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Database: UniProt/TrEMBL
Entry: D2PEA0_SULID
LinkDB: D2PEA0_SULID
Original site: D2PEA0_SULID 
ID   D2PEA0_SULID            Unreviewed;       545 AA.
AC   D2PEA0;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   11-JUN-2014, entry version 27.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit;
DE            EC=6.1.1.20;
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
GN   Name=pheT; OrderedLocusNames=LD85_2287;
OS   Sulfolobus islandicus (strain L.D.8.5 / Lassen #2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=425944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L.D.8.5 / Lassen #2;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP +
CC       diphosphate + L-phenylalanyl-tRNA(Phe).
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta
CC       subunit family. Type 2 subfamily.
CC   -!- SIMILARITY: Contains 1 B5 domain.
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DR   EMBL; CP001731; ADB87933.1; -; Genomic_DNA.
DR   RefSeq; YP_003420303.1; NC_013769.1.
DR   EnsemblBacteria; ADB87933; ADB87933; LD85_2287.
DR   GeneID; 8762136; -.
DR   KEGG; sii:LD85_2287; -.
DR   HOGENOM; HOG000105094; -.
DR   KO; K01890; -.
DR   OMA; FPMMGVE; -.
DR   BioCyc; SISL425944:GHS5-2298-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.56.20; -; 1.
DR   HAMAP; MF_00284; Phe_tRNA_synth_beta2; 1.
DR   InterPro; IPR005146; B3/B4_tRNA-bd.
DR   InterPro; IPR009061; DNA-bd_dom_put.
DR   InterPro; IPR004531; Phe-tRNA-synth_IIc_bsu_arc.
DR   InterPro; IPR022918; Phe_tRNA_ligase_beta2_bac/arc.
DR   InterPro; IPR005147; tRNA_synthase_B5-dom.
DR   Pfam; PF03483; B3_4; 1.
DR   Pfam; PF03484; B5; 1.
DR   SMART; SM00873; B3_4; 1.
DR   SMART; SM00874; B5; 1.
DR   SUPFAM; SSF46955; SSF46955; 2.
DR   TIGRFAMs; TIGR00471; pheT_arch; 1.
DR   PROSITE; PS51483; B5; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   DOMAIN      268    343       B5 (By similarity).
FT   METAL       321    321       Magnesium (By similarity){EA3}.
FT   METAL       327    327       Magnesium; via carbonyl oxygen (By
FT                                similarity){EA3}.
FT   METAL       330    330       Magnesium (By similarity){EA3}.
FT   METAL       331    331       Magnesium (By similarity){EA3}.
SQ   SEQUENCE   545 AA;  61714 MW;  52B11F2944CAB4F3 CRC64;
     MVTIVLNKYK LLDKIHIGQQ KLEDLLFNLK SEVKPIDENN IEIEINADRL DLLSSDGIAR
     AIKGLLEKEL GEAKYNVTDT EYTLIVDNVR TRPYALAAIV YNAKIDLEEL IQFQEKLHGT
     IGRKRKKVAI GIHDLRKVDS KTIEYKEVPL SYKFVPLYGN KELTISEILE KTEQGKLYGN
     ISIANGVSPA IVQDDGEVLS IPPIINSNKT RLDENTKDFF IDVTGTSFEA VAQTLDIIVS
     NLAEAGGTIG RVKVLKSANS SQLSSPLFLH KIQNVREEYV KKILGIKTSK EEICKHVMRM
     RMNCDIENGV IRVTVPQYRV DILNEIDVVE DIAMSIGYNN LEPSKYISTN YGSYDYMTLL
     ERKIRELGIG AGYVEISNFV LIKDEKLFSN KYVKILNPVT EEYNAVRNSL IPGLLDFLSK
     NQHAKFPIRV FETGDVVVYD SSTDTGFRND KRAAYAIMDN KVSYEDIQAP IHYILKSLGL
     EVNYKEENNN IFIEGRSASI FYENEKMGVI GEVNPDVLIR FGIEYPAVIA ELYISEIAKR
     LTNQR
//
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