ID A0A1H1TL10_9CELL Unreviewed; 857 AA.
AC A0A1H1TL10;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00283};
DE EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00283};
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00283};
DE Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00283};
GN Name=pheT {ECO:0000256|HAMAP-Rule:MF_00283};
GN ORFNames=SAMN04489860_1933 {ECO:0000313|EMBL:SDS60888.1};
OS Paraoerskovia marina.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Paraoerskovia.
OX NCBI_TaxID=545619 {ECO:0000313|EMBL:SDS60888.1, ECO:0000313|Proteomes:UP000185663};
RN [1] {ECO:0000313|EMBL:SDS60888.1, ECO:0000313|Proteomes:UP000185663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22126 {ECO:0000313|EMBL:SDS60888.1,
RC ECO:0000313|Proteomes:UP000185663};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|ARBA:ARBA00000395, ECO:0000256|HAMAP-
CC Rule:MF_00283};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00283};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP-
CC Rule:MF_00283};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00283}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00283}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 1 subfamily. {ECO:0000256|ARBA:ARBA00008653,
CC ECO:0000256|HAMAP-Rule:MF_00283}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00283}.
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DR EMBL; LT629776; SDS60888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1TL10; -.
DR STRING; 545619.SAMN04489860_1933; -.
DR eggNOG; COG0072; Bacteria.
DR eggNOG; COG0073; Bacteria.
DR OrthoDB; 9805455at2; -.
DR Proteomes; UP000185663; Chromosome i.
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:UniProtKB-UniRule.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00769; PheRS_beta_core; 1.
DR CDD; cd02796; tRNA_bind_bactPheRS; 1.
DR Gene3D; 3.30.56.10; -; 2.
DR Gene3D; 3.30.70.380; Ferrodoxin-fold anticodon-binding domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 1.
DR HAMAP; MF_00283; Phe_tRNA_synth_beta1; 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; IPR005121; Fdx_antiC-bd.
DR InterPro; IPR036690; Fdx_antiC-bd_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu_bact.
DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR InterPro; IPR041616; PheRS_beta_core.
DR InterPro; IPR002547; tRNA-bd_dom.
DR InterPro; IPR033714; tRNA_bind_bactPheRS.
DR InterPro; IPR005147; tRNA_synthase_B5-dom.
DR NCBIfam; TIGR00472; pheT_bact; 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; PF03483; B3_4; 1.
DR Pfam; PF03484; B5; 1.
DR Pfam; PF03147; FDX-ACB; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR Pfam; PF17759; tRNA_synthFbeta; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SMART; SM00896; FDX-ACB; 1.
DR SUPFAM; SSF54991; Anticodon-binding domain of PheRS; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF56037; PheT/TilS domain; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR PROSITE; PS51483; B5; 1.
DR PROSITE; PS51447; FDX_ACB; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00283};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00283}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00283};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00283};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00283};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00283};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00283}; Reference proteome {ECO:0000313|Proteomes:UP000185663};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00209};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW ProRule:PRU00209}.
FT DOMAIN 41..162
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
FT DOMAIN 433..510
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
FT DOMAIN 763..856
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
FT BINDING 488
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00283"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00283"
FT BINDING 498
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00283"
SQ SEQUENCE 857 AA; 90856 MW; 1100C91752A2BD1C CRC64;
MPHIVLDWLA EHVDLPEGLG AEQLAADLVR VGLEEEEIHA AAVTGPLVVG RVLELVAEPQ
KNGKTINWCQ VDVGTHNVEG VDGAPATPRG IVCGAHNFGV GDLVVVALPG TVLPGPFAIA
SRKTYGHVSD GMICSTTELG LGDESDGIIV LGRDLLHGRT DLEPGQDAVE LLALGDEVLE
INVTPDRGYC FSYRGVAREF AHSTGVSFTD PGMPGTPPPS STPDGFPVVI DDRAPIHGLV
GCDRFVTRIV RGIDPTAPSP AWMQRRLTGS GMRPISLTVD VTNYVMLDLG QPLHAYDLAG
LAAPIVVRRA RAGERLTTLD DVDRALDPQD LLITDSPDED ASRVLGLAGV MGGASTEVTD
RTTDVLVEAA HFDPVSVART ARRHKLPSEA AKRFERGVDP RLAAVAAQRV VDLLVELGGG
TADAAVSDVD TVPGVEPIEF RVSEVERLTS LDVDEARVRS ILEEIGCTVG DTPGIGVVRV
TVPTWRPDLV GPAHLVEEVA RLVGYDEIPS VLPPAPAGRG LTRTQQLRRS VARSLAEAGY
VETLSYPFVD PAQHDALRLA ADDPRRRALR LANPLAGDRP EMRTSLLGTL LETLRRNLGR
GNDDVALYEI GRVTRPEDGA PAAPQLPGGV RPTEDQLAVL AAAVPAQPRR VAGVVAGNAD
PRGWWGPGRA GDWTDALAGA RLVADRVGVD VVVTPDTDHA PWHPGRCARL SLVDGTVVGH
AGELHPKALE NLGLPARTVA FEVDLDVLLD AVEAEPFAAR PVSTFPAAKE DLALVVEESV
PADQVRQALV DGAGDLLEHV ELFDVFRGEQ LGEGRKSLAF ALRLRAADRT LSADEVVEVR
RAAVAAAQEQ TGATLRA
//
