GenomeNet

Database: UniProt
Entry: SEPS_METMA
LinkDB: SEPS_METMA
Original site: SEPS_METMA 
ID   SEPS_METMA              Reviewed;         539 AA.
AC   Q8PX39;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   05-JUN-2019, entry version 109.
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};
GN   OrderedLocusNames=MM_1383;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 /
OS   JCM 11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene
RT   transfer between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(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
CC         + O-phospho-L-seryl-tRNA(Cys); Xref=Rhea:RHEA:25678, Rhea:RHEA-
CC         COMP:9661, Rhea:RHEA-COMP:9719, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57524, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78551, ChEBI:CHEBI:456215; EC=6.1.1.27;
CC         Evidence={ECO:0000255|HAMAP-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
CC       family. O-phosphoseryl-tRNA(Cys) synthetase subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01674}.
DR   EMBL; AE008384; AAM31079.1; -; Genomic_DNA.
DR   RefSeq; WP_011033329.1; NC_003901.1.
DR   SMR; Q8PX39; -.
DR   STRING; 192952.MM_1383; -.
DR   EnsemblBacteria; AAM31079; AAM31079; MM_1383.
DR   GeneID; 1479725; -.
DR   KEGG; mma:MM_1383; -.
DR   PATRIC; fig|192952.21.peg.1601; -.
DR   eggNOG; arCOG00411; Archaea.
DR   eggNOG; COG2024; LUCA.
DR   HOGENOM; HOG000015472; -.
DR   KO; K07587; -.
DR   OMA; RSHMTSG; -.
DR   BioCyc; MMAZ192952:G1FZI-1441-MONOMER; -.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 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   TIGRFAMs; TIGR00470; sepS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    539       O-phosphoserine--tRNA(Cys) ligase.
FT                                /FTId=PRO_0000363762.
FT   REGION      188    190       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01674}.
FT   REGION      233    235       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01674}.
FT   REGION      275    276       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01674}.
FT   BINDING     327    327       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01674}.
SQ   SEQUENCE   539 AA;  60905 MW;  36F9E0984AB9499C CRC64;
     MKFDPEKIKK DAKENFDHAW NEGKKMVKTP TLNERYPRTT LRYGKAHPVY DTIQKLREAY
     MRMGFEEMMN PLIVDEKEVH KQFGSEALAV LDRCFYLAGL PRPNVGISDE RIAQITEILG
     DIGEEGIDKI RKELHAYKKG KIEGDDLVPE ISAALEVSDA LVADMIDRVF PEFKELIPQA
     STKTLRSHMT SGWFISLGAL LEREEPPFQF FSIDRCFRRE QQEDASRLMT YYSASCVIMD
     EDVTVDHGKA VSEGLLSQFG FEKFLFRPDE KRSKYYVPDT QTEVFAFHPK LVGSNSKYSD
     GWIEVATFGI YSPTALAEYD IPYPVMNLGL GVERLAMILH DAPDVRSLTY PQIPQYSEWE
     MSDSGLAKQV FVDRMPETPE GQEIASAVVA QCELHGEEPS PCEFPAWEGE VCGRKVKVSV
     IEPEENTKLC GPAAFNEVVA YQGDILGIPN NKKWQKAFEN HSARAGIRFI EAFAAQAARE
     IEEAAMSGAD EHIVRIRIVK VPSEVNLKIG ATAQRYITGK NKKIDIRGPV FTSVKAEFE
//
DBGET integrated database retrieval system