(data stored in SCRATCH zone)

SWISSPROT: C1AT04_RHOOB

ID   C1AT04_RHOOB            Unreviewed;       828 AA.
AC   C1AT04;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   05-JUL-2017, entry version 71.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00283};
DE            EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00283};
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00283};
DE            Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00283};
GN   Name=pheT {ECO:0000256|HAMAP-Rule:MF_00283,
GN   ECO:0000313|EMBL:BAH48936.1};
GN   OrderedLocusNames=ROP_06890 {ECO:0000313|EMBL:BAH48936.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48936.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48936.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48936.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP +
CC       diphosphate + L-phenylalanyl-tRNA(Phe). {ECO:0000256|HAMAP-
CC       Rule:MF_00283, ECO:0000256|SAAS:SAAS00385044}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00283};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP-
CC       Rule:MF_00283};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00283, ECO:0000256|SAAS:SAAS00385214}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00283,
CC       ECO:0000256|SAAS:SAAS00710994}.
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta
CC       subunit family. Type 1 subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00283, ECO:0000256|SAAS:SAAS00570605}.
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DR   EMBL; AP011115; BAH48936.1; -; Genomic_DNA.
DR   RefSeq; WP_012687938.1; NC_012522.1.
DR   STRING; 632772.ROP_06890; -.
DR   EnsemblBacteria; BAH48936; BAH48936; ROP_06890.
DR   KEGG; rop:ROP_06890; -.
DR   PATRIC; fig|632772.20.peg.750; -.
DR   eggNOG; ENOG4105C6A; Bacteria.
DR   eggNOG; COG0072; LUCA.
DR   eggNOG; COG0073; LUCA.
DR   HOGENOM; HOG000292086; -.
DR   KO; K01890; -.
DR   OMA; LTPNRSD; -.
DR   OrthoDB; POG091H01YS; -.
DR   Proteomes; UP000002212; Chromosome.
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:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   CDD; cd02796; tRNA_bind_bactPheRS; 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; IPR005121; Fdx_antiC-bd.
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; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR033714; tRNA_bind_bactPheRS.
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;
DR   PRODOM; C1AT04.
DR   SWISS-2DPAGE; C1AT04.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00283,
KW   ECO:0000256|SAAS:SAAS00089714, ECO:0000313|EMBL:BAH48936.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00283,
KW   ECO:0000256|SAAS:SAAS00089645};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00283,
KW   ECO:0000256|SAAS:SAAS00710959};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00283,
KW   ECO:0000256|SAAS:SAAS00089691, ECO:0000313|EMBL:BAH48936.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00283,
KW   ECO:0000256|SAAS:SAAS00089695};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00283,
KW   ECO:0000256|SAAS:SAAS00089707};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00283,
KW   ECO:0000256|SAAS:SAAS00462081};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00283,
KW   ECO:0000256|SAAS:SAAS00089659};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00209,
KW   ECO:0000256|SAAS:SAAS00514389};
KW   tRNA-binding {ECO:0000256|PROSITE-ProRule:PRU00209,
KW   ECO:0000256|SAAS:SAAS00514462}.
FT   DOMAIN       44    155       TRNA-binding. {ECO:0000259|PROSITE:
FT                                PS50886}.
FT   DOMAIN      406    486       B5. {ECO:0000259|PROSITE:PS51483}.
FT   DOMAIN      734    827       FDX-ACB. {ECO:0000259|PROSITE:PS51447}.
FT   METAL       464    464       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00283}.
FT   METAL       470    470       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00283}.
FT   METAL       473    473       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00283}.
FT   METAL       474    474       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00283}.
SQ   SEQUENCE   828 AA;  87602 MW;  CC386B9ECF19276D CRC64;
     MRVAQSWLTE ILQRATPDWD VTAEELDAGF VRVGLEVEEV DRLEPVDGPL VVGKVLEITE
     LTEFKKPIRF CKVDVGAAEP QGIVCGARNF AEGDLVVVAL PGAVLPGGFA IASRKTYGQV
     SDGMICSVAE LGIGKDHSGI LVLEPGTALP GADANELMGL HDTVIELNIT PDRGYCFSVR
     GLTRELACGF DLDFADPAAV APSPADGEAW PIRVEPESKA TRFAARRVTG IDPNAVSPWW
     LQRRLLLSGV RPISPAVDVT NYVLLELGQP LHAFDAAKIR GELVVRRAVA GEKLTTLDET
     ERVLDPEDVV IADDSGVLSL AGIMGGASTE VGPGTTDILL EAATWDPLAV FKTARRHKLS
     SEAGKRFERV VDPEIPVAAL DRAAALLVDI AGGRVESALT DIGEVTPHRP IHMDIDLPDR
     VAGVDYPTGT SARRLTQIGC SVEVGVSDSG HGQLVAAPPS WRPDLVQPAD LVEEVLRLEG
     LEKIPSVLPA APAGRGLTPT QRRKRAVGRA LAFSGYVEIL PPVFLPTAVF DTWGLDPEDP
     RRNTGRVLNP LESDRPELAT TLLPGLLEVL ARNVSRGQRD LSLFGIAQVV LPGADTKPVA
     ALPVDRRPTD EQITALLQSL PDQPVHVAVV LTGQREPSGP WGAGRAADAT DAFAAARTVA
     AAAGVEFEFR AAQYLPWHPG RGAELLVDGV VVGHAGELHP AVLERAGLPP RTSAVEIDLS
     ALPLVENLPA PKVSPFPAVL QDVAVVVDTA VPAAEVQAAL RSGGGELLED IRLFDVFEGE
     QVGEGRKSLA FALRFRGADR TLTEDEASAA RDAAVAAASA AVGAELRS
//

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