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PROX_ACESD
ID   PROX_ACESD              Reviewed;         164 AA.
AC   Q9L4Q7; E3PU02;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Prolyl-tRNA editing protein ProX;
DE   AltName: Full=Prolyl-tRNA deacylase ProX;
GN   Name=proX; Synonyms=prdX; OrderedLocusNames=CLOST_2238;
OS   Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS   9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Acetoanaerobium.
OX   NCBI_TaxID=499177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX   PubMed=10085076; DOI=10.1074/jbc.274.13.8445;
RA   Kabisch U.C., Graentzdoerffer A., Schierhorn A., Ruecknagel K.P.,
RA   Andreesen J.R., Pich A.;
RT   "Identification of D-proline reductase from Clostridium sticklandii as a
RT   selenoenzyme and indications for a catalytically active pyruvoyl group
RT   derived from a cysteine residue by cleavage of a proprotein.";
RL   J. Biol. Chem. 274:8445-8454(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX   PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA   Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA   Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA   Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT   "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT   its metabolism through its genome sequence.";
RL   BMC Genomics 11:555-555(2010).
RN   [3]
RP   FUNCTION AS TRNA(PRO) EDITING PROTEIN.
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX   PubMed=14663147; DOI=10.1073/pnas.2136934100;
RA   Ahel I., Korencic D., Ibba M., Soll D.;
RT   "Trans-editing of mischarged tRNAs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:15422-15427(2003).
RN   [4]
RP   CHARACTERIZATION OF GENERAL DEACYLASE ACTIVITY.
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX   PubMed=15886196; DOI=10.1074/jbc.m502174200;
RA   Ruan B., Soll D.;
RT   "The bacterial YbaK protein is a Cys-tRNAPro and Cys-tRNA Cys deacylase.";
RL   J. Biol. Chem. 280:25887-25891(2005).
CC   -!- FUNCTION: Functions in trans to edit the amino acid moiety from
CC       incorrectly charged Ala-tRNA(Pro). Has weak activity on correctly
CC       charged tRNA(Ala), tRNA(Gly) as well as tRNA(Cys), tRNA(Met),
CC       tRNA(Pro), tRNA(Ser) and tRNA(Leu). {ECO:0000269|PubMed:14663147}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PRORSD1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CBH22356.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ130879; CAB71308.1; -; Genomic_DNA.
DR   EMBL; FP565809; CBH22356.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q9L4Q7; -.
DR   SMR; Q9L4Q7; -.
DR   STRING; 1511.CLOST_2238; -.
DR   EnsemblBacteria; CBH22356; CBH22356; CLOST_2238.
DR   KEGG; cst:CLOST_2238; -.
DR   eggNOG; COG3760; Bacteria.
DR   HOGENOM; CLU_104635_0_0_9; -.
DR   Proteomes; UP000007041; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043906; F:Ala-tRNA(Pro) hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IDA:UniProtKB.
DR   Gene3D; 3.90.960.10; -; 1.
DR   InterPro; IPR040285; ProX/PRXD1.
DR   InterPro; IPR036754; YbaK/aa-tRNA-synt-asso_dom_sf.
DR   InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
DR   PANTHER; PTHR31423; PTHR31423; 1.
DR   Pfam; PF04073; tRNA_edit; 1.
DR   SUPFAM; SSF55826; SSF55826; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..164
FT                   /note="Prolyl-tRNA editing protein ProX"
FT                   /id="PRO_0000392535"
SQ   SEQUENCE   164 AA;  18519 MW;  708333ABCAE8304E CRC64;
     MDMDAKQAVI AKLDELKINY TLIEHDPVYT IEEMEKIDIE NVDYIVKNLF LRDAKGRQHY
     LVVADKDQKI DLKTLQDKIG STKLSFASED RLQKYLKLTK GAVSPFGVLN DETAEVEVVF
     DKNLVGRSCV AVHPNDNSAT VVLSYEDLEK IVKANGNTFK AIEL
 
 
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