SEPS_METJA
ID SEPS_METJA Reviewed; 539 AA.
AC Q59054;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=O-phosphoserine--tRNA(Cys) ligase;
DE Short=O-phosphoserine--tRNA ligase;
DE EC=6.1.1.27;
DE AltName: Full=Non-canonical O-phosphoseryl-tRNA(Cys) synthetase;
DE AltName: Full=O-phosphoseryl-tRNA(Cys) synthetase;
DE Short=SepRS;
GN Name=sepS; OrderedLocusNames=MJ1660;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION.
RX PubMed=15790858; DOI=10.1126/science.1108329;
RA Sauerwald A., Zhu W., Major T.A., Roy H., Palioura S., Jahn D.,
RA Whitman W.B., Yates J.R. III, Ibba M., Soell D.;
RT "RNA-dependent cysteine biosynthesis in archaea.";
RL Science 307:1969-1972(2005).
RN [3]
RP INTERACTION WITH SEPCYSS, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=18425141; DOI=10.1038/nsmb.1423;
RA Zhang C.-M., Liu C., Slater S., Hou Y.-M.;
RT "Aminoacylation of tRNA with phosphoserine for synthesis of cysteinyl-
RT tRNA(Cys).";
RL Nat. Struct. Mol. Biol. 15:507-514(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS), AND SUBUNIT.
RX PubMed=17351629; DOI=10.1038/nsmb1219;
RA Fukunaga R., Yokoyama S.;
RT "Structural insights into the first step of RNA-dependent cysteine
RT biosynthesis in archaea.";
RL Nat. Struct. Mol. Biol. 14:272-279(2007).
CC -!- FUNCTION: Catalyzes the attachment of O-phosphoserine (Sep) to
CC tRNA(Cys). {ECO:0000269|PubMed:15790858}.
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;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 uM for tRNA(Cys) (at 60 degrees Celsius and pH 6.0)
CC {ECO:0000269|PubMed:18425141};
CC -!- SUBUNIT: Homotetramer. Interacts with SepCysS.
CC {ECO:0000269|PubMed:17351629, ECO:0000269|PubMed:18425141}.
CC -!- INTERACTION:
CC Q59054; Q59072: pscS; NbExp=4; IntAct=EBI-15698391, EBI-15698426;
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC O-phosphoseryl-tRNA(Cys) synthetase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB99678.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L77117; AAB99678.1; ALT_INIT; Genomic_DNA.
DR PIR; B64507; B64507.
DR RefSeq; WP_064496988.1; NC_000909.1.
DR PDB; 2DU7; X-ray; 3.60 A; A/B/C/D=1-539.
DR PDB; 5X6C; X-ray; 3.10 A; A/B=1-539.
DR PDBsum; 2DU7; -.
DR PDBsum; 5X6C; -.
DR AlphaFoldDB; Q59054; -.
DR SMR; Q59054; -.
DR DIP; DIP-46382N; -.
DR IntAct; Q59054; 1.
DR STRING; 243232.MJ_1660; -.
DR PRIDE; Q59054; -.
DR EnsemblBacteria; AAB99678; AAB99678; MJ_1660.
DR GeneID; 1452569; -.
DR KEGG; mja:MJ_1660; -.
DR eggNOG; arCOG00411; Archaea.
DR HOGENOM; CLU_506822_0_0_2; -.
DR InParanoid; Q59054; -.
DR OMA; RSHMTSG; -.
DR OrthoDB; 6499at2157; -.
DR PhylomeDB; Q59054; -.
DR BioCyc; MetaCyc:MON-14996; -.
DR BRENDA; 6.1.1.27; 3260.
DR SABIO-RK; Q59054; -.
DR EvolutionaryTrace; Q59054; -.
DR Proteomes; UP000000805; 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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..539
FT /note="O-phosphoserine--tRNA(Cys) ligase"
FT /id="PRO_0000126829"
FT BINDING 188..190
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 233..235
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 275..276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:5X6C"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 48..61
FT /evidence="ECO:0007829|PDB:5X6C"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 124..138
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 208..217
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 229..239
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:5X6C"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:5X6C"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 293..303
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 305..310
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 324..332
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 337..341
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 352..356
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 368..383
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 388..401
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 404..414
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:5X6C"
FT TURN 424..427
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 429..433
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 451..461
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 462..468
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 469..486
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 491..499
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:5X6C"
FT HELIX 511..519
FT /evidence="ECO:0007829|PDB:5X6C"
FT STRAND 528..539
FT /evidence="ECO:0007829|PDB:5X6C"
SQ SEQUENCE 539 AA; 62153 MW; 301201548E9ADE40 CRC64;
MRFDIKKVLE LAEKDFETAW RETRALIKDK HIDNKYPRLK PVYGKPHPVM ETIERLRQAY
LRMGFEEMIN PVIVDEMEIY KQFGPEAMAV LDRCFYLAGL PRPDVGLGNE KVEIIKNLGI
DIDEEKKERL REVLHLYKKG AIDGDDLVFE IAKALNVSNE MGLKVLETAF PEFKDLKPES
TTLTLRSHMT SGWFITLSSL IKKRKLPLKL FSIDRCFRRE QREDRSHLMS YHSASCVVVG
EDVSVDDGKV VAEGLLAQFG FTKFKFKPDE KKSKYYTPET QTEVYAYHPK LGEWIEVATF
GVYSPIALAK YNIDVPVMNL GLGVERLAMI IYGYEDVRAM VYPQFYEYRL SDRDIAGMIR
VDKVPILDEF YNFANELIDI CIANKDKESP CSVEVKREFN FNGERRVIKV EIFENEPNKK
LLGPSVLNEV YVYDGNIYGI PPTFEGVKEQ YIPILKKAKE EGVSTNIRYI DGIIYKLVAK
IEEALVSNVD EFKFRVPIVR SLSDINLKID ELALKQIMGE NKVIDVRGPV FLNAKVEIK
