ID SYS_THET2 Reviewed; 421 AA.
AC P34945;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 27-MAR-2024, entry version 162.
DE RecName: Full=Serine--tRNA ligase;
DE EC=6.1.1.11;
DE AltName: Full=Seryl-tRNA synthetase;
DE Short=SerRS;
DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase;
GN Name=serS; OrderedLocusNames=TT_C0520;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SUBUNIT.
RX PubMed=8230201; DOI=10.1006/jmbi.1993.1576;
RA Fujinaga M., Berthet-Colominas C., Yaremchuk A.D., Tukalo M.A., Cusack S.;
RT "Refined crystal structure of the seryl-tRNA synthetase from Thermus
RT thermophilus at 2.5-A resolution.";
RL J. Mol. Biol. 234:222-233(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS.
RX PubMed=8128224; DOI=10.1126/science.8128224;
RA Belrhali H., Yaremchuk A.D., Tukalo M.A., Larsen K., Berthet-Colominas C.,
RA Leberman R., Beijer B., Sproat B., Als-Nielsen J., Gruebel G.,
RA Legrand J.-F., Lehmann M., Cusack S.;
RT "Crystal structures at 2.5 angstrom resolution of seryl-tRNA synthetase
RT complexed with two analogs of seryl adenylate.";
RL Science 263:1432-1436(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH TRNA(SER), AND
RP SUBUNIT.
RX PubMed=8128220; DOI=10.1126/science.8128220;
RA Biou V., Yaremchuk A.D., Tukalo M.A., Cusack S.;
RT "The 2.9 A crystal structure of T. thermophilus seryl-tRNA synthetase
RT complexed with tRNA(Ser).";
RL Science 263:1404-1410(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH TRNA(SER) AND
RP SUBSTRATE ANALOG, AND SUBUNIT.
RX PubMed=8654381; DOI=10.1002/j.1460-2075.1996.tb00644.x;
RA Cusack S., Yaremchuk A.D., Tukalo M.A.;
RT "The crystal structure of the ternary complex of T.thermophilus seryl-tRNA
RT synthetase with tRNA(Ser) and a seryl-adenylate analogue reveals a
RT conformational switch in the active site.";
RL EMBO J. 15:2834-2842(1996).
CC -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also
CC probably able to aminoacylate tRNA(Sec) with serine, to form the
CC misacylated tRNA L-seryl-tRNA(Sec), which will be further converted
CC into selenocysteinyl-tRNA(Sec).
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 -!- 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 -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
CC -!- SUBUNIT: Homodimer. A single tRNA molecule binds across the dimer.
CC {ECO:0000269|PubMed:8128220, ECO:0000269|PubMed:8230201,
CC ECO:0000269|PubMed:8654381}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N-
CC terminal extension that is involved in tRNA binding.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type-1 seryl-tRNA synthetase subfamily. {ECO:0000305}.
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DR EMBL; AE017221; AAS80868.1; -; Genomic_DNA.
DR RefSeq; WP_011172965.1; NZ_CP133179.1.
DR PDB; 1SER; X-ray; 2.90 A; A/B=1-421.
DR PDB; 1SES; X-ray; 2.50 A; A/B=1-421.
DR PDB; 1SET; X-ray; 2.55 A; A/B=1-421.
DR PDB; 1SRY; X-ray; 2.50 A; A/B=1-421.
DR PDB; 3ERR; X-ray; 2.27 A; A/B=94-419.
DR PDB; 5EIU; X-ray; 1.91 A; A/D=49-78.
DR PDB; 5F7T; X-ray; 2.29 A; E/F/H/L=49-78.
DR PDB; 5IEA; X-ray; 3.26 A; A/B/C/D/F/K=49-78.
DR PDB; 5VA4; X-ray; 2.31 A; A=49-78.
DR PDBsum; 1SER; -.
DR PDBsum; 1SES; -.
DR PDBsum; 1SET; -.
DR PDBsum; 1SRY; -.
DR PDBsum; 3ERR; -.
DR PDBsum; 5EIU; -.
DR PDBsum; 5F7T; -.
DR PDBsum; 5IEA; -.
DR PDBsum; 5VA4; -.
DR AlphaFoldDB; P34945; -.
DR SMR; P34945; -.
DR KEGG; tth:TT_C0520; -.
DR eggNOG; COG0172; Bacteria.
DR HOGENOM; CLU_023797_0_1_0; -.
DR OrthoDB; 9804647at2; -.
DR BRENDA; 6.1.1.11; 2305.
DR UniPathway; UPA00906; UER00895.
DR EvolutionaryTrace; P34945; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IMP:CAFA.
DR GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0070905; F:serine binding; IDA:CAFA.
DR GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IDA:CAFA.
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; 2.
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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..421
FT /note="Serine--tRNA ligase"
FT /id="PRO_0000122145"
FT BINDING 225..227
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT BINDING 256..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 279
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT BINDING 345..348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 380
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:1SES"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:1SES"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:1SER"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:5EIU"
FT HELIX 63..78
FT /evidence="ECO:0007829|PDB:5EIU"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:1SER"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1SES"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1SES"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:1SES"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:1SES"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:1SES"
FT HELIX 164..182
FT /evidence="ECO:0007829|PDB:1SES"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:1SES"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:1SES"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:1SES"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:1SES"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1SES"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:1SES"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:1SES"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:1SES"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:1SES"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:1SES"
FT STRAND 245..255
FT /evidence="ECO:0007829|PDB:1SES"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:1SRY"
FT STRAND 273..284
FT /evidence="ECO:0007829|PDB:1SES"
FT HELIX 288..308
FT /evidence="ECO:0007829|PDB:1SES"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:1SES"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:1SES"
FT STRAND 328..336
FT /evidence="ECO:0007829|PDB:1SES"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:1SES"
FT STRAND 341..353
FT /evidence="ECO:0007829|PDB:1SES"
FT HELIX 355..360
FT /evidence="ECO:0007829|PDB:1SES"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:1SES"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:1SES"
FT STRAND 375..384
FT /evidence="ECO:0007829|PDB:1SES"
FT HELIX 386..395
FT /evidence="ECO:0007829|PDB:1SES"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:1SES"
FT HELIX 409..412
FT /evidence="ECO:0007829|PDB:1SES"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:1SES"
SQ SEQUENCE 421 AA; 47813 MW; 5E89B0D131EFC209 CRC64;
MVDLKRLRQE PEVFHRAIRE KGVALDLEAL LALDREVQEL KKRLQEVQTE RNQVAKRVPK
APPEEKEALI ARGKALGEEA KRLEEALREK EARLEALLLQ VPLPPWPGAP VGGEEANREI
KRVGGPPEFS FPPLDHVALM EKNGWWEPRI SQVSGSRSYA LKGDLALYEL ALLRFAMDFM
ARRGFLPMTL PSYAREKAFL GTGHFPAYRD QVWAIAETDL YLTGTAEVVL NALHSGEILP
YEALPLRYAG YAPAFRSEAG SFGKDVRGLM RVHQFHKVEQ YVLTEASLEA SDRAFQELLE
NAEEILRLLE LPYRLVEVAT GDMGPGKWRQ VDIEVYLPSE GRYRETHSCS ALLDWQARRA
NLRYRDPEGR VRYAYTLNNT ALATPRILAM LLENHQLQDG RVRVPQALIP YMGKEVLEPC
G
//
