRPWDRDYY SSLSPNFTRP
     NHRVDGFTSI NTYFSLGVVM QGISDLFRDI YGISLKPVVA QAGETWAPDV RKLQVISETE
     GIIGLIYCDL LERPGKTTSP SHFTVCCSRQ IYPEENDFST IQVGENPDGS RFQMPVISLI
     CNFRATRHGK NKSLCLLELS DVETLFHEMG HALHSMLGRT QLQNLSGTRC VTDFVELPSI
     LMEHFAKDRR VLLRISSNYA TGEPIPEELL SAFQEQNNFL KNTETFSQIK MSMLDQRLHS
     ITDQDDIIAV YHGLEREMEV LVDDQTNWCG RFGHLFGYGA SYYSYLMDRA IAAKIWDHLF
     KKDPFSRSSG EKFKEGVLKW GGSRDAWQCI ADALDEPRLV KGDDWAMRFI GEVEDM
 
 
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