SYS_AQUAE
ID SYS_AQUAE Reviewed; 425 AA.
AC O66647;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
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}; OrderedLocusNames=aq_298;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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}.
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DR EMBL; AE000657; AAC06595.1; -; Genomic_DNA.
DR PIR; C70327; C70327.
DR RefSeq; NP_213207.1; NC_000918.1.
DR RefSeq; WP_010880145.1; NC_000918.1.
DR PDB; 2DQ3; X-ray; 3.00 A; A/B=1-425.
DR PDBsum; 2DQ3; -.
DR AlphaFoldDB; O66647; -.
DR SMR; O66647; -.
DR STRING; 224324.aq_298; -.
DR EnsemblBacteria; AAC06595; AAC06595; aq_298.
DR KEGG; aae:aq_298; -.
DR PATRIC; fig|224324.8.peg.245; -.
DR eggNOG; COG0172; Bacteria.
DR HOGENOM; CLU_023797_1_1_0; -.
DR InParanoid; O66647; -.
DR OMA; SPCFRRE; -.
DR OrthoDB; 353391at2; -.
DR UniPathway; UPA00906; UER00895.
DR EvolutionaryTrace; O66647; -.
DR Proteomes; UP000000798; 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 Gene3D; 3.30.930.10; -; 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 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 SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00414; serS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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_0000121995"
FT BINDING 231..233
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 262..264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 285
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 349..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 385
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 11..18
FT /evidence="ECO:0007829|PDB:2DQ3"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 26..59
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:2DQ3"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 76..103
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:2DQ3"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:2DQ3"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 170..188
FT /evidence="ECO:0007829|PDB:2DQ3"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:2DQ3"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 202..208
FT /evidence="ECO:0007829|PDB:2DQ3"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:2DQ3"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2DQ3"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:2DQ3"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:2DQ3"
FT STRAND 252..261
FT /evidence="ECO:0007829|PDB:2DQ3"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:2DQ3"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:2DQ3"
FT STRAND 279..290
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 295..313
FT /evidence="ECO:0007829|PDB:2DQ3"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:2DQ3"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:2DQ3"
FT STRAND 332..341
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:2DQ3"
FT STRAND 346..355
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 359..364
FT /evidence="ECO:0007829|PDB:2DQ3"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:2DQ3"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:2DQ3"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:2DQ3"
FT STRAND 380..388
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 389..399
FT /evidence="ECO:0007829|PDB:2DQ3"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:2DQ3"
FT HELIX 414..417
FT /evidence="ECO:0007829|PDB:2DQ3"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:2DQ3"
SQ SEQUENCE 425 AA; 49433 MW; 30173C92567DC784 CRC64;
MIDINLIREK PDYVKERLAT RDKELVSLVD KVLELDKRRR EIIKRLEALR SERNKLSKEI
GKLKREGKDT TEIQNRVKEL KEEIDRLEEE LRKVEEELKN TLLWIPNLPH PSVPVGEDEK
DNVEVRRWGE PRKFDFEPKP HWEIGERLGI LDFKRGAKLS GSRFTVIAGW GARLERALIN
FMLDLHTKKG YKEICPPHLV KPEILIGTGQ LPKFEEDLYK CERDNLYLIP TAEVPLTNLY
REEILKEENL PIYLTAYTPC YRREAGAYGK DIRGIIRQHQ FDKVELVKIV HPDTSYDELE
KLVKDAEEVL QLLGLPYRVV ELCTGDLGFS AAKTYDIEVW FPSQNKYREI SSCSNCEDFQ
ARRMNTRFKD SKTGKNRFVH TLNGSGLAVG RTLAAILENY QQEDGSVVVP EVLRDYVGTD
VIRPE
