SYS2_METTP
ID SYS2_METTP Reviewed; 500 AA.
AC A0B5E9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Mthe_0123;
OS Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS PT) (Methanosaeta thermophila).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=349307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT "Complete sequence of Methanosaeta thermophila PT.";
RL Submitted (OCT-2006) 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_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;
CC Evidence={ECO:0000255|HAMAP-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}.
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DR EMBL; CP000477; ABK13923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0B5E9; -.
DR SMR; A0B5E9; -.
DR STRING; 349307.Mthe_0123; -.
DR PRIDE; A0B5E9; -.
DR EnsemblBacteria; ABK13923; ABK13923; Mthe_0123.
DR KEGG; mtp:Mthe_0123; -.
DR HOGENOM; CLU_542524_0_0_2; -.
DR OMA; YYVCPPK; -.
DR UniPathway; UPA00906; UER00895.
DR Proteomes; UP000000674; 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 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 Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF18490; tRNA_bind_4; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 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..500
FT /note="Type-2 serine--tRNA ligase"
FT /id="PRO_0000286170"
FT BINDING 305
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT BINDING 337..339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT BINDING 337
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT BINDING 348..349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT BINDING 354..356
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT BINDING 401
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT BINDING 430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT BINDING 433
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT BINDING 459
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT BINDING 466
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
SQ SEQUENCE 500 AA; 58083 MW; 2F27B81E766AFD4B CRC64;
MKFHLEVSLK LSGDAANAEG DLAEFFEKQA VDLLKKGAPE GMGAKVAGWR ITGDQLEIKI
ESDRYVRAHD ALLRLRKPLA NLLGRKHRLG IRGINVSRFE IQIESNRQIT HRIPYVRESR
YEDGLLTLIL GVEDPKRGWT WMLENRIPDR IVNLLEEKLQ SYGGKAEHWE LLWESPPREF
KFSGDPTQEM VKRGWIKHGS ARGQWIHGPQ STHLFRTFER IVLEEILVPL GYREMIFPKL
DTWDVWKRSG HAQGVYPEIY YVCPPKSRDP AFWEEVIDYY KVTHEIPLDL IKEKIDYPIG
GMCYAQCPTF WVFLQGATLP NDELPIKVFD RSGTSHRYES GGIHGIERVD EFHRIEIVWL
GTKQQVMEEA ERLKERYKHI FEEILELRWR MAWVTPWFMA QEGRTGLAEM EGAGTIDYEA
LLPYSGNWIE FQNLSVNGEK YPKGFSVKAQ SGESLWSGCS GVGLERWTSV FLGQKGLDPD
NWPDEFRKRF GEMPRGIRFL
