ID A0A1J5GP64_9BACT Unreviewed; 654 AA.
AC A0A1J5GP64;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN ORFNames=AUK08_02525 {ECO:0000313|EMBL:OIP74107.1};
OS Candidatus Pacebacteria bacterium CG2_30_36_39.
OC Bacteria; Candidatus Paceibacterota.
OX NCBI_TaxID=1805300 {ECO:0000313|EMBL:OIP74107.1, ECO:0000313|Proteomes:UP000182294};
RN [1] {ECO:0000313|EMBL:OIP74107.1, ECO:0000313|Proteomes:UP000182294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_36_39 {ECO:0000313|EMBL:OIP74107.1};
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., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:OIP74107.1}.
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DR EMBL; MNZB01000003; OIP74107.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5GP64; -.
DR STRING; 1805300.AUK08_02525; -.
DR Proteomes; UP000182294; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.30.56.10; -; 2.
DR Gene3D; 3.30.70.380; Ferrodoxin-fold anticodon-binding domain; 1.
DR Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 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; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR InterPro; IPR041616; PheRS_beta_core.
DR InterPro; IPR005147; tRNA_synthase_B5-dom.
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; 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; SSF56037; PheT/TilS domain; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 2.
DR PROSITE; PS51483; B5; 1.
PE 4: Predicted;
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}.
FT DOMAIN 298..373
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
SQ SEQUENCE 654 AA; 74134 MW; 674171CE4D85D35D CRC64;
MNILIPHKWL LEQLETELSP TKIQEYVSLC GPSIERIYER GNDKVYDIEI TTNRVDSMSV
RGVAREAAVI LGQFDIPAKL AKQNLTLKNL KENNLLPLPK IIDPHKFCKR TLCVVLQNVK
RTVTPKWMAD RLTQVEMNIH DSAIDITNYV THELGHPIHA FDYDRIMALG GEIHVTEAKK
GEAFVTLDGE LHSCVGGEIV FKNSKGEIID LPAIKGTANS SVNADTKNIL LWIESLEPSK
IRFASMSHAI RTVAAQLSEK GIDPHLAEPT FVRAIELYQD LCEATVASKI HDDFSGEEQP
QPIIFDKEKI DIYLGLEIEK ERIVEILKKL ECKVEVIRNT FHIVPPTFRK DLQIPADIVE
EIARIHGYHN LPSVLMPTKI PLTKPKDLNF SAEETIKHFL ADRGWFEIYT YSMVSEKIAQ
QSGFQITRHL QLANSLTEDK VYLRRSLSPS LQETIANNPQ VENLSVFELA NVYHPQENEL
PNETMLLSLV SQKPLAIVKG DFEALLRKFY LTKPVVKQKN GESYGEILVD SIKIGRIWLE
NNLTCIEIEL AILLPLVKQH PNYQPLPKTS SIKESLTFTL PVETQIGPVI DEIAGLSQYI
KSVTLEDVYQ QNCSFGIEYW DQKKNLANEN IKPLREKVVA MVTKQFNGKL VGKL
//
