(data stored in ACNUC7421 zone)

SWISSPROT: C8W306_DESAS

ID   C8W306_DESAS            Unreviewed;       196 AA.
AC   C8W306;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   16-JAN-2019, entry version 55.
DE   RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000256|HAMAP-Rule:MF_00083, ECO:0000256|RuleBase:RU000673};
DE            Short=PTH {ECO:0000256|HAMAP-Rule:MF_00083};
DE            EC=3.1.1.29 {ECO:0000256|HAMAP-Rule:MF_00083, ECO:0000256|RuleBase:RU000673};
GN   Name=pth {ECO:0000256|HAMAP-Rule:MF_00083};
GN   OrderedLocusNames=Dtox_0209 {ECO:0000313|EMBL:ACV61162.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61162.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61162.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-
CC       tRNAs which drop off the ribosome during protein synthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00083}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-acyl-L-alpha-aminoacyl-tRNA = an N-acyl-L-amino
CC         acid + H(+) + tRNA; Xref=Rhea:RHEA:54448, Rhea:RHEA-COMP:10123,
CC         Rhea:RHEA-COMP:13883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:59874, ChEBI:CHEBI:78442, ChEBI:CHEBI:138191;
CC         EC=3.1.1.29; Evidence={ECO:0000256|HAMAP-Rule:MF_00083,
CC         ECO:0000256|RuleBase:RU000673};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00083}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00083}.
CC   -!- SIMILARITY: Belongs to the PTH family. {ECO:0000256|HAMAP-
CC       Rule:MF_00083, ECO:0000256|RuleBase:RU004320}.
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DR   EMBL; CP001720; ACV61162.1; -; Genomic_DNA.
DR   RefSeq; WP_015755883.1; NC_013216.1.
DR   STRING; 485916.Dtox_0209; -.
DR   EnsemblBacteria; ACV61162; ACV61162; Dtox_0209.
DR   KEGG; dae:Dtox_0209; -.
DR   eggNOG; ENOG4108ZPD; Bacteria.
DR   eggNOG; COG0193; LUCA.
DR   HOGENOM; HOG000004797; -.
DR   KO; K01056; -.
DR   OMA; RYAHTRH; -.
DR   OrthoDB; 1676462at2; -.
DR   BioCyc; DACE485916:G1GFV-215-MONOMER; -.
DR   Proteomes; UP000002217; 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; C8W306.
DR   SWISS-2DPAGE; C8W306.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00083};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00083,
KW   ECO:0000256|RuleBase:RU000673, ECO:0000313|EMBL:ACV61162.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
SQ   SEQUENCE   196 AA;  21742 MW;  BC0FF6D8C15FAFE3 CRC64;
     MKLIVGLGNP GIEYRNTRHN IGFMVIDQLA EKYGVDVQKK MMRSVLGQGW LGSQKVILAK
     PLTYMNLSGQ SVQALMNWYK LTAQELLVIC DDLNLEAGHL RLRKKGSDGG HNGLKSIIQA
     LGTSDFPRLR LGIGRPSHPG QEQVSFVLGK FAPQEAELLS QLIGRGEQAA AVWVENGIDA
     AMNEFNRSRR EDKEDK
//

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