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Database: UniProt
Entry: A0A1G1GDN4_9BACT
LinkDB: A0A1G1GDN4_9BACT
Original site: A0A1G1GDN4_9BACT 
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
//
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