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Database: UniProt
Entry: A0A0P0GGQ3_9BACT
LinkDB: A0A0P0GGQ3_9BACT
Original site: A0A0P0GGQ3_9BACT 
ID   A0A0P0GGQ3_9BACT        Unreviewed;       428 AA.
AC   A0A0P0GGQ3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Serine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00176};
DE            EC=6.1.1.11 {ECO:0000256|HAMAP-Rule:MF_00176};
DE   AltName: Full=Seryl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00176};
DE            Short=SerRS {ECO:0000256|HAMAP-Rule:MF_00176};
DE   AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000256|HAMAP-Rule:MF_00176};
GN   Name=serS {ECO:0000256|HAMAP-Rule:MF_00176,
GN   ECO:0000313|EMBL:ALJ56831.1};
GN   ORFNames=AMD24_00666 {ECO:0000313|EMBL:ALJ56831.1};
OS   Candidatus Xiphinematobacter sp. Idaho Grape.
OC   Bacteria; Verrucomicrobiota; Spartobacteria; Candidatus Xiphinematobacter.
OX   NCBI_TaxID=1704307 {ECO:0000313|EMBL:ALJ56831.1, ECO:0000313|Proteomes:UP000062177};
RN   [1] {ECO:0000313|EMBL:ALJ56831.1, ECO:0000313|Proteomes:UP000062177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Idaho Grape {ECO:0000313|EMBL:ALJ56831.1,
RC   ECO:0000313|Proteomes:UP000062177};
RX   PubMed=26362082; DOI=10.1093/gbe/evv176;
RA   Brown A.M., Howe D.K., Wasala S.K., Peetz A.B., Zasada I.A., Denver D.R.;
RT   "Comparative Genomics of a Plant-Parasitic Nematode Endosymbiont Suggest a
RT   Role in Nutritional Symbiosis.";
RL   Genome Biol. Evol. 7:2727-2746(2015).
CC   -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able
CC       to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-
CC       seryl-tRNA(Sec), which will be further converted into selenocysteinyl-
CC       tRNA(Sec). {ECO:0000256|HAMAP-Rule:MF_00176}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-
CC         seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742,
CC         Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00176};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-
CC         seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669,
CC         Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00176};
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, ECO:0000256|HAMAP-Rule:MF_00176}.
CC   -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer.
CC       {ECO:0000256|HAMAP-Rule:MF_00176}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176}.
CC   -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N-
CC       terminal extension that is involved in tRNA binding.
CC       {ECO:0000256|HAMAP-Rule:MF_00176}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type-1 seryl-tRNA synthetase subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00176}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00176}.
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DR   EMBL; CP012665; ALJ56831.1; -; Genomic_DNA.
DR   RefSeq; WP_062100651.1; NZ_CP012665.1.
DR   AlphaFoldDB; A0A0P0GGQ3; -.
DR   STRING; 1704307.AMD24_00666; -.
DR   KEGG; xii:AMD24_00666; -.
DR   PATRIC; fig|1704307.3.peg.742; -.
DR   OrthoDB; 9804647at2; -.
DR   UniPathway; UPA00906; UER00895.
DR   Proteomes; UP000062177; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00770; SerRS_core; 1.
DR   Gene3D; 1.10.287.40; Serine-tRNA synthetase, tRNA binding domain; 1.
DR   HAMAP; MF_00176; Ser_tRNA_synth_type1; 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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00176};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00176}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00176};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00176};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00176}; Reference proteome {ECO:0000313|Proteomes:UP000062177}.
FT   DOMAIN          140..412
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          113..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         234..236
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT   BINDING         265..267
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT   BINDING         288
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT   BINDING         352..355
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT   BINDING         387
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
SQ   SEQUENCE   428 AA;  47681 MW;  81D6B3CE503FF3AA CRC64;
     MLDIRLIREN SGLIKAKLAA RGKSLDAAID AVLECDADCR LAKTRLQLLY AERRRLSRQV
     EKLRRGEGGA PLQAEATANS LGEEINALNS RTTELNLRQK DLLLQLPNLP EEAVPHGTSA
     SANPTLRTWG NPSEKSTTED HVAIGRRLGL FDFNRAAKIS GSGFLCFTGA GARLERSLLN
     FLLDLHTVQH GYREVNTPLL VHRECMVGTG QLPKFEEDMY AVNGDSSRLF LAPTAEVPVT
     NLYRDEVLNI SHLPLCFVAY TPCFRREAGS AGRDTRGMIR LHQFDKVELV KICEVEDSEQ
     ELQSLTVDVE KVLQLLDLPY RVVELCTGDL GFSASHTYDI EVWSPGQGSF LEVSSCSNFR
     DFQSRRMNLR YKDFNGKSRF AHTLNGSGTA LPRLYVALLE NHVQSDGSVL LPQSLRGYFR
     ADCIEPVS
//
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