ID D2PEA0_SULID Unreviewed; 545 AA.
AC D2PEA0;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 01-MAY-2013, entry version 22.
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; FFPNRPD; -.
DR BioCyc; SISL425944:GHS5-2331-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA: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; Putativ_DNA_bind; 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).
FT METAL 327 327 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 330 330 Magnesium (By similarity).
FT METAL 331 331 Magnesium (By similarity).
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
//
