ID A0A1Q3NN35_9BACT Unreviewed; 627 AA.
AC A0A1Q3NN35;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE RecName: Full=alanine--tRNA ligase {ECO:0000256|ARBA:ARBA00013168};
DE EC=6.1.1.7 {ECO:0000256|ARBA:ARBA00013168};
GN ORFNames=BGO18_03605 {ECO:0000313|EMBL:OJU97227.1};
OS Candidatus Saccharibacteria bacterium 47-87.
OC Bacteria; Candidatus Saccharibacteria.
OX NCBI_TaxID=1895828 {ECO:0000313|EMBL:OJU97227.1, ECO:0000313|Proteomes:UP000185868};
RN [1] {ECO:0000313|EMBL:OJU97227.1, ECO:0000313|Proteomes:UP000185868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47-87 {ECO:0000313|EMBL:OJU97227.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OJU97227.1}.
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DR EMBL; MKSO01000001; OJU97227.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3NN35; -.
DR STRING; 1895828.BGO18_03605; -.
DR Proteomes; UP000185868; 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:OJU97227.1};
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..627
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
SQ SEQUENCE 627 AA; 70953 MW; 2FE447179D38392E CRC64;
MNAQEIRNSY LEFFKERGHA IVKRAPLLLK DDPSTLFTGS GMQPMIPYLL GQPHPEGARI
ADSQTSLRAQ DIDDIGDNRH TTFFEMLGNW SMGDYFKEQQ IEWMFEWLSE VVKLDMSRLY
VTAFIGAPEY GIEKDTEAAA VWKRLFEARG IQAEEAEIGS EEDGYARGIK EGERIFYYDG
SKNWWSRNGK PETTPVGDPC GPDSEMFYDF GTPHDPSFGE FCHPNCDCGR FMEIGNNVFM
AYRKVAEGQF EPLEKPNIDH GSGLERIAAA AIDSPDVFRI SVMWPIIEKL EKLSGKSYES
NTTSMRVIAD HLRAATFLAV DGCVPANKEQ GYVMRRLLRR AIRFAFDLGI EQNFFEEIVP
VIADLYQADY PEVAENRDTI IAVLVKEEKV FRQTLRKGLQ QLGKFAADGV VTGNELFTLY
DTYGFPVELS TEEAFKQAIA LSENWREEFD AKMEEQRNRS RTATKGEFKG GLGGQDLIHK
KYHTATHLLQ SALREIFGPE LRQHGSNITE ERLRFDFNLD HKMTPEEIAK AEELVNGWIA
EDLPVSFKLY PTQEALDMGA IGPFGERYAE EVKVYQMGEG DHIASLEICG GPHVDHTGQL
AEDGKKFKIT KEEASSAGIR RIKAVLV
//
