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Database: UniProt
Entry: A0A1J5JAL5_9EURY
LinkDB: A0A1J5JAL5_9EURY
Original site: A0A1J5JAL5_9EURY 
ID   A0A1J5JAL5_9EURY        Unreviewed;       491 AA.
AC   A0A1J5JAL5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   10-APR-2019, entry version 12.
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=AUK59_02080 {ECO:0000313|EMBL:OIQ05900.1};
OS   Candidatus Altiarchaeum sp. CG2_30_32_3053.
OC   Archaea; Euryarchaeota; Candidatus Altiarchaeales;
OC   Candidatus Altiarchaeum.
OX   NCBI_TaxID=1803514 {ECO:0000313|EMBL:OIQ05900.1, ECO:0000313|Proteomes:UP000182290};
RN   [1] {ECO:0000313|EMBL:OIQ05900.1, ECO:0000313|Proteomes:UP000182290}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG2_30_32_3053 {ECO:0000313|EMBL:OIQ05900.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C.,
RA   Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO
RT   concentrations.";
RL   Environ. Microbiol. 0:0-0(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:OIQ05900.1}.
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DR   EMBL; MNZY01000069; OIQ05900.1; -; Genomic_DNA.
DR   Proteomes; UP000182290; 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:UP000182290};
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}.
FT   DOMAIN      238    476       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
SQ   SEQUENCE   491 AA;  57542 MW;  1FD9318BDA9D571D CRC64;
     MDNFHPNELK ILKILEGRQN IKKISERANL STDAVARTID WLKTKNLVNV SEKIQKFVFL
     NDEGKEYLSR GLPERQLLNL IKAKNISEIT IDDLIKIIDE NNLKVNVHLT IGWLRRKKHI
     VFKDRVIVFS DFAVRDDEIL LKNTDKRDLN TLSDAEKKSY EILNSRKIIN LKETREIFAS
     LTDEGIKIKE NIAGLKEQIS QLTPEMLTKK SWKGAEFRKY DVSVFVEPQY LAKFHPLTNL
     INDIREIFVG MGFKEMRGNL IEPTFWDFDA LFQPQDHPAR DMQDTFYLKN FVHEVDGFEK
     FKNPIRDAHE KGWKYQWNEE EAKKFILRTH TTAVSAHFIT TLKKHDLPAK IFTIGKVFRN
     ETIDFKHLPE FYQVEGIVVS EDVNFRNLLG ILKNFYNSLG FEKIRFRPGY FPYTEMSIEP
     EIYLESKEQW IELGGAGIFR QEVVKPLLGF ECPVLAWGLG LDRIAALRLN LSDIRDLYIS
     DIDWLRKVKV I
//
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