ID A0A0G0KUA3_9BACT Unreviewed; 591 AA.
AC A0A0G0KUA3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE RecName: Full=alanine--tRNA ligase {ECO:0000256|ARBA:ARBA00013168};
DE EC=6.1.1.7 {ECO:0000256|ARBA:ARBA00013168};
GN ORFNames=US99_C0003G0011 {ECO:0000313|EMBL:KKQ79090.1};
OS Candidatus Daviesbacteria bacterium GW2011_GWF2_38_6.
OC Bacteria; Candidatus Daviesbacteria.
OX NCBI_TaxID=1618432 {ECO:0000313|EMBL:KKQ79090.1, ECO:0000313|Proteomes:UP000034324};
RN [1] {ECO:0000313|EMBL:KKQ79090.1, ECO:0000313|Proteomes:UP000034324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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:KKQ79090.1}.
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DR EMBL; LBVC01000003; KKQ79090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0KUA3; -.
DR PATRIC; fig|1618432.3.peg.46; -.
DR Proteomes; UP000034324; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00673; AlaRS_core; 1.
DR Gene3D; 3.30.54.20; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR012947; tRNA_SAD.
DR PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR00980; TRNASYNTHALA.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF101353; Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS); 1.
DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 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, ECO:0000313|EMBL:KKQ79090.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 1..591
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
SQ SEQUENCE 591 AA; 67748 MW; 70E64F33D5323FE1 CRC64;
MDSKTLRKKF LDFFEKNDHV IIPSASLVPS EEEQLAGKEK VLFTSAGMQQ LIPYLMGKPH
PKGNKLADVQ KCVRTDDIEQ VGDATHHTFF EMLGNWSLGD YWKDKAIELS FKFLTEELKI
PIEKLAISVF AGDEDAPKDE ESANKWKSLG ILGKRIAYLG KEANWWPTNS SSFGPCGPDT
EMFIWTGEGS APEEFDPKDP KWIEVWNDVF MEFNRKSDGT LEELPQKNVD TGMGLERMLA
VINGKDNDYE TDLSSSIIEK ICEELRVSYE QYKQPIRIIS DHIKASVFLI KDDVISSNKM
QGYVLRRLLR RAATKAFQIN KEFGRKPFKS LVKSVTDIYP MYFDEMSVES IEREVSIEIG
KFRKTLEKGL REVEKIEKID GKIAFDLYQT FGFPYEVTEE LFRQKGQEID KEQFKAEFEK
HQQLSRTASS GMFKGGLENH SEVVIKYHTA THLLHQALRD ILGPQVFQKG SNITAERLRF
DFSFDRKLTD SETRQVEELV NQKIKDDLKV DHMIIPLDEA KKMNAIGLFD EKYADKVSIY
GIGPQPRGRY YSLEFCGGPH VEHTGVIGKI AIFKEEAVSF GIRRIYANIA L
//
