(data stored in ACNUC7421 zone)

SWISSPROT: PTH_EXIS2

ID   PTH_EXIS2               Reviewed;         185 AA.
AC   B1YGP7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   11-DEC-2019, entry version 76.
DE   RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000255|HAMAP-Rule:MF_00083};
DE            Short=PTH {ECO:0000255|HAMAP-Rule:MF_00083};
DE            EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00083};
GN   Name=pth {ECO:0000255|HAMAP-Rule:MF_00083}; OrderedLocusNames=Exig_0043;
OS   Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15).
OC   Bacteria; Firmicutes; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=262543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17290 / JCM 13490 / 255-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA   Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA   Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC       which drop off the ribosome during protein synthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-acyl-L-alpha-aminoacyl-tRNA = an N-acyl-L-amino acid +
CC         H(+) + tRNA; Xref=Rhea:RHEA:54448, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC         COMP:13883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59874,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:138191; EC=3.1.1.29;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00083};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- SIMILARITY: Belongs to the PTH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00083}.
DR   EMBL; CP001022; ACB59530.1; -; Genomic_DNA.
DR   RefSeq; WP_012368956.1; NC_010556.1.
DR   SMR; B1YGP7; -.
DR   STRING; 262543.Exig_0043; -.
DR   PRIDE; B1YGP7; -.
DR   EnsemblBacteria; ACB59530; ACB59530; Exig_0043.
DR   KEGG; esi:Exig_0043; -.
DR   eggNOG; ENOG4108ZPD; Bacteria.
DR   eggNOG; COG0193; LUCA.
DR   HOGENOM; HOG000004797; -.
DR   KO; K01056; -.
DR   OMA; RYAHTRH; -.
DR   OrthoDB; 1676462at2; -.
DR   Proteomes; UP000001681; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00462; PTH; 1.
DR   Gene3D; 3.40.50.1470; -; 1.
DR   HAMAP; MF_00083; Pept_tRNA_hydro_bact; 1.
DR   InterPro; IPR001328; Pept_tRNA_hydro.
DR   InterPro; IPR018171; Pept_tRNA_hydro_CS.
DR   InterPro; IPR036416; Pept_tRNA_hydro_sf.
DR   PANTHER; PTHR17224; PTHR17224; 1.
DR   Pfam; PF01195; Pept_tRNA_hydro; 1.
DR   SUPFAM; SSF53178; SSF53178; 1.
DR   TIGRFAMs; TIGR00447; pth; 1.
DR   PROSITE; PS01195; PEPT_TRNA_HYDROL_1; 1.
DR   PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1YGP7.
DR   SWISS-2DPAGE; B1YGP7.
KW   Cytoplasm; Hydrolase.
FT   CHAIN           1..185
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_1000092941"
SQ   SEQUENCE   185 AA;  20430 MW;  3835F9631AF819BE CRC64;
     MKCIVGLGNP GAKYTNTRHN IGFLAIDALA KEHGIKLTES KFKAVFGTGM IKGERVVLVK
     PLTYMNLSGE AVRPLLDFYK IAVEDVLVIY DDLDLPLEKM RLRSKGSAGG HNGVKSLIQH
     LGTQDIKRLK LGVGRPPAPI QVIDWVLMPF AKSEQTTLQH VLSDSVNIAT DFIDTPFLAL
     MNRYN
//

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