PTH_ARCFU
ID PTH_ARCFU Reviewed; 115 AA.
AC O28185;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000255|HAMAP-Rule:MF_00628};
DE Short=PTH {ECO:0000255|HAMAP-Rule:MF_00628};
DE EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00628};
GN Name=pth {ECO:0000255|HAMAP-Rule:MF_00628}; OrderedLocusNames=AF_2095;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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_00628}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-
CC amino acid + H(+); 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_00628};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00628}.
CC -!- SIMILARITY: Belongs to the PTH2 family. {ECO:0000255|HAMAP-
CC Rule:MF_00628}.
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DR EMBL; AE000782; AAB89160.1; -; Genomic_DNA.
DR PIR; G69511; G69511.
DR RefSeq; WP_010879586.1; NC_000917.1.
DR PDB; 1RZW; NMR; -; A=1-115.
DR PDB; 3ERJ; X-ray; 1.80 A; A/B=1-115.
DR PDBsum; 1RZW; -.
DR PDBsum; 3ERJ; -.
DR AlphaFoldDB; O28185; -.
DR BMRB; O28185; -.
DR SMR; O28185; -.
DR STRING; 224325.AF_2095; -.
DR EnsemblBacteria; AAB89160; AAB89160; AF_2095.
DR GeneID; 24795842; -.
DR KEGG; afu:AF_2095; -.
DR eggNOG; arCOG04228; Archaea.
DR HOGENOM; CLU_073661_2_2_2; -.
DR OMA; GHAAVEC; -.
DR OrthoDB; 115947at2157; -.
DR PhylomeDB; O28185; -.
DR BRENDA; 3.1.1.29; 414.
DR EvolutionaryTrace; O28185; -.
DR Proteomes; UP000002199; 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; cd02430; PTH2; 1.
DR Gene3D; 3.40.1490.10; -; 1.
DR HAMAP; MF_00628; Pept_tRNA_hydro_arch; 1.
DR InterPro; IPR023476; Pep_tRNA_hydro_II_dom_sf.
DR InterPro; IPR034759; Pept_tRNA_hydro_arch.
DR InterPro; IPR002833; PTH2.
DR PANTHER; PTHR12649; PTHR12649; 1.
DR Pfam; PF01981; PTH2; 1.
DR SUPFAM; SSF102462; SSF102462; 1.
DR TIGRFAMs; TIGR00283; arch_pth2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..115
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_0000120288"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:3ERJ"
FT HELIX 17..34
FT /evidence="ECO:0007829|PDB:3ERJ"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:3ERJ"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:3ERJ"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:3ERJ"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:3ERJ"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3ERJ"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:3ERJ"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:3ERJ"
SQ SEQUENCE 115 AA; 12487 MW; 4DEEC200CF881489 CRC64;
MTLKQVIVVR DDLKLSRGKL AVQVAHAAII GYLKSDSSLR RKWLDEGQKK VVLKVKSLEE
LLGIKHKAES LGLVTGLVQD AGLTEVPPGT ITAVVIGPDE ERKIDKVTGN LPLLK
