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Database: UniProt
Entry: A0A0F0LVN4_9MICO
LinkDB: A0A0F0LVN4_9MICO
Original site: A0A0F0LVN4_9MICO 
ID   A0A0F0LVN4_9MICO        Unreviewed;       348 AA.
AC   A0A0F0LVN4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 21.
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:KJL36365.1};
GN   ORFNames=RR49_01697 {ECO:0000313|EMBL:KJL36365.1};
OS   Microbacterium ginsengisoli.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=400772 {ECO:0000313|EMBL:KJL36365.1, ECO:0000313|Proteomes:UP000033451};
RN   [1] {ECO:0000313|EMBL:KJL36365.1, ECO:0000313|Proteomes:UP000033451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18659 {ECO:0000313|EMBL:KJL36365.1,
RC   ECO:0000313|Proteomes:UP000033451};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on
RT   heavy metal contaminated environments.";
RL   Submitted (FEB-2015) 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:KJL36365.1}.
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DR   EMBL; JYIY01000074; KJL36365.1; -; Genomic_DNA.
DR   RefSeq; WP_045247631.1; NZ_JYIY01000074.1.
DR   EnsemblBacteria; KJL36365; KJL36365; RR49_01697.
DR   PATRIC; fig|400772.4.peg.1719; -.
DR   OrthoDB; 469058at2; -.
DR   Proteomes; UP000033451; 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};
KW   Complete proteome {ECO:0000313|Proteomes:UP000033451};
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:KJL36365.1};
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:UP000033451}.
FT   DOMAIN      122    322       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   METAL       266    266       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00281}.
SQ   SEQUENCE   348 AA;  38349 MW;  0C7EFCF58E1FFFF1 CRC64;
     MSDAPENEIT PEAVTAAAEA AVAAIAAASD SAELKAARQA HVAEGSPLAR LNARMRDVPA
     DRKAEFGKLV GQARGQVTQA LAARETALAE AELAAKLEGE RVDITAVPQR TRVGARHPLT
     LLQEQIGDIF VGMGWEIAEG PELEHEWFNF DALNVDPDHP ARQMQDTFYV DPVERHLVLR
     TQTSPVQMRT MLSRDVPIYV ISPGRVYRTD EFDATHLPVF TQFEGLVVDK GITMAHLKGT
     LDHVAKQLFG AEAKTRFRAN FFPFTEPSAE LDLWHPTFKG GARWIEWGGC GMVNPNVLRA
     AGLDPEVYSG FAFGMGVERT LMFRSDVQDM RDMAEGDVRF SEQFGMVV
//
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