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Database: UniProt
Entry: A0A099JN18_9MICO
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Original site: A0A099JN18_9MICO 
ID   A0A099JN18_9MICO        Unreviewed;       337 AA.
AC   A0A099JN18;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   08-MAY-2019, entry version 28.
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=GY21_06345 {ECO:0000313|EMBL:KGJ79007.1};
OS   Cryobacterium roopkundense.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Cryobacterium.
OX   NCBI_TaxID=1001240 {ECO:0000313|EMBL:KGJ79007.1, ECO:0000313|Proteomes:UP000029864};
RN   [1] {ECO:0000313|EMBL:KGJ79007.1, ECO:0000313|Proteomes:UP000029864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RuG17 {ECO:0000313|EMBL:KGJ79007.1,
RC   ECO:0000313|Proteomes:UP000029864};
RA   Sisinthy S.;
RL   Submitted (AUG-2014) 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:KGJ79007.1}.
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DR   EMBL; JPXF01000019; KGJ79007.1; -; Genomic_DNA.
DR   RefSeq; WP_035835881.1; NZ_JPXF01000019.1.
DR   STRING; 1001240.GY21_06345; -.
DR   EnsemblBacteria; KGJ79007; KGJ79007; GY21_06345.
DR   GeneID; 36019216; -.
DR   OrthoDB; 469058at2; -.
DR   Proteomes; UP000029864; 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:KGJ79007.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110882};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029864};
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:UP000029864}.
FT   DOMAIN      117    311       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   METAL       255    255       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00281}.
SQ   SEQUENCE   337 AA;  36638 MW;  21F01DDDE753A33F CRC64;
     MAVSAAVEAA LAAISSAETS AALKAVRSEH VGESSPLAKL NGLIRTVPGD QKAAAGKLLG
     QARGRVTQAL TARETEIGEA EAIAQLAAET VDVTAAASTW KPGARHPISL LTERASDVFV
     AMGWEVAEGP ELESEWFNFD GLNFDEDHPA RAMQDTFFVE PTDAHLVLRT QTSPVQLRAL
     LSRDLPVYVV APGRVFRTDE LDATHTPVFN QIEGIAIDKG LTMAHLRGTL DHFVQALFGP
     EAKVRLRPNY FPFTEPSAEL DVWHPTFKDG ARWIEWGGCG MVHANVLRAA GIDPEVYSGF
     AFGVGVERAL MFRNDVKDMH DMVEGDIRFS QEYGMNV
//
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