ID A0A1G1GDN4_9BACT Unreviewed; 868 AA.
AC A0A1G1GDN4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE RecName: Full=Alanine--tRNA ligase {ECO:0000256|ARBA:ARBA00017959};
DE EC=6.1.1.7 {ECO:0000256|ARBA:ARBA00013168};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00032577};
DE Flags: Fragment;
GN ORFNames=A2010_06065 {ECO:0000313|EMBL:OGW42002.1};
OS Nitrospirae bacterium GWD2_57_9.
OC Bacteria; Nitrospirota.
OX NCBI_TaxID=1801701 {ECO:0000313|EMBL:OGW42002.1, ECO:0000313|Proteomes:UP000176220};
RN [1] {ECO:0000313|EMBL:OGW42002.1, ECO:0000313|Proteomes:UP000176220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGW42002.1}.
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DR EMBL; MHED01000023; OGW42002.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1GDN4; -.
DR Proteomes; UP000176220; 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; 2.40.30.130; -; 1.
DR Gene3D; 3.10.310.40; -; 1.
DR Gene3D; 3.30.54.20; -; 1.
DR Gene3D; 6.10.250.550; -; 1.
DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 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; IPR023033; Ala_tRNA_ligase_euk/bac.
DR InterPro; IPR003156; DHHA1_dom.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR NCBIfam; TIGR00344; alaS; 1.
DR PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02272; DHHA1; 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 SUPFAM; SSF50447; Translation proteins; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OGW42002.1};
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..702
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT COILED 718..752
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGW42002.1"
SQ SEQUENCE 868 AA; 95386 MW; 72C9E55169202C0D CRC64;
DFFAAKNHKI VPSSALVPRN DPTLLFTNAG MVQFKGLFLG EETRAYQRAV TSQKCMRAGG
KHNDLENVGH TARHHTFFEM LGNFSFGDYF KKDAIAFAWE LLTAQLKLPK EKLWVTIYKD
DDEAFKLWQD VAGVAADRIV RLGEKDNFWQ MGDTGPCGPC SEILIDQGPE VGCGKSACAV
GCDCDRYLEI WNLVFMQFNR DETGKLTPLP KPSIDTGMGL ERLSAVVQGV KSNFETDLFQ
PIIRQIAAVA GVPYHKDQQA DISYQVIADH LRAMTFLISD GVLPSNEGRG YVLRRVIRRA
SRYGKLIGVE KPFLFKLTGV VVDEMREAYP ELVDSREHVA RVVLLEEERF ATTLTSGLAL
LNETVAKIKA GHKNVIPGDV LFKLYDTFGF PLDLVTDMAR DMELELDNEG YQKAMQEQRD
KARAAWAGSG EAKVKPVYKE VAAGIKKPQF TGYDLTQDNG QIIAIIKEGR KASEAHEGDE
VEIVLDRTPF YAESGGQVGD KGDLLGEATK FAVDDTVKPV EDLVVHRGKL KKGGLKLGDT
VLARVDEAGR GDTARHHTAT HLLHATLRYV LGDHVKQSGS LVSPERLRFD FTHYTAMTDR
EIARVEELIN EYIRENHPVQ TQVLDVEQAV ASGAMALFDE KYGDKVRVVS VKDVSKELCG
GTHTRASGDI GVFKVLSEAG IAAGVRRIEA VAGRQAYEAF KREEQGLHDI AQLLKTTDQD
AVSRVEKLLS QAKALEKELD QFKHKLQSSQ AGDIATDAQT VNGVKVLARR AEGLDAKDLR
DFADKLRDKL GSGILALGSA KDDKVSLIVM VSKDLTGRFN AGTIIKEMAL ILGGTGGGKP
DLAQAGGKDA AKLEPALEAL YGIIKRGK
//