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Database: UniProt
Entry: D1Y6W8_9BACT
LinkDB: D1Y6W8_9BACT
Original site: D1Y6W8_9BACT 
ID   D1Y6W8_9BACT            Unreviewed;       347 AA.
AC   D1Y6W8;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   08-MAY-2019, entry version 55.
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:EFB89973.1};
GN   ORFNames=HMPREF7215_0515 {ECO:0000313|EMBL:EFB89973.1};
OS   Pyramidobacter piscolens W5455.
OC   Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae;
OC   Pyramidobacter.
OX   NCBI_TaxID=352165 {ECO:0000313|EMBL:EFB89973.1, ECO:0000313|Proteomes:UP000006462};
RN   [1] {ECO:0000313|EMBL:EFB89973.1, ECO:0000313|Proteomes:UP000006462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W5455 {ECO:0000313|EMBL:EFB89973.1,
RC   ECO:0000313|Proteomes:UP000006462};
RA   Shrivastava S., Madupu R., Durkin A.S., Torralba M., Methe B.,
RA   Sutton G.G., Strausberg R.L., Nelson K.E.;
RL   Submitted (DEC-2009) 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:EFB89973.1}.
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DR   EMBL; ADFP01000102; EFB89973.1; -; Genomic_DNA.
DR   RefSeq; WP_009165599.1; NZ_ADFP01000102.1.
DR   STRING; 352165.HMPREF7215_0515; -.
DR   EnsemblBacteria; EFB89973; EFB89973; HMPREF7215_0515.
DR   eggNOG; ENOG4105CSS; Bacteria.
DR   eggNOG; COG0016; LUCA.
DR   OrthoDB; 469058at2; -.
DR   BioCyc; GCF_000177335-HMP:HMPREF7215_RS09360-MONOMER; -.
DR   Proteomes; UP000006462; 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:UP000006462};
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:EFB89973.1};
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:UP000006462}.
FT   DOMAIN      123    335       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   COILED       69     96       {ECO:0000256|SAM:Coils}.
FT   METAL       257    257       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00281}.
SQ   SEQUENCE   347 AA;  38265 MW;  C55220733CD6982A CRC64;
     MSSEIALGIE KIRGTIESAL KDGATLGSLN DCRIAVFGKK GAMTGLQKML GKLSPQERPE
     AGKIINGAKD EFQSKLDEAI EKLERQKLTE MELRDRVDVT QPARGRACGG AHPVVQVTMD
     VLEVLEGLGF VTVTGPEIET DFFNFEALNI PPHHPARDMQ DTFYFGDGRL LRTHTSGMEI
     HAMLDMGAPL RVACPGRVYR RDNDPTHSPM FHQVEGLVVD KNISVGDLKG CLEAMIHGVF
     GRKLKARYRA SYFPFTEPSM EVDIECFKCG GSDCRCQICK GTGWLEIGGM GMCHPNVLRY
     GGIDPDVYNG FAWGMGLDRI AMLKYGLTDL RALFDGDVSY LLSGRHE
//
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