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Database: UniProt
Entry: U3BY41_9VIBR
LinkDB: U3BY41_9VIBR
Original site: U3BY41_9VIBR 
ID   U3BY41_9VIBR            Unreviewed;       327 AA.
AC   U3BY41;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   08-MAY-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   ECO:0000313|EMBL:GAD74239.1};
GN   ORFNames=VAZ01S_005_00390 {ECO:0000313|EMBL:GAD74239.1};
OS   Vibrio azureus NBRC 104587.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=1219077 {ECO:0000313|EMBL:GAD74239.1, ECO:0000313|Proteomes:UP000016567};
RN   [1] {ECO:0000313|EMBL:GAD74239.1, ECO:0000313|Proteomes:UP000016567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 104587 {ECO:0000313|EMBL:GAD74239.1,
RC   ECO:0000313|Proteomes:UP000016567};
RA   Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y.,
RA   Tsuchikane K., Noguchi M., Hirakata S., Ichikawa N., Ohji S.,
RA   Yamazoe A., Fujita N.;
RT   "Whole genome shotgun sequence of Vibrio azureus NBRC 104587.";
RL   Submitted (SEP-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:GAD74239.1}.
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DR   EMBL; BATL01000005; GAD74239.1; -; Genomic_DNA.
DR   RefSeq; WP_021708019.1; NZ_BATL01000005.1.
DR   STRING; 1219077.VAZ01S_005_00390; -.
DR   EnsemblBacteria; GAD74239; GAD74239; VAZ01S_005_00390.
DR   Proteomes; UP000016567; 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:UP000016567};
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:GAD74239.1};
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:UP000016567}.
FT   DOMAIN      116    317       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   COILED        1     21       {ECO:0000256|SAM:Coils}.
FT   METAL       252    252       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00281}.
SQ   SEQUENCE   327 AA;  36987 MW;  6CC336FA3921AC65 CRC64;
     MQHLEEIIAN ASTAIEAAQS LVALDEVRVQ YLGKKGELTA QLQSLGKLPP EERREAGQEI
     NKAKGVVQQA IAARKDALQR AELEAKLAAE TIDVTLPGRR IENGGLHPVT RTVERIEKFF
     GELGFNTESG PEIEDAFHNF DALNIAADHP ARTDHDTFFF NPDLMLRTHT SGVQIRTMEN
     GKPPFRFIAP GRVYRNDYDQ THTPMFHQVE GMLVDENVNF AQLKGILHDF LCNFFEEEVE
     VRFRPSYFPF TEPSAEVDVM GKNGKWLEVL GCGMVHPNVL RSVGIDPEKY SGFAFGMGVE
     RLTMLRYGVN DLRAFFENDL RFLKQFK
//
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