ID A0A1H1EXQ7_9EURY Unreviewed; 579 AA.
AC A0A1H1EXQ7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00284};
DE EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00284};
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00284};
DE Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00284};
GN Name=pheT {ECO:0000256|HAMAP-Rule:MF_00284};
GN ORFNames=DWB78_09450 {ECO:0000313|EMBL:RDI71929.1}, SAMN05216278_3108
GN {ECO:0000313|EMBL:SDQ93314.1};
OS Halopelagius longus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae.
OX NCBI_TaxID=1236180 {ECO:0000313|EMBL:SDQ93314.1, ECO:0000313|Proteomes:UP000199289};
RN [1] {ECO:0000313|EMBL:SDQ93314.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12397 {ECO:0000313|EMBL:SDQ93314.1};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000199289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12397 {ECO:0000313|Proteomes:UP000199289};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RDI71929.1, ECO:0000313|Proteomes:UP000255421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC12-B1 {ECO:0000313|EMBL:RDI71929.1,
RC ECO:0000313|Proteomes:UP000255421};
RA Zhang X.;
RT "Genome sequence of extremly halophilic archaeon Halopelagius longus strain
RT BC12-B1.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) +
CC L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668,
CC Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00284};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00284};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00284}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00284}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 2 subfamily. {ECO:0000256|ARBA:ARBA00007438,
CC ECO:0000256|HAMAP-Rule:MF_00284}.
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DR EMBL; QQST01000001; RDI71929.1; -; Genomic_DNA.
DR EMBL; FNKQ01000003; SDQ93314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1EXQ7; -.
DR OrthoDB; 10073at2157; -.
DR Proteomes; UP000199289; Unassembled WGS sequence.
DR Proteomes; UP000255421; 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:InterPro.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00769; PheRS_beta_core; 1.
DR Gene3D; 3.30.56.10; -; 2.
DR Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 1.
DR HAMAP; MF_00284; Phe_tRNA_synth_beta2; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005146; B3/B4_tRNA-bd.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR InterPro; IPR004531; Phe-tRNA-synth_IIc_bsu_arc_euk.
DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR InterPro; IPR022918; Phe_tRNA_ligase_beta2_arc.
DR InterPro; IPR041616; PheRS_beta_core.
DR InterPro; IPR005147; tRNA_synthase_B5-dom.
DR NCBIfam; TIGR00471; pheT_arch; 1.
DR PANTHER; PTHR10947:SF0; PHENYLALANINE--TRNA LIGASE BETA SUBUNIT; 1.
DR PANTHER; PTHR10947; PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47; 1.
DR Pfam; PF03484; B5; 1.
DR Pfam; PF17759; tRNA_synthFbeta; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 2.
DR PROSITE; PS51483; B5; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00284};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00284}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00284};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00284};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00284};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00284};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00284};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00284}.
FT DOMAIN 284..371
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00284"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00284"
FT BINDING 358
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00284"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00284"
SQ SEQUENCE 579 AA; 64336 MW; 3380B353B712342C CRC64;
MPVVDVHPDE LRQLTGHEDK SDEEFVDDLF ALGLEFEGET EDGAFQLEFG PDRLDRLSVE
GVARSLRYQY GDDRGVYVPN TNNPDYTFVV DEDVPDERPY VTGAIIRGVD LDEDALDSLI
QLQEKLHATM GRQRAKGAIG IHDLTMIKGE VLSEEGGGNS ITYTGIDPDG DTFVPLDSDA
ELSPAEVLEE HATGREYADL VSEYDRYPAI YDELGLFSFP PVINGRRTEV STDSRELLVE
LTGTDQWTID RMCNIICYAL SARGATIEEV EVEYPDGTLL RPDFEVETKR VSHDRIETML
GVEFEKREVA DLFERSGLGV ELADDESGGD GAGEDGTVYE VSIPPYRVDV LHPLDLVDDV
GRAYGFNELE PRYPDVGTVG ERHERSRLED ATRNTLVGLG FEDLLNFHMT NEDALTTRMN
VEEGDEVLGG GEPARITEPY SEDYTVLRTW ALPSLMMVLE NNTHRAYPQD LAEIGFVAER
DDDVNTRVRE RRHVAAVLAR HDATYEDAKA RLQSLCSDFG VELETPATSH PSFIDGRAAS
VVIDGEDVGV VGEIHPTVLV EHDLELPVAA FEFDLNALA
//
