PTH_PYRHO
ID PTH_PYRHO Reviewed; 121 AA.
AC O74017;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 118.
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=PH1539;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA30649.1; -; Genomic_DNA.
DR PIR; A71031; A71031.
DR PDB; 1WN2; X-ray; 1.20 A; A=1-121.
DR PDB; 2D3K; X-ray; 1.90 A; A/B=1-121.
DR PDBsum; 1WN2; -.
DR PDBsum; 2D3K; -.
DR AlphaFoldDB; O74017; -.
DR SMR; O74017; -.
DR STRING; 70601.3257966; -.
DR EnsemblBacteria; BAA30649; BAA30649; BAA30649.
DR KEGG; pho:PH1539; -.
DR eggNOG; arCOG04228; Archaea.
DR OMA; GHAAVEC; -.
DR BRENDA; 3.1.1.29; 5244.
DR EvolutionaryTrace; O74017; -.
DR Proteomes; UP000000752; 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.
FT CHAIN 1..121
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_0000120301"
FT STRAND 7..17
FT /evidence="ECO:0007829|PDB:1WN2"
FT HELIX 21..42
FT /evidence="ECO:0007829|PDB:1WN2"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:1WN2"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:1WN2"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:1WN2"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:1WN2"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:1WN2"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:1WN2"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1WN2"
SQ SEQUENCE 121 AA; 13377 MW; BE7129443A95F98B CRC64;
MIKMFKYKQV IVARADLKLS KGKLAAQVAH GAVTAAFEAY KKKREWFEAW FREGQKKVVV
KVESEEELFK LKAEAEKLGL PNALIRDAGL TEIPPGTVTV LAVGPAPEEI VDKVTGNLKL
L
