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PTH_SACS2
ID   PTH_SACS2               Reviewed;         120 AA.
AC   Q980V1;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 116.
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=SSO0175;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-10, FUNCTION, AND CHARACTERIZATION.
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=12799450; DOI=10.1093/nar/gkg428;
RA   Fromant M., Ferri-Fioni M.-L., Plateau P., Blanquet S.;
RT   "Peptidyl-tRNA hydrolase from Sulfolobus solfataricus.";
RL   Nucleic Acids Res. 31:3227-3235(2003).
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, ECO:0000269|PubMed:12799450}.
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   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the PTH2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00628}.
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DR   EMBL; AE006641; AAK40521.1; -; Genomic_DNA.
DR   PIR; B90158; B90158.
DR   RefSeq; WP_009990400.1; NC_002754.1.
DR   PDB; 1XTY; X-ray; 1.80 A; A/B/C/D=1-120.
DR   PDBsum; 1XTY; -.
DR   AlphaFoldDB; Q980V1; -.
DR   SMR; Q980V1; -.
DR   STRING; 273057.SSO0175; -.
DR   EnsemblBacteria; AAK40521; AAK40521; SSO0175.
DR   GeneID; 44129141; -.
DR   KEGG; sso:SSO0175; -.
DR   PATRIC; fig|273057.12.peg.171; -.
DR   eggNOG; arCOG04228; Archaea.
DR   HOGENOM; CLU_073661_2_2_2; -.
DR   InParanoid; Q980V1; -.
DR   OMA; GHAAVEC; -.
DR   PhylomeDB; Q980V1; -.
DR   BRENDA; 3.1.1.29; 6163.
DR   EvolutionaryTrace; Q980V1; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IBA:GO_Central.
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; Direct protein sequencing; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..120
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_0000120304"
FT   STRAND          2..12
FT                   /evidence="ECO:0007829|PDB:1XTY"
FT   HELIX           16..35
FT                   /evidence="ECO:0007829|PDB:1XTY"
FT   HELIX           40..51
FT                   /evidence="ECO:0007829|PDB:1XTY"
FT   STRAND          56..63
FT                   /evidence="ECO:0007829|PDB:1XTY"
FT   HELIX           64..76
FT                   /evidence="ECO:0007829|PDB:1XTY"
FT   STRAND          81..85
FT                   /evidence="ECO:0007829|PDB:1XTY"
FT   STRAND          88..92
FT                   /evidence="ECO:0007829|PDB:1XTY"
FT   STRAND          97..106
FT                   /evidence="ECO:0007829|PDB:1XTY"
FT   HELIX           107..114
FT                   /evidence="ECO:0007829|PDB:1XTY"
SQ   SEQUENCE   120 AA;  13140 MW;  A90F6A3ADC714B91 CRC64;
     MIKMVIVVRS DIKMGKGKIA AQVAHAAVTL VVSIINSNNL RWKEWLNEWL HQGQPKIIVK
     VNSLDEIISR AKKAETMNLP FSIIEDAGKT QLEPGTITCL GIGPAPENLV DSITGDLKLL
 
 
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