GenomeNet

Database: UniProt
Entry: W3TZE7_BARQI
LinkDB: W3TZE7_BARQI
Original site: W3TZE7_BARQI 
ID   W3TZE7_BARQI            Unreviewed;       359 AA.
AC   W3TZE7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   05-JUN-2019, entry version 34.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00281};
DE            EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00281};
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00281};
DE            Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00281};
GN   Name=pheS {ECO:0000256|HAMAP-Rule:MF_00281};
GN   ORFNames=Q649_00352 {ECO:0000313|EMBL:ETS16795.1};
OS   Bartonella quintana JK 73.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=1402976 {ECO:0000313|EMBL:ETS16795.1, ECO:0000313|Proteomes:UP000018945};
RN   [1] {ECO:0000313|EMBL:ETS16795.1, ECO:0000313|Proteomes:UP000018945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JK 73 {ECO:0000313|EMBL:ETS16795.1,
RC   ECO:0000313|Proteomes:UP000018945};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Kirby J., Birtles R., Dasch G., Hendrix L., Koehler J.,
RA   Kosoy M., Young S., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA   Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J.,
RA   McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A.,
RA   Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bartonella quintana JK 73.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate +
CC         H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413,
CC         Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215;
CC         EC=6.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00281,
CC         ECO:0000256|SAAS:SAAS01124652};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00281};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP-
CC       Rule:MF_00281};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00281, ECO:0000256|SAAS:SAAS01133340}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00281,
CC       ECO:0000256|SAAS:SAAS00089481}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00281, ECO:0000256|SAAS:SAAS00541523}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ETS16795.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; AZZX01000006; ETS16795.1; -; Genomic_DNA.
DR   RefSeq; WP_034450684.1; NZ_KI911825.1.
DR   EnsemblBacteria; ETS16795; ETS16795; Q649_00352.
DR   PATRIC; fig|1402976.3.peg.454; -.
DR   Proteomes; UP000018945; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00281; Phe_tRNA_synth_alpha1; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR   InterPro; IPR004188; Phe-tRNA_ligase_II_N.
DR   InterPro; IPR022911; Phe_tRNA_ligase_alpha1_bac.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   Pfam; PF02912; Phe_tRNA-synt_N; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   TIGRFAMs; TIGR00468; pheS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110915, ECO:0000313|EMBL:ETS16795.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110882};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018945};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS00461853};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110936};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS00017000};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS00017079};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110884};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110938};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018945}.
FT   DOMAIN      111    356       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   METAL       260    260       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00281}.
SQ   SEQUENCE   359 AA;  41241 MW;  6FA14AC42226196D CRC64;
     MNDIERLEKE ICLALEAASD EQTLETVRIA ALGKKGCISE KLKALGKMDV EERHKVGPVL
     NGLKNRVLEL WVQKRDLLRR QAMNTRLSRE TVDVTLPVRS SPLERGRIHP ISQVIEEIIA
     IYANMGFSLA EGPDIETDYY NFTALNFPEG HPAREMHDTF FFDVDKTGER KLLRTHTSPV
     QIRTMEKQKA PIRIIIPGKT YRMDSDATHS PMFHQVEGLV IDKTSTIAHM MWLHETFCKA
     FFEVPSVKMR FRPSFFPFTE PSMEVDIQCD RSGSKVKFGE GQDWLEILGC GMVHPYVLQN
     VGLDPDVYQG FAWGMGIDRI AMLKYGMPDL RAFFDADLRW LDHYGFRCFD MPAFFPGLR
//
DBGET integrated database retrieval system