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Database: UniProt
Entry: K2JQC5_9GAMM
LinkDB: K2JQC5_9GAMM
Original site: K2JQC5_9GAMM 
ID   K2JQC5_9GAMM            Unreviewed;       327 AA.
AC   K2JQC5;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   08-MAY-2019, entry version 39.
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   ECO:0000313|EMBL:EKE76707.1};
GN   ORFNames=B3C1_03900 {ECO:0000313|EMBL:EKE76707.1};
OS   Gallaecimonas xiamenensis 3-C-1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Gallaecimonas.
OX   NCBI_TaxID=745411 {ECO:0000313|EMBL:EKE76707.1, ECO:0000313|Proteomes:UP000006755};
RN   [1] {ECO:0000313|EMBL:EKE76707.1, ECO:0000313|Proteomes:UP000006755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3-C-1 {ECO:0000313|EMBL:EKE76707.1,
RC   ECO:0000313|Proteomes:UP000006755};
RX   PubMed=23209203; DOI=10.1128/JB.01854-12;
RA   Lai Q., Wang L., Wang W., Shao Z.;
RT   "Genome Sequence of Gallaecimonas xiamenensis Type Strain 3-C-1.";
RL   J. Bacteriol. 194:6937-6937(2012).
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:EKE76707.1}.
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DR   EMBL; AMRI01000004; EKE76707.1; -; Genomic_DNA.
DR   RefSeq; WP_008483052.1; NZ_AMRI01000004.1.
DR   STRING; 745411.B3C1_03900; -.
DR   EnsemblBacteria; EKE76707; EKE76707; B3C1_03900.
DR   PATRIC; fig|745411.4.peg.770; -.
DR   OrthoDB; 469058at2; -.
DR   Proteomes; UP000006755; 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};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110882}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006755};
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, ECO:0000313|EMBL:EKE76707.1};
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:UP000006755}.
FT   DOMAIN      116    317       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   COILED       60     91       {ECO:0000256|SAM:Coils}.
FT   METAL       252    252       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00281}.
SQ   SEQUENCE   327 AA;  36799 MW;  08741B2F66B7F70A CRC64;
     MQHLDEIVSQ ATAAVEAATD MAALDAIRVD YLGKKGLLTL QMQSLRDLSP EERPKAGAVI
     NQAKEAVQEV LNAKKNAMVE AELNAKLAAE QVDVTLPGRR QPLAGLHPVT RTIERIESFF
     GELGFAVKEG PEIEDAFHNF DALNIPAHHP ARADHDTFYF TPDMLLRTQT SGVQIRTMEV
     EQPPLRIISP GRVYRNDYDQ THTPMFHQVE GLLVDENISF ADLKGILHDF LQNFFEEDLE
     VRFRPSFFPF TEPSAEVDVK GKNGKWLEVL GCGMVHPNVL KAVGIDPEKY TGFAFGMGVE
     RLTMLRYGVN DLRAFFENDV RFLKQFN
//
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