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Database: UniProt
Entry: A0A0G0MQV2_9BACT
LinkDB: A0A0G0MQV2_9BACT
Original site: A0A0G0MQV2_9BACT 
ID   A0A0G0MQV2_9BACT        Unreviewed;       421 AA.
AC   A0A0G0MQV2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Serine--tRNA ligase {ECO:0000256|ARBA:ARBA00039158};
DE            EC=6.1.1.11 {ECO:0000256|ARBA:ARBA00012840};
DE   AltName: Full=Seryl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031113};
DE   AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000256|ARBA:ARBA00033352};
GN   ORFNames=US86_C0001G0223 {ECO:0000313|EMBL:KKQ67296.1};
OS   Candidatus Daviesbacteria bacterium GW2011_GWA2_38_24.
OC   Bacteria; Candidatus Daviesbacteria.
OX   NCBI_TaxID=1618422 {ECO:0000313|EMBL:KKQ67296.1, ECO:0000313|Proteomes:UP000034235};
RN   [1] {ECO:0000313|EMBL:KKQ67296.1, ECO:0000313|Proteomes:UP000034235}
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   -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC       biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005045}.
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:KKQ67296.1}.
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DR   EMBL; LBUP01000001; KKQ67296.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0MQV2; -.
DR   PATRIC; fig|1618422.5.peg.227; -.
DR   Proteomes; UP000034235; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00770; SerRS_core; 1.
DR   Gene3D; 1.10.287.40; Serine-tRNA synthetase, tRNA binding domain; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR002317; Ser-tRNA-ligase_type_1.
DR   InterPro; IPR015866; Ser-tRNA-synth_1_N.
DR   InterPro; IPR042103; SerRS_1_N_sf.
DR   InterPro; IPR033729; SerRS_core.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   NCBIfam; TIGR00414; serS; 1.
DR   PANTHER; PTHR43697:SF1; SERINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43697; SERYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02403; Seryl_tRNA_N; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
DR   PRINTS; PR00981; TRNASYNTHSER.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF46589; tRNA-binding arm; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   4: Predicted;
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:KKQ67296.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          125..406
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   COILED          30..83
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   421 AA;  48278 MW;  7F9764986ADCCE30 CRC64;
     MLDINFIREN KEKVIDAAKQ KGVDIDINRL LEVDQTRREL IKKVDDLRAQ RNEAAKNRDI
     EKGRQIKSEL DTWELELKEA QERFEHQMSF IPNVPLPAVP RGDESNNKVI KKAGEVPNFN
     FTVRDHLELA EMLDIVDIPR ATKVSGSRFY YLKNEGVLLE LALLQYALKK LMAEGFSPIF
     PPALIKQDIT QGLGYWAGGN HNNYYLVQDF EEVEKGVENP NPLYLIGTAE HALVPMHKDE
     VFKEEALPKK YVGFSPSFRR EAGTYGKDTR GILRVHQFNK VEMVAFVRVE DDQETRKHLL
     NLAESFMQDL RLPYQVVQLA SGDTSFPAAE TIDIETWLPG QDKYRETHSI STTTDFQARR
     LNIKYKDQSG QMKFVYILNG TAFAIGRTLI AILENYQQED GSVKVPEVLI PYTGFDVIKP
     K
//
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