ID SYS2_METKA Reviewed; 527 AA. AC Q8TVD2; DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 112. DE RecName: Full=Type-2 serine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01278}; DE EC=6.1.1.11 {ECO:0000255|HAMAP-Rule:MF_01278}; DE AltName: Full=Seryl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01278}; DE Short=SerRS {ECO:0000255|HAMAP-Rule:MF_01278}; DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000255|HAMAP-Rule:MF_01278}; GN Name=serS {ECO:0000255|HAMAP-Rule:MF_01278}; OrderedLocusNames=MK1460; OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938). OC Archaea; Euryarchaeota; Methanomada group; Methanopyri; Methanopyrales; OC Methanopyraceae; Methanopyrus. OX NCBI_TaxID=190192; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938; RX PubMed=11930014; DOI=10.1073/pnas.032671499; RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., RA Koonin E.V., Kozyavkin S.A.; RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and RT monophyly of archaeal methanogens."; RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(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_01278}. 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_01278}; 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_01278}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01278}; CC Note=Binds 1 Zn(2+) ion per subunit. This ion is coordinated with 2 CC cysteines, 1 glutamate and a water molecule that dissociates from the CC zinc ion to allow the coordination of the amino group of the serine CC substrate, which is essential for catalysis. {ECO:0000255|HAMAP- CC Rule:MF_01278}; 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_01278}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01278}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01278}. CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N- CC terminal extension that is presumably involved in tRNA binding. CC {ECO:0000255|HAMAP-Rule:MF_01278}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC Type-2 seryl-tRNA synthetase subfamily. {ECO:0000255|HAMAP- CC Rule:MF_01278}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE009439; AAM02673.1; -; Genomic_DNA. DR PDB; 3W3S; X-ray; 3.10 A; A=1-527. DR PDBsum; 3W3S; -. DR AlphaFoldDB; Q8TVD2; -. DR SMR; Q8TVD2; -. DR STRING; 190192.MK1460; -. DR PaxDb; 190192-MK1460; -. DR EnsemblBacteria; AAM02673; AAM02673; MK1460. DR KEGG; mka:MK1460; -. DR PATRIC; fig|190192.8.peg.1616; -. DR HOGENOM; CLU_542524_0_0_2; -. DR InParanoid; Q8TVD2; -. DR OrthoDB; 115981at2157; -. DR BRENDA; 6.1.1.11; 3274. DR UniPathway; UPA00906; UER00895. DR Proteomes; UP000001826; 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:0008270; F:zinc ion binding; 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; cd00670; Gly_His_Pro_Ser_Thr_tRS_core; 1. DR Gene3D; 3.30.70.1920; -; 1. DR HAMAP; MF_01278; Ser_tRNA_synth_type2; 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; IPR004503; Ser-tRNA-ligase_2_arc. DR InterPro; IPR041293; SerS_tRNA-bd. DR NCBIfam; TIGR00415; serS_MJ; 1. DR PANTHER; PTHR43697:SF1; SERINE--TRNA LIGASE; 1. DR PANTHER; PTHR43697; SERYL-TRNA SYNTHETASE; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR Pfam; PF18490; tRNA_bind_4; 1. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 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 Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1..527 FT /note="Type-2 serine--tRNA ligase" FT /id="PRO_0000286169" FT BINDING 317 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278" FT BINDING 319 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278" FT BINDING 349..351 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278" FT BINDING 349 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278" FT BINDING 360..361 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278" FT BINDING 366..368 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278" FT BINDING 368 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278" FT BINDING 478 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278" FT BINDING 485 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278" FT STRAND 2..15 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 19..35 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 50..56 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 58..71 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 73..92 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 96..109 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 116..119 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 126..130 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 132..141 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 144..148 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 151..163 FT /evidence="ECO:0007829|PDB:3W3S" FT TURN 164..167 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 169..171 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 181..184 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 196..202 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 205..208 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 215..217 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 219..235 FT /evidence="ECO:0007829|PDB:3W3S" FT TURN 236..241 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 249..252 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 253..258 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 261..264 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 266..268 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 279..292 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 297..305 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 312..314 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 321..326 FT /evidence="ECO:0007829|PDB:3W3S" FT TURN 333..335 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 338..342 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 345..348 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 358..360 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 362..373 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 375..395 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 400..404 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 412..414 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 415..418 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 428..434 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 436..438 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 444..446 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 447..457 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 459..463 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 467..470 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 475..482 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 483..494 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 498..500 FT /evidence="ECO:0007829|PDB:3W3S" FT HELIX 503..513 FT /evidence="ECO:0007829|PDB:3W3S" FT STRAND 523..525 FT /evidence="ECO:0007829|PDB:3W3S" SQ SEQUENCE 527 AA; 61368 MW; 7526147D81EFC5CD CRC64; MELKFSAEVE LTLSREVDPA EIEPTVEEFV KEANEDLLQR GVPTGKEGAK IESYRVLEDT IEMEITGTRY LRPHEAAMRV RKRLAERLGR KHRVGVRDLK IPRYEVVLRF DREVTRDDVG YVPVADDVVV EDGTVRLTFQ DVDEEMLRRH VIDRVIRLVA WAVEERSELV ERVTKVEPGT VVDESGPREI RFDGDVTEEA RRRGWVKEFP GRGQWIYTPP MAALFEVLRD FLLERVTRKL GFEPALFPKL IPLETMFRMR YLHGLPDGMY YVCPPKRDPE LFDDFKRELY VWGELNERTL GSLKEKLRDP GYVLAPAQCE PFYELLRDEV VDPERLPIKL YDCSGWTYRW EGGAAKGLER VNEFQRIEHV WIAEPEEAER IREELLEATK RVAEELELEW KVVVSDDPFY LEGRLLEDRD IELPDVPSYE FEVYLPFKGE RSSEEAWISV GSFNVHGEHF VDGFNVKEKS GRTLFTGCAG LGVTRWVVGL LAQHGFEPEE WPEPILERID EKFGGLPEVP KTLTWPE //