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Database: UniProt
Entry: Q9PQ33
LinkDB: Q9PQ33
Original site: Q9PQ33 
ID   SYFB_UREPA              Reviewed;         772 AA.
AC   Q9PQ33;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   29-OCT-2014, entry version 90.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit;
DE            EC=6.1.1.20;
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
DE            Short=PheRS;
GN   Name=pheT; OrderedLocusNames=UU457;
OS   Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=273119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700970;
RX   PubMed=11048724; DOI=10.1038/35037619;
RA   Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA   Cassell G.H.;
RT   "The complete sequence of the mucosal pathogen Ureaplasma
RT   urealyticum.";
RL   Nature 407:757-762(2000).
CC   -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP +
CC       diphosphate + L-phenylalanyl-tRNA(Phe).
CC   -!- COFACTOR: Binds 2 magnesium ions per tetramer. {ECO:0000250}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta
CC       subunit family. Type 1 subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 B5 domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 FDX-ACB domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 tRNA-binding domain. {ECO:0000305}.
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DR   EMBL; AF222894; AAF30869.1; -; Genomic_DNA.
DR   RefSeq; NP_078294.1; NC_002162.1.
DR   RefSeq; WP_010891780.1; NC_002162.1.
DR   ProteinModelPortal; Q9PQ33; -.
DR   STRING; 273119.UU457; -.
DR   EnsemblBacteria; AAF30869; AAF30869; UU457.
DR   GeneID; 876345; -.
DR   KEGG; uur:UU457; -.
DR   PATRIC; 20534497; VBIUrePar45146_0473.
DR   eggNOG; COG0072; -.
DR   HOGENOM; HOG000048955; -.
DR   KO; K01890; -.
DR   OMA; DIFVPVA; -.
DR   OrthoDB; EOG6CCH1J; -.
DR   BioCyc; UPAR273119:GHVP-476-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
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:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.56.20; -; 1.
DR   Gene3D; 3.50.40.10; -; 1.
DR   HAMAP; MF_00283; Phe_tRNA_synth_beta1; 1.
DR   InterPro; IPR005146; B3/B4_tRNA-bd.
DR   InterPro; IPR009061; DNA-bd_dom_put.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu.
DR   InterPro; IPR020825; Phe-tRNA_synthase_B3/B4.
DR   InterPro; IPR005121; PheS_beta_Fdx_antiC-bd.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR005147; tRNA_synthase_B5-dom.
DR   Pfam; PF03483; B3_4; 1.
DR   Pfam; PF03484; B5; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   SMART; SM00873; B3_4; 1.
DR   SMART; SM00874; B5; 1.
DR   SUPFAM; SSF46955; SSF46955; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF56037; SSF56037; 1.
DR   TIGRFAMs; TIGR00472; pheT_bact; 1.
DR   PROSITE; PS51483; B5; 1.
DR   PROSITE; PS51447; FDX_ACB; 1.
DR   PROSITE; PS50886; TRBD; 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; Reference proteome; RNA-binding; tRNA-binding.
FT   CHAIN         1    772       Phenylalanine--tRNA ligase beta subunit.
FT                                /FTId=PRO_0000126980.
FT   DOMAIN       40    158       tRNA-binding.
FT   DOMAIN      397    468       B5.
FT   DOMAIN      691    772       FDX-ACB.
FT   METAL       446    446       Magnesium. {ECO:0000250}.
FT   METAL       452    452       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       455    455       Magnesium. {ECO:0000250}.
FT   METAL       456    456       Magnesium. {ECO:0000250}.
SQ   SEQUENCE   772 AA;  88192 MW;  CCBE070438AEB6E6 CRC64;
     MILSLNLLHK ISPKLKKIPL NELCAALMDL GCEVETINSI KPSTNLVFAK VLEKTRHPNA
     NHLNLVKVKA NQKVYEIVCG ANNFSVHNWV VLAKLNAELA NGLKITPREL RGYVSNGMLC
     AYSEINPQAT SFLTSTDLDG ILVLDDNYDH YKTPNQIFNL DDVILDLSIP SNRNDLNGYF
     WIAKELCAYF DFEYVVDATI NHRPHKEIID VRILSDDVNS YGIIEVKNIQ NYILKWNTKS
     ILINNQIKVL NNFADNMNFL TLLTANPLHA FDARKISGQI VVKNAEEDAI LLGLDQKEYL
     IKKGDLIIVD DQKILALAGI IGSNDSKIDA TSTTAYIECA NFNPMLIANT ARRLKINTAA
     AMRFSKPLTN YVTKVTLKKL LANFKSDAKL IYYFKHSVHN VIKNKINQVS DFVGAEIDLD
     TAQTFLKRLG YKINKSNLIT PSHRYDVLNE FDVYEDIMKK ISIQEIKPQP ISFDILNFEN
     NLAYDFEKKV SDFLVDQGLF ECKTYNLKNQ TQAHEFNFFN FKQAYEINNP TSNMRSHLKL
     NNLNSLLEVL EYNQNQKNEL ENIFEISKIN PVDSSQQTVL SIILCKPLIN SKINDSLIVN
     NFVTTKALLH ALLTKLNIDY AYDKNHVVNE LYDNNQLALI NANKQVFGFI GQLKNQVKKT
     YGLSNDIFII NLNLTSYLNQ KQVITKVIKP SMYHDVIRDI SVKLASDVDL NNIIANIKKI
     KNIRKVEISD LYIKDDGIIY TFKYYINDHL SNLSSEQIII IEQEVNNYLK QF
//
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