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SYS2_META3
ID   SYS2_META3              Reviewed;         522 AA.
AC   A6UX37;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Type-2 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=Maeo_1483;
OS   Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS   Nankai-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=419665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus aeolicus Nankai-3.";
RL   Submitted (JUN-2007) 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) (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
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:0000250};
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type-2 seryl-tRNA synthetase subfamily. {ECO:0000305}.
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DR   EMBL; CP000743; ABR57059.1; -; Genomic_DNA.
DR   RefSeq; WP_011974191.1; NC_009635.1.
DR   AlphaFoldDB; A6UX37; -.
DR   SMR; A6UX37; -.
DR   STRING; 419665.Maeo_1483; -.
DR   PRIDE; A6UX37; -.
DR   EnsemblBacteria; ABR57059; ABR57059; Maeo_1483.
DR   GeneID; 5326589; -.
DR   KEGG; mae:Maeo_1483; -.
DR   eggNOG; arCOG00403; Archaea.
DR   HOGENOM; CLU_542524_0_0_2; -.
DR   OMA; YYVCPPK; -.
DR   OrthoDB; 9543at2157; -.
DR   UniPathway; UPA00906; UER00895.
DR   Proteomes; UP000001106; 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:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.930.10; -; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004503; Ser-tRNA-ligase_2_arc.
DR   InterPro; IPR041293; SerS_tRNA-bd.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF18490; tRNA_bind_4; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00415; serS_MJ; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..522
FT                   /note="Type-2 serine--tRNA ligase"
FT                   /id="PRO_1000165220"
FT   BINDING         319
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000250"
FT   BINDING         321
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         350..352
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         350
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000250"
FT   BINDING         361..362
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         367..369
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000250"
FT   BINDING         369
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         476
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         483
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   522 AA;  60579 MW;  3F6E19B8AE30DA9D CRC64;
     MKFELNGKII FSKEITDDAK KDIIEVLNDR TILLKGVPTG KEEEASKIVN YEFKGNELIL
     NIISGTYARA HEAIIRLKKP IMEKVGKIHK MGIRDIKIDN YEITINAPHN IDALENLKVP
     ECETELNEEE NTIKIIFKNI GDSELKRNIV DRAIKFVKTE IDNIGDSGEE CDLTYEVCGI
     APNTIVSEYK AERTISYNKD PTEESEKLGW VKRFSGKGQW FYTPPMTKLL RAFEELLMEE
     CINKIGFDEC LFPKLIPLEV MYKMRYLEGL PEGMYYVSPP KRDPEMFKEF VNEMMIKNEI
     PIHKLKDLLR NPGYVLAPAQ CEPFYQFFDH ELVDIDNPVK FVDKSGWTYR WEGGGSKGLD
     RVHEFLRIET VQMGAPEFVN SVRDDTLKYA EKLAEKLDLE YWTEVGDDPF YLEGRKKEER
     NIEFPEVPKY EMRLWLPHVK DERKGVAVTS ANVHGTHFVE GFGVKDYKNR TVWTGCTGFG
     LSRWVIGFLA QYGFDYNDWP ELIKDKIGEM PNIPKVITWP KK
 
 
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