PTH_SULAC
ID PTH_SULAC Reviewed; 120 AA.
AC Q877G5; Q4JAN6;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=Saci_0770;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RA Esnault C., Trehin A., Duguet M.;
RT "AAA family ATPase in the archeae Sulfolobus acidocaldarius.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY80143.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY255679; AAP13474.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY80143.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_015385493.1; NC_007181.1.
DR AlphaFoldDB; Q877G5; -.
DR SMR; Q877G5; -.
DR STRING; 330779.Saci_0770; -.
DR PRIDE; Q877G5; -.
DR EnsemblBacteria; AAY80143; AAY80143; Saci_0770.
DR GeneID; 3473833; -.
DR KEGG; sai:Saci_0770; -.
DR PATRIC; fig|330779.12.peg.736; -.
DR eggNOG; arCOG04228; Archaea.
DR HOGENOM; CLU_073661_2_2_2; -.
DR Proteomes; UP000001018; 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 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..120
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_0000120303"
SQ SEQUENCE 120 AA; 13148 MW; 2FE443DD10B1F69C CRC64;
MKMAVLVRTD LDMGKGKIAA QVAHAAVSLV LEIVQKRSKA EWKEWLEMWI NQGQPKIVLK
VKNLDELLEK YNKALQSGLP ATIIQDAGKT QIEPGTITCA GIGPGPEEMI DNITGDLKLL
