ID A0K0B5_ARTS2 Unreviewed; 385 AA.
AC A0K0B5;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN OrderedLocusNames=Arth_3360 {ECO:0000313|EMBL:ABK04735.1};
OS Arthrobacter sp. (strain FB24).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=290399 {ECO:0000313|EMBL:ABK04735.1, ECO:0000313|Proteomes:UP000000754};
RN [1] {ECO:0000313|Proteomes:UP000000754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB24 {ECO:0000313|Proteomes:UP000000754};
RX PubMed=24501649; DOI=10.4056/sigs.4438185;
RA Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL Stand. Genomic Sci. 9:106-116(2013).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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DR EMBL; CP000454; ABK04735.1; -; Genomic_DNA.
DR RefSeq; WP_011693185.1; NC_008541.1.
DR AlphaFoldDB; A0K0B5; -.
DR STRING; 290399.Arth_3360; -.
DR KEGG; art:Arth_3360; -.
DR eggNOG; COG0016; Bacteria.
DR HOGENOM; CLU_022696_2_0_11; -.
DR OrthoDB; 489670at2; -.
DR Proteomes; UP000000754; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0043039; P:tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.30.70.380; Ferrodoxin-fold anticodon-binding domain; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005121; Fdx_antiC-bd.
DR InterPro; IPR036690; Fdx_antiC-bd_sf.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR PANTHER; PTHR11538:SF41; PHENYLALANINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SMART; SM00896; FDX-ACB; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS51447; FDX_ACB; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:ABK04735.1};
KW Ligase {ECO:0000313|EMBL:ABK04735.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000754}.
FT DOMAIN 275..385
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
SQ SEQUENCE 385 AA; 42382 MW; 1260A9B9FDBF388D CRC64;
MKNYLSLTEL NTALALRDLT DPDAGAHAMQ QLLADVVTAL ERQWDIPSET HRLNPLVAIA
DNYDRLGYSP GDATRESRYS RHISPTVMLR SHTSAGIPAI LDSLRGEQGR YDRLHVLPGL
VYRRDAVDRT HVGTPHQVDV WRIKARGLLG PSHLQAMMAA VVDAVLPAAD HPGVQWRATP
SAHSYTAAGR QLDVLVTLQD GRREWLELAE CGLVAAPVLR SSGLDPRRWA GLALGMGLDR
ALMLRKGIDD IRLLRSKNPE IQGQLLDLAP YRPVSLMPPV RRDLSLVLAD PAEADIELLG
DRARRVLGDD AEVLAALEIK AVTPTAELPP AAVDRLRMAP GDVNVLLRLV LQPLERTLTD
QQANRLRDRV YIALHQGKVQ ELIAG
//
