SYS_THET8
ID SYS_THET8 Reviewed; 421 AA.
AC Q5SJX7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=TTHA0875;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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}.
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DR EMBL; AP008226; BAD70698.1; -; Genomic_DNA.
DR RefSeq; WP_011228260.1; NC_006461.1.
DR RefSeq; YP_144141.1; NC_006461.1.
DR PDB; 3ERR; X-ray; 2.27 A; A/B=1-34, A/B=63-126, A/B=254-419.
DR PDBsum; 3ERR; -.
DR AlphaFoldDB; Q5SJX7; -.
DR SMR; Q5SJX7; -.
DR STRING; 300852.55772257; -.
DR EnsemblBacteria; BAD70698; BAD70698; BAD70698.
DR GeneID; 3168248; -.
DR KEGG; ttj:TTHA0875; -.
DR PATRIC; fig|300852.9.peg.868; -.
DR eggNOG; COG0172; Bacteria.
DR HOGENOM; CLU_023797_0_1_0; -.
DR OMA; SPCFRRE; -.
DR PhylomeDB; Q5SJX7; -.
DR UniPathway; UPA00906; UER00895.
DR Proteomes; UP000000532; 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; -; 2.
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..421
FT /note="Serine--tRNA ligase"
FT /id="PRO_0000122146"
FT BINDING 225..227
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 256..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 279
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 345..348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 380
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3ERR"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 163..182
FT /evidence="ECO:0007829|PDB:3ERR"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:3ERR"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:3ERR"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:3ERR"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:3ERR"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:3ERR"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:3ERR"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:3ERR"
FT STRAND 245..255
FT /evidence="ECO:0007829|PDB:3ERR"
FT STRAND 273..284
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 288..308
FT /evidence="ECO:0007829|PDB:3ERR"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:3ERR"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:3ERR"
FT STRAND 328..337
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:3ERR"
FT STRAND 342..353
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 355..360
FT /evidence="ECO:0007829|PDB:3ERR"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:3ERR"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:3ERR"
FT STRAND 375..384
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 386..395
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 409..412
FT /evidence="ECO:0007829|PDB:3ERR"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:3ERR"
SQ SEQUENCE 421 AA; 47787 MW; 6CE0A2EF086B31F0 CRC64;
MVDLKRLRQE PEVFHRAIRE KGVALDLEAL LALDQEVQEL KKRLQEVQTE RNQVAKRVPK
APPEEKEALI ARGRALGEEA KRLEEALREK EAQLEALLLQ VPLPPWPGAP VGGEEANREI
KRVGSPPEFS FPPLDHVALM EKNGWWEPRI SQVSGSRSYA LKGDLALYEL ALLRFAMDFM
ARRGFLPMTL PSYAREKAFL GTGHFPAYRD QVWAIAETDL YLTGTAEVVL NALHSGEILP
YEALPLRYAG YAPAFRSEAG SFGKDVRGLM RVHQFHKVEQ YVLTEASLEA SDRAFQELLE
NAEEILRLLE LPYRLVEVAT GDMGPGKWRQ VDVEVYLPSE GRYRETHSCS ALLDWQARRA
NLRYRDPEGR VRYAYTLNNT ALATPRILAM LLENHQLQDG RVRVPKALVP YMGKEVLEPC
G
