(data stored in ACNUC29543 zone)

SWISSPROT: SYS_SYNR3

ID   SYS_SYNR3               Reviewed;         425 AA.
AC   A5GRE1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 75.
DE   RecName: Full=Serine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00176};
DE            EC=6.1.1.11 {ECO:0000255|HAMAP-Rule:MF_00176};
DE   AltName: Full=Seryl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00176};
DE            Short=SerRS {ECO:0000255|HAMAP-Rule:MF_00176};
DE   AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000255|HAMAP-Rule:MF_00176};
GN   Name=serS {ECO:0000255|HAMAP-Rule:MF_00176};
GN   OrderedLocusNames=SynRCC307_0547;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00176}.
CC   -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer.
CC       {ECO:0000255|HAMAP-Rule:MF_00176}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00176}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type-1 seryl-tRNA synthetase subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00176}.
DR   EMBL; CT978603; CAK27450.1; -; Genomic_DNA.
DR   RefSeq; WP_011934965.1; NC_009482.1.
DR   SMR; A5GRE1; -.
DR   STRING; 316278.SynRCC307_0547; -.
DR   EnsemblBacteria; CAK27450; CAK27450; SynRCC307_0547.
DR   KEGG; syr:SynRCC307_0547; -.
DR   eggNOG; ENOG4105CGR; Bacteria.
DR   eggNOG; COG0172; LUCA.
DR   HOGENOM; HOG000035938; -.
DR   KO; K01875; -.
DR   OMA; SPCFRRE; -.
DR   OrthoDB; 353391at2; -.
DR   BioCyc; SSP316278:G1GJL-534-MONOMER; -.
DR   UniPathway; UPA00906; UER00895.
DR   Proteomes; UP000001115; 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:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00770; SerRS_core; 1.
DR   Gene3D; 1.10.287.40; -; 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; 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   PANTHER; PTHR43697; PTHR43697; 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; SSF46589; SSF46589; 1.
DR   TIGRFAMs; TIGR00414; serS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GRE1.
DR   SWISS-2DPAGE; A5GRE1.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..425
FT                   /note="Serine--tRNA ligase"
FT                   /id="PRO_1000019850"
FT   NP_BIND         264..266
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   NP_BIND         351..354
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   REGION          233..235
FT                   /note="Serine binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   BINDING         287
FT                   /note="Serine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   BINDING         385
FT                   /note="Serine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
SQ   SEQUENCE   425 AA;  47543 MW;  72BB71DE409ED4EC CRC64;
     MLDQRLLRDN PELISQQLGR RGMEVDLTKL QLIAKQERDL EEQRSNLQAE GNRTGKEVGM
     LIKGGAAPDS DEVKALREKG NRIKQQVAVL EEEEKGLEAK LREQLLALPN LPSADAPEGK
     SEADNVEVKR WGEPRQGKDL EEHWQLADRL GLFETERSVR IAQSRFITLM GDGARLERAL
     ISFMLDLHST KGYTEVMPPI LVNSASLTGS GQLPKFAEES FRCADDDLWL TPTAEVPLTS
     LHRDEVIAVE QLPLKYAAYT PCFRREAGSY GRDTRGLIRL HQFNKVELYW FCHPEKSAEA
     HEQLTLDAEA VLEALELPYR RLELCTGDMG FSAARTYDLE VWLPGAGSYR EISSCSTCGD
     FQARRSAIRF KEGKGTQLLH TLNGSGLAIG RTMAALLENG QQPDGSIQLP AALVPYFGRE
     RLTPQ
//

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