ID U3A4L9_9EURY Unreviewed; 576 AA.
AC U3A4L9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=MBEHAL_1349 {ECO:0000313|EMBL:GAD52589.1};
OS Halarchaeum acidiphilum MH1-52-1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae.
OX NCBI_TaxID=1261545 {ECO:0000313|EMBL:GAD52589.1, ECO:0000313|Proteomes:UP000016986};
RN [1] {ECO:0000313|EMBL:GAD52589.1, ECO:0000313|Proteomes:UP000016986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16109 {ECO:0000313|EMBL:GAD52589.1,
RC ECO:0000313|Proteomes:UP000016986};
RA Shimane Y., Minegishi H., Nishi S., Echigo A., Shuto A., Konishi M.,
RA Ito T., Ohkuma M., Ohta Y., Nagano Y., Tsubouchi T., Mori K., Usui K.,
RA Kamekura M., Usami R., Takaki Y., Hatada Y.;
RT "Whole genome sequencing of Halarchaeum acidiphilum strain MH1-52-1.";
RL Submitted (SEP-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAD52589.1}.
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DR EMBL; BATA01000027; GAD52589.1; -; Genomic_DNA.
DR RefSeq; WP_020221520.1; NZ_BATA01000027.1.
DR AlphaFoldDB; U3A4L9; -.
DR eggNOG; arCOG00412; Archaea.
DR OrthoDB; 10073at2157; -.
DR Proteomes; UP000016986; 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 288..368
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
FT BINDING 346
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 352
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 356
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 576 AA; 63290 MW; 13786B16D2A4677F CRC64;
MPVVDVDPDE LRELTGHEEK GDDELKDDLF GIGLEYEGTS EDGEFQLEFA PDRLDRLSVE
GVARSLRYQY GDASGVYVPD TNDAEWTIEV ADSVPDERPC VTGAIVRGVD LSGGALESLI
QLQEKLHATM GRERTKGAIG IHDLTMVKGG SLDPDTTDAE ASNSITYRGI DPDGDTFVAL
DDDAERTPAD VLTEHPTGQT YADLLDDYER YPAIYDDLGL FSFPPVINGR RTEVTENSRN
LLVELTGTDQ WTIDRMCNII CYALDARGGT IEDVTVSYPD TDVPKPDLET DEKVVTHERI
ESTLGIDLTE EEVLDLLGRA GLGAESEVWG EQGIDYVVEI PPYRTDVLHP VDIVDDVGRA
YGFNDLVPRY PDVSTVGGRT DRSRLERAVR ETLVGLGHQD LLNFHLTNED ENYDRMRLDP
GSDVVGGGEP ATIAEPYSED YTIVRTWALP SLMALLENNT HRAYPQDVAE VGFAAERDDS
NTGVAERRTV AGAVVRHDAS YEDAKARLQV LARDFDVELA TPETSHPTFI DGRVASVAID
GEDVGVIGEV HPEVLVEHDL EVPVAAFELR LDALAE
//
