ID A0A0S8EXD8_9GAMM Unreviewed; 760 AA.
AC A0A0S8EXD8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000256|ARBA:ARBA00017032};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000256|ARBA:ARBA00033189};
DE Flags: Fragment;
GN ORFNames=AMJ59_26475 {ECO:0000313|EMBL:KPK52846.1};
OS Gammaproteobacteria bacterium SG8_31.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1703405 {ECO:0000313|EMBL:KPK52846.1, ECO:0000313|Proteomes:UP000051321};
RN [1] {ECO:0000313|EMBL:KPK52846.1, ECO:0000313|Proteomes:UP000051321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_31 {ECO:0000313|EMBL:KPK52846.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|ARBA:ARBA00011209}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 1 subfamily. {ECO:0000256|ARBA:ARBA00008653}.
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:KPK52846.1}.
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DR EMBL; LJTI01000207; KPK52846.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8EXD8; -.
DR Proteomes; UP000051321; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
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 39..148
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
FT DOMAIN 401..476
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
FT DOMAIN 698..760
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
FT NON_TER 760
FT /evidence="ECO:0000313|EMBL:KPK52846.1"
SQ SEQUENCE 760 AA; 83341 MW; C5FC9CACE4F280A7 CRC64;
MKFSEAWLRE WVDPNMSTET LVHELTMAGL EVDGFEPVAP KFDQVVVGEV LNCEPHPEAD
KLTVCSVDAG TGAPLTIVCG APNVRAGMKT PTALEGARLP EGLRIRRAKL RGVESRGMLC
SEIELGLGDG ADGIMELPSD APTGEDLRDY LELDDTVIDV DLTPNRGDCF SILGIARETA
VKSGKTLKWP ELPAVEPEID TTFPIDVEAP EACPRFCGRV IQGIDPAART PGWMQEKLRR
SGIRSISPVV DITNYVMMEL GQPLHGFDLD TLQDGIIVRF ANRGEKLVLL DGRQVNLDDD
MLVIADHRGP RALAGIMGGE ASGVSDGTVN VFFEVAFFNP AYISGRPRRL GLHTDASLRF
ERGVDPAGQR RAIERATELL TSIAGGQPGP VTEAMSAEHL PERPGVKLRS ARLAAVLGVE
IDGDEVESIL TSLGMKTAAE NGGWLVTPPS WRFDFVVEED LIEEVARVHG YDSIPETPAR
GDTTFSPVTE TVVSQEVVDR ALVDRGYREV VTYSFVDERI QSLLFPDVTP IRLNNPISSE
MSDMRVSLWP GMIGVLRQNL SRQLERVRIF ESGLKFFLQD GEIRQVPCLA ALMAGPRVAE
QWSAKREDGD FFDLKGDLEA VLSLTGAAGQ FRFIPDTHPA LHPGQSARIC RGDLDVGWIG
ALHPALASRF DISINPYLFE IETDIGLESL VPEYTEISRY PVVRRDLAVL VEERISSESL
IKEVLEGGGK LLREVRIFDV YRGDRIDSGL KSVAFSLILQ
//
