SEPS_METAC
ID SEPS_METAC Reviewed; 539 AA.
AC Q8TUH7;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=O-phosphoserine--tRNA(Cys) ligase {ECO:0000255|HAMAP-Rule:MF_01674};
DE Short=O-phosphoserine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01674};
DE EC=6.1.1.27 {ECO:0000255|HAMAP-Rule:MF_01674};
DE AltName: Full=Non-canonical O-phosphoseryl-tRNA(Cys) synthetase {ECO:0000255|HAMAP-Rule:MF_01674};
DE AltName: Full=O-phosphoseryl-tRNA(Cys) synthetase {ECO:0000255|HAMAP-Rule:MF_01674};
DE Short=SepRS {ECO:0000255|HAMAP-Rule:MF_01674};
GN Name=sepS {ECO:0000255|HAMAP-Rule:MF_01674}; Synonyms=pheRS;
GN OrderedLocusNames=MA_0090;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
CC -!- FUNCTION: Catalyzes the attachment of O-phosphoserine (Sep) to
CC tRNA(Cys). {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_01674};
CC -!- SUBUNIT: Homotetramer. Interacts with SepCysS. {ECO:0000255|HAMAP-
CC Rule:MF_01674}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC O-phosphoseryl-tRNA(Cys) synthetase subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01674}.
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DR EMBL; AE010299; AAM03544.1; -; Genomic_DNA.
DR RefSeq; WP_011020149.1; NC_003552.1.
DR AlphaFoldDB; Q8TUH7; -.
DR SMR; Q8TUH7; -.
DR STRING; 188937.MA_0090; -.
DR EnsemblBacteria; AAM03544; AAM03544; MA_0090.
DR GeneID; 1471982; -.
DR KEGG; mac:MA_0090; -.
DR HOGENOM; CLU_506822_0_0_2; -.
DR InParanoid; Q8TUH7; -.
DR OMA; RSHMTSG; -.
DR OrthoDB; 6499at2157; -.
DR PhylomeDB; Q8TUH7; -.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IBA:GO_Central.
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:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central.
DR Gene3D; 3.30.930.10; -; 1.
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 PANTHER; PTHR11538:SF38; PTHR11538:SF38; 1.
DR Pfam; PF18006; SepRS_C; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00470; sepS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..539
FT /note="O-phosphoserine--tRNA(Cys) ligase"
FT /id="PRO_0000363760"
FT BINDING 188..190
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01674"
FT BINDING 233..235
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01674"
FT BINDING 275..276
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01674"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01674"
SQ SEQUENCE 539 AA; 60781 MW; A72BBC58270C777B CRC64;
MRFDPEKIKK DAKENFDLTW NEGKKMVKTP TLNERYPRTT FRYGKAHPVY DTIQKLREAY
LRMGFEEMMN PLIVDEKEVH KQFGSEALAV LDRCFYLAGL PRPNVGISDE RIAQINGILG
DIGDEGIDKV RKVLHAYKKG KVEGDDLVPE ISAALEVSDA LVADMIEKVF PEFKELVAQA
STKTLRSHMT SGWFISLGAL LERKEPPFHF FSIDRCFRRE QQEDASRLMT YYSASCVIMD
ENVTVDHGKA VAEGLLSQFG FEKFLFRPDE KRSKYYVPDT QTEVFAFHPK LVGSNSKYSD
GWIEIATFGI YSPTALAEYD IPCPVMNLGL GVERLAMILH DAPDIRSLTY PQIPQYSEWE
MSDSELAKQV FVDKTPETPE GREIADAVVA QCELHGEEPS PCEFPAWEGE VCGRKVKVSV
IEPEENTKLC GPAAFNEVVT YQGDILGIPN TKKWQKAFEN HSAMAGIRFI EAFAAQAARE
IEEAAMSGAD EHIVRVRIVK VPSEVNIKIG ATAQRYITGK NKKIDMRGPI FTSAKAEFE
