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Database: UniProt
Entry: A0A133V440_9EURY
LinkDB: A0A133V440_9EURY
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ID   A0A133V440_9EURY        Unreviewed;       492 AA.
AC   A0A133V440;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   10-APR-2019, entry version 15.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00282};
DE            EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00282};
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00282};
DE            Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00282};
GN   Name=pheS {ECO:0000256|HAMAP-Rule:MF_00282};
GN   ORFNames=AKJ41_02350 {ECO:0000313|EMBL:KXB01218.1};
OS   candidate division MSBL1 archaeon SCGC-AAA259O05.
OC   Archaea; Euryarchaeota; candidate division MSBL1.
OX   NCBI_TaxID=1698271 {ECO:0000313|EMBL:KXB01218.1, ECO:0000313|Proteomes:UP000070344};
RN   [1] {ECO:0000313|EMBL:KXB01218.1, ECO:0000313|Proteomes:UP000070344}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC-AAA259O05 {ECO:0000313|EMBL:KXB01218.1};
RX   PubMed=26758088; DOI=10.1038/srep19181;
RA   Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W.,
RA   Anthony Kamau A., Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V.,
RA   Stingl U.;
RT   "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT   pools of the Red Sea.";
RL   Sci. Rep. 6:19181-19181(2016).
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_00282};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00282};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP-
CC       Rule:MF_00282};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00282}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00282}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00282}.
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:KXB01218.1}.
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DR   EMBL; LHXV01000021; KXB01218.1; -; Genomic_DNA.
DR   EnsemblBacteria; KXB01218; KXB01218; AKJ41_02350.
DR   PATRIC; fig|1698271.3.peg.632; -.
DR   Proteomes; UP000070344; 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   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_00282; Phe_tRNA_synth_alpha2; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR   InterPro; IPR022917; Phe_tRNA_ligase_alpha_bac/arc.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF46785; SSF46785; 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_00282};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00282};
KW   Complete proteome {ECO:0000313|Proteomes:UP000070344};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00282};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00282};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00282};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00282};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00282};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00282};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070344}.
FT   DOMAIN      236    490       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
SQ   SEQUENCE   492 AA;  56463 MW;  DC50A4A8B6BB5097 CRC64;
     MGELGGEAEV KNIQDLADLS QSAVMRSALS LEDEGFLEIS RESRDEIFIT DEGREYLKDS
     LPERKLLEVL AEEEFLVIDS LSENVDIPEE KIGISIGWLK RKGWAEVDTR EGEKILRITE
     DGLRALDDKE KDELLLEKFE EVESLFSDQV PSDLEAEIST LASRNLIRIR SRPSHGLNLT
     EKGKKALDFD LEAEEKVSVL SKELIRTGKW REVELRDYNV TASGPSLHPG KEHPQRRMIE
     ELRSILLRMG FKEIGGPVVE SEFWNFDALF QAQNHPAREI HDTLSLSKPE RAKILDEDLV
     ERVKRAHEQG VAGSEGWGYE FDEDVSRRTV LRSQTTADTV RHLAQNPDPP VKVFCIDKVF
     RRERIDYQHL AEFPQAEGIV MAPDLNFRHM LGYLKQILIE IGIPKIRFRP GYFPYTEPSA
     EADGYFPELD EWIELLGAGM FRPELLNPLG IDHPVLAWGI GFSRLAMIRM GIEDMRDLHN
     NDIDWLRKQP LR
//
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