ID SYS_METMA Reviewed; 422 AA.
AC Q8PYJ6;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 129.
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=MM_0865;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM30561.1; -; Genomic_DNA.
DR RefSeq; WP_011032815.1; NC_003901.1.
DR PDB; 6X94; X-ray; 1.45 A; A=1-420.
DR PDBsum; 6X94; -.
DR AlphaFoldDB; Q8PYJ6; -.
DR SMR; Q8PYJ6; -.
DR GeneID; 82159889; -.
DR KEGG; mma:MM_0865; -.
DR PATRIC; fig|192952.21.peg.1024; -.
DR eggNOG; arCOG00403; Archaea.
DR HOGENOM; CLU_023797_1_1_2; -.
DR UniPathway; UPA00906; UER00895.
DR Proteomes; UP000000595; 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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..422
FT /note="Serine--tRNA ligase"
FT /id="PRO_0000122175"
FT BINDING 229..231
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 258..260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 281
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 379
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:6X94"
FT HELIX 11..20
FT /evidence="ECO:0007829|PDB:6X94"
FT HELIX 26..64
FT /evidence="ECO:0007829|PDB:6X94"
FT HELIX 70..101
FT /evidence="ECO:0007829|PDB:6X94"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6X94"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:6X94"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:6X94"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:6X94"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:6X94"
FT HELIX 169..187
FT /evidence="ECO:0007829|PDB:6X94"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:6X94"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:6X94"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:6X94"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:6X94"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:6X94"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:6X94"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:6X94"
FT STRAND 245..257
FT /evidence="ECO:0007829|PDB:6X94"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:6X94"
FT STRAND 275..286
FT /evidence="ECO:0007829|PDB:6X94"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:6X94"
FT HELIX 291..309
FT /evidence="ECO:0007829|PDB:6X94"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:6X94"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:6X94"
FT STRAND 328..336
FT /evidence="ECO:0007829|PDB:6X94"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:6X94"
FT STRAND 341..351
FT /evidence="ECO:0007829|PDB:6X94"
FT HELIX 355..360
FT /evidence="ECO:0007829|PDB:6X94"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:6X94"
FT STRAND 374..382
FT /evidence="ECO:0007829|PDB:6X94"
FT HELIX 383..393
FT /evidence="ECO:0007829|PDB:6X94"
FT HELIX 405..411
FT /evidence="ECO:0007829|PDB:6X94"
SQ SEQUENCE 422 AA; 48072 MW; 00EA5469C25A6D98 CRC64;
MLELKFVRNN PDIVGRALIS RNMGTELIDS LLEYDAAWRE CLIEGDDLKH KRNVVTREIA
QLKKENKDAA SRINEMQGIN SRIKELDDKI RDYKSKINEI MLSIPNIPSE TTPVGKDEND
NPVVRVVGEP REFTFTPKPH WEIGESLDIL DFERAAKISG QGFAVYKGMG AKLERALINF
MLDVHTRQGY LEVFPPVLIN EKAMTGTGQL PKFKDDMYGC TDGFYLAPTA EVPVTNLFMD
EYMENLPVFL TAYTACFRRE AGKHGQDTRG IIRNHQFNKV ELVKFVMPET SYEELEKLTL
DAEEILKLLK LPYRVVSLCT GDLGFSAAKT YDLEVWVPTQ EKYREISSCS NFDNFQARRA
NIRYRTPEGP QFVHTLNGSG LAVGRTVVAI LENYQREDGS VEIPEVLRPY MGGAEEIRKV
CH
//
