ID D9PTZ8_METTM Unreviewed; 531 AA.
AC D9PTZ8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=O-phosphoserine--tRNA(Cys) ligase {ECO:0000256|HAMAP-Rule:MF_01674};
DE Short=O-phosphoserine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01674};
DE EC=6.1.1.27 {ECO:0000256|HAMAP-Rule:MF_01674};
DE AltName: Full=Non-canonical O-phosphoseryl-tRNA(Cys) synthetase {ECO:0000256|HAMAP-Rule:MF_01674};
DE AltName: Full=O-phosphoseryl-tRNA(Cys) synthetase {ECO:0000256|HAMAP-Rule:MF_01674};
DE Short=SepRS {ECO:0000256|HAMAP-Rule:MF_01674};
GN Name=sepS {ECO:0000256|HAMAP-Rule:MF_01674};
GN Synonyms=pheS1 {ECO:0000313|EMBL:ADL57696.1};
GN OrderedLocusNames=MTBMA_c00860 {ECO:0000313|EMBL:ADL57696.1};
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929 {ECO:0000313|EMBL:ADL57696.1, ECO:0000313|Proteomes:UP000000345};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Marburg;
RA Kaster A., Seedorf H., Goenrich M., Wiezer A., Liesegang H., Thauer R.,
RA Gottschalk G.;
RT "The genome sequence of Methanothermobacter marburgensis.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADL57696.1, ECO:0000313|Proteomes:UP000000345}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg {ECO:0000313|Proteomes:UP000000345};
RX PubMed=20802048; DOI=10.1128/JB.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
CC -!- FUNCTION: Catalyzes the attachment of O-phosphoserine (Sep) to
CC tRNA(Cys). {ECO:0000256|HAMAP-Rule:MF_01674}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + O-phospho-L-serine + tRNA(Cys) = AMP + diphosphate + O-
CC phospho-L-seryl-tRNA(Cys); Xref=Rhea:RHEA:25678, Rhea:RHEA-COMP:9661,
CC Rhea:RHEA-COMP:9719, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57524, ChEBI:CHEBI:78442, ChEBI:CHEBI:78551,
CC ChEBI:CHEBI:456215; EC=6.1.1.27; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01674};
CC -!- SUBUNIT: Homotetramer. Interacts with SepCysS. {ECO:0000256|HAMAP-
CC Rule:MF_01674}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC O-phosphoseryl-tRNA(Cys) synthetase subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01674}.
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DR EMBL; CP001710; ADL57696.1; -; Genomic_DNA.
DR RefSeq; WP_013294925.1; NC_014408.1.
DR AlphaFoldDB; D9PTZ8; -.
DR STRING; 79929.MTBMA_c00860; -.
DR PaxDb; 79929-MTBMA_c00860; -.
DR GeneID; 9703791; -.
DR KEGG; mmg:MTBMA_c00860; -.
DR PATRIC; fig|79929.8.peg.85; -.
DR HOGENOM; CLU_506822_0_0_2; -.
DR OrthoDB; 145125at2157; -.
DR Proteomes; UP000000345; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043816; F:phosphoserine-tRNA(Cys) ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR GO; GO:0043039; P:tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01674; Sep_tRNA_synth; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005246; O-Pseryl-tRNA(Cys)_ligase.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR InterPro; IPR041590; SepRS_C.
DR NCBIfam; TIGR00470; sepS; 1.
DR PANTHER; PTHR11538:SF38; O-PHOSPHOSERINE--TRNA(CYS) LIGASE; 1.
DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF18006; SepRS_C; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01674,
KW ECO:0000313|EMBL:ADL57696.1};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01674};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01674, ECO:0000313|EMBL:ADL57696.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01674};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_01674}.
FT DOMAIN 204..341
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 186..188
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01674"
FT BINDING 231..233
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01674"
FT BINDING 273..274
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01674"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01674"
SQ SEQUENCE 531 AA; 60669 MW; 7A10F4B8CDF9FAF3 CRC64;
MKKKDIVKLS RRDFERAWLE SGKLLKKPHH DLQYPRLRFG VGKSHVLYDT IWMIREAYLR
LGFSEMVNPV FIDEEHIYRQ FGPEAPAVLD RCFYLGGLPR PDIGLGLDKI RMIEEMGVEV
TEDRIQGLKE VFRSYKKGDI SGDDLVLEVS GALEVESHDA LRIIERVFPE IRDLKPVAGR
TTLRSHMTSG WFISLQNIHD RYPLPLKLFS IDRCFRREQR EDSSHLMTYH SASCVVVDDE
VPLDVGKAVA EGLLEHFGFS RFKFLPDEKK SKYYIPGTQT EVYAYHPGLR DWVEIATFGL
YSPIALSMYG IDEEVMNLGV GVERVAMILN QVDDVREMVY PQIHGPWRLT DRDIAGMLRI
NLHPVTSDGR MLMERIIETW RAHADAESPC SFEVYSGEFL GRRIRVEAVE DEENTRLLGP
AVWNTIYIHD GNILGVPPGT ELDNELIASA RRDGLNTGIT YMDALAAEAA YRVEEMAVSG
ADEVEVRSTI ARSLSDLNLI LDDVAMRYIT SRNREIDLRG PLFSTVRGML E
//
