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Database: UniProt
Entry: Q9A9E5
LinkDB: Q9A9E5
Original site: Q9A9E5 
ID   SYFB_CAUCR              Reviewed;         799 AA.
AC   Q9A9E5;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   29-OCT-2014, entry version 85.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00283};
DE            EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00283};
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00283};
DE            Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00283};
GN   Name=pheT {ECO:0000255|HAMAP-Rule:MF_00283};
GN   OrderedLocusNames=CC_1043;
OS   Caulobacter crescentus (strain ATCC 19089 / CB15).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J.,
RA   Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J.,
RA   Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L.,
RA   Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
CC   -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP +
CC       diphosphate + L-phenylalanyl-tRNA(Phe). {ECO:0000255|HAMAP-
CC       Rule:MF_00283}.
CC   -!- COFACTOR: Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP-
CC       Rule:MF_00283}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00283}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00283}.
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta
CC       subunit family. Type 1 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00283}.
CC   -!- SIMILARITY: Contains 1 B5 domain. {ECO:0000255|HAMAP-
CC       Rule:MF_00283}.
CC   -!- SIMILARITY: Contains 1 FDX-ACB domain. {ECO:0000255|HAMAP-
CC       Rule:MF_00283}.
CC   -!- SIMILARITY: Contains 1 tRNA-binding domain. {ECO:0000255|HAMAP-
CC       Rule:MF_00283}.
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DR   EMBL; AE005673; AAK23027.1; -; Genomic_DNA.
DR   PIR; G87378; G87378.
DR   RefSeq; NP_419859.1; NC_002696.2.
DR   RefSeq; WP_010918927.1; NC_002696.2.
DR   ProteinModelPortal; Q9A9E5; -.
DR   SMR; Q9A9E5; 1-792.
DR   EnsemblBacteria; AAK23027; AAK23027; CC_1043.
DR   GeneID; 940568; -.
DR   KEGG; ccr:CC_1043; -.
DR   PATRIC; 21299058; VBICauCre124313_1059.
DR   eggNOG; COG0073; -.
DR   HOGENOM; HOG000292085; -.
DR   KO; K01890; -.
DR   OMA; RTSCDET; -.
DR   OrthoDB; EOG6CCH1J; -.
DR   BioCyc; CAULO:CC1043-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; 3.30.70.380; -; 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; PF03147; FDX-ACB; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   SMART; SM00873; B3_4; 1.
DR   SMART; SM00874; B5; 1.
DR   SMART; SM00896; FDX-ACB; 1.
DR   SUPFAM; SSF46955; SSF46955; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF54991; SSF54991; 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    799       Phenylalanine--tRNA ligase beta subunit.
FT                                /FTId=PRO_0000126863.
FT   DOMAIN       39    148       tRNA-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00283}.
FT   DOMAIN      403    477       B5. {ECO:0000255|HAMAP-Rule:MF_00283}.
FT   DOMAIN      706    798       FDX-ACB. {ECO:0000255|HAMAP-
FT                                Rule:MF_00283}.
FT   METAL       455    455       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00283}.
FT   METAL       461    461       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00283}.
FT   METAL       464    464       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00283}.
FT   METAL       465    465       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00283}.
SQ   SEQUENCE   799 AA;  83872 MW;  70EA95DEB73B4180 CRC64;
     MKFTLSWLKD HLETTATVPE IVAAMTMAGL EVEHVIDPAT KLAPFTVCKI VEAARHPNAD
     RLQVCQVDTV DGRKEIVCGA PNARPGLTTI YAPIGAYVPG LDVTLVEKPV RGVVSNGMLC
     SAAELEYASE SDGIMELEGS LAVGTPAVDA LGLEAVIDFE VTPNRPDWLG VAGIARDLAA
     AGVGTLKDLS IAPIAGTYPS PISVTVDGEA CPAFAGRYIR GVKNGPSPKW LQDRLTAIGL
     RPINALVDVT NLISYDRARP LHVYDAHKLS GTQISTRLGR HGEHGDEHLI ALDGKTYELT
     PEMCVIADAN GERPIGLGGV MGGESTGCSE DTVDVFVESA WFEPIRIAQT GRTTGIASDA
     QYRFARTVDT GSLVPGIELA TKLILELCGG EPSEVVYVGE VPAAPKGFAF DPDYVGQLSG
     LAVTPEKTHQ ILAALGFDVV LGSPWTVTPP TFRRDVEGKA DLVEEVARIA GYGALPSTPL
     PEVPRAVGGI LTAKQARARA ARRALAAAGY AEAVTFSFTN RKTASLFGGG QDVLVLANPI
     ASELDCMRPS LLPNLIEAAG RNARQGFADA ALFEIGPTFH GDKPADQRTV VSAILAPKAP
     RGWDKAAQGD VFTVKADLLA LLEELGAPVA SLQTAQGSAS SWWHPGRSAR LQLGPKAVMA
     EFGEIHPAVL KALDVAGPVF GFEITLEAIP EPKKKSIKTK PAFSPSALMP LTRDFAFLVE
     KAKAAGDLVK AAAGADKALI TAARVFDVYE GPGVPDGFKS VAIEVVVQPR EATLTDAEIE
     ALSAKVVAAA EKAGGKLRS
//
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