ID A1QZU8_BORT9 Unreviewed; 515 AA.
AC A1QZU8;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN OrderedLocusNames=BT0513 {ECO:0000313|EMBL:AAX17840.1};
OS Borrelia turicatae (strain 91E135).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borrelia.
OX NCBI_TaxID=314724 {ECO:0000313|EMBL:AAX17840.1, ECO:0000313|Proteomes:UP000001205};
RN [1] {ECO:0000313|Proteomes:UP000001205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91E135 {ECO:0000313|Proteomes:UP000001205};
RA Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA Schwan T.G.;
RT "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT comparative analysis of two agents of endemic N. America relapsing fever.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Phe-tRNA synthetase alpha subunit type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00006703}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000049; AAX17840.1; -; Genomic_DNA.
DR RefSeq; WP_011772458.1; NZ_CP073176.1.
DR AlphaFoldDB; A1QZU8; -.
DR KEGG; btu:BT0513; -.
DR eggNOG; COG0016; Bacteria.
DR eggNOG; COG3398; Bacteria.
DR HOGENOM; CLU_025086_2_2_12; -.
DR Proteomes; UP000001205; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00496; PheRS_alpha_core; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR NCBIfam; TIGR00468; pheS; 1.
DR PANTHER; PTHR11538:SF40; PHENYLALANINE--TRNA LIGASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000313|EMBL:AAX17840.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 263..500
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 515 AA; 58111 MW; F47697C8F73C2476 CRC64;
MKNRFEVVRT LHPLEIKVIL NYKEGDEIFA LRLVADLLYN EGQSNKTIEW LVSKGILRET
FRKLNVFYRL TERGVDALAN GLVEERIINL VSRKTVLVAN LPSELEIDAR DAGKAFGNLS
KEGVLSLGLG KEILVKDLNR SSYNIVKELL SKAQNSDLLE DDLSQDELLV ISNYSKKKGA
GDVLFKVIES LDLKFEFSKF GLEVKSELGR SNLTGDEIVK LTPEMLKNKT YENKNFRAYN
IHVSSNKTFI GRANPYSEYI AKVKDKLVSL GFEEFDGPLV ESEFFNNDAL FMPQFHPARD
IRDVYYIKEP SSLKSLPEPY FSNVKAVHED GYTTGSRGWR YDFSESISKR LVLRSQGTVL
SAKQLIDAKN PGKYFGIVRC FRYDQVDATH GADFYQTEGI VIGDVNIKTL LGLLEIFAKE
LAGATEVKYV PAYFPFTEPS IEVHVKHPVL GWFELGGSGI FRPEVTKPFG IDVPVIAWGI
GIDRMALMHL GLSDLRELFT HNIGDVVLRR GKVNA
//
