(data stored in ACNUC7421 zone)

SWISSPROT: PTH_ANADE

ID   PTH_ANADE               Reviewed;         192 AA.
AC   Q2IM62;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 77.
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};
GN   OrderedLocusNames=Adeh_0119;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-
CC       tRNAs 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
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: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; CP000251; ABC79896.1; -; Genomic_DNA.
DR   RefSeq; WP_011419179.1; NC_007760.1.
DR   STRING; 290397.Adeh_0119; -.
DR   EnsemblBacteria; ABC79896; ABC79896; Adeh_0119.
DR   KEGG; ade:Adeh_0119; -.
DR   eggNOG; ENOG4108ZPD; Bacteria.
DR   eggNOG; COG0193; LUCA.
DR   HOGENOM; HOG000004797; -.
DR   KO; K01056; -.
DR   OMA; RYAHTRH; -.
DR   BioCyc; ADEH290397:G1G5W-123-MONOMER; -.
DR   Proteomes; UP000001935; 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; Q2IM62.
DR   SWISS-2DPAGE; Q2IM62.
KW   Complete proteome; Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN         1    192       Peptidyl-tRNA hydrolase.
FT                                /FTId=PRO_0000264003.
SQ   SEQUENCE   192 AA;  20717 MW;  442847C4A5D3024E CRC64;
     MKLVVGLGNP GEEYARTRHN VGFVVADRLA QLAGASFTAK KFAAELAEAR LGPERVWILK
     PQTYMNHSGE AVGAALRFWK LGLDDLVVVH DDLELEPFRV QLKVGGGHGG HNGVKSVNAH
     VGSPEYARVR VGVGRPPPRM DPADYVLGKF AKGEDAELDL CVEQAVEATR LAVELGAAKA
     MNQVNRRSRA AE
//

If you have problems or comments...

PBIL Back to PBIL home page