SPSS_METJA
ID SPSS_METJA Reviewed; 377 AA.
AC Q59072;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=O-phospho-L-seryl-tRNA:Cys-tRNA synthase;
DE EC=2.5.1.73;
DE AltName: Full=Sep-tRNA:Cys-tRNA synthase;
DE Short=SepCysS;
GN Name=pscS {ECO:0000303|PubMed:15790858}; OrderedLocusNames=MJ1678;
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, AND CATALYTIC ACTIVITY.
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 SEPRS, 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).
CC -!- FUNCTION: Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L-
CC cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)). {ECO:0000269|PubMed:15790858}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hydrogen sulfide + O-phospho-L-seryl-tRNA(Cys) = L-
CC cysteinyl-tRNA(Cys) + phosphate; Xref=Rhea:RHEA:25686, Rhea:RHEA-
CC COMP:9679, Rhea:RHEA-COMP:9719, ChEBI:CHEBI:15378, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:78517, ChEBI:CHEBI:78551; EC=2.5.1.73;
CC Evidence={ECO:0000269|PubMed:15790858};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25687;
CC Evidence={ECO:0000305|PubMed:15790858};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000305};
CC -!- SUBUNIT: Homodimer. Interacts with SepRS.
CC {ECO:0000269|PubMed:18425141}.
CC -!- INTERACTION:
CC Q59072; Q59054: sepS; NbExp=4; IntAct=EBI-15698426, EBI-15698391;
CC -!- SIMILARITY: Belongs to the SepCysS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB99700.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L77117; AAB99700.1; ALT_INIT; Genomic_DNA.
DR PIR; D64509; D64509.
DR PDB; 3WKR; X-ray; 2.80 A; A/B/E/F=2-377.
DR PDB; 3WKS; X-ray; 3.03 A; A/B=2-377.
DR PDB; 5X6B; X-ray; 2.60 A; I/J=1-377.
DR PDBsum; 3WKR; -.
DR PDBsum; 3WKS; -.
DR PDBsum; 5X6B; -.
DR AlphaFoldDB; Q59072; -.
DR SMR; Q59072; -.
DR DIP; DIP-46383N; -.
DR IntAct; Q59072; 1.
DR STRING; 243232.MJ_1678; -.
DR PRIDE; Q59072; -.
DR EnsemblBacteria; AAB99700; AAB99700; MJ_1678.
DR KEGG; mja:MJ_1678; -.
DR eggNOG; arCOG00091; Archaea.
DR HOGENOM; CLU_060476_0_0_2; -.
DR InParanoid; Q59072; -.
DR OMA; HKSMAAS; -.
DR PhylomeDB; Q59072; -.
DR BioCyc; MetaCyc:MON-14997; -.
DR BRENDA; 2.5.1.73; 3260.
DR SABIO-RK; Q59072; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0043766; F:Sep-tRNA:Cys-tRNA synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01675; Sep_Cys_tRNA_synth; 1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR013375; Sep_Cys-tRNA_synth_arc.
DR InterPro; IPR008829; SepSecS/SepCysS.
DR PANTHER; PTHR43586:SF3; PTHR43586:SF3; 1.
DR Pfam; PF05889; SepSecS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR02539; SepCysS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Protein biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..377
FT /note="O-phospho-L-seryl-tRNA:Cys-tRNA synthase"
FT /id="PRO_0000107475"
FT BINDING 82..83
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT BINDING 189
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT BINDING 212..214
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT MOD_RES 215
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT HELIX 1..4
FT /evidence="ECO:0007829|PDB:5X6B"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:3WKS"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:5X6B"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:5X6B"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:5X6B"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:5X6B"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:5X6B"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:5X6B"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:5X6B"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:5X6B"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:5X6B"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:5X6B"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:5X6B"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:5X6B"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:5X6B"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:5X6B"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:5X6B"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:5X6B"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:5X6B"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:5X6B"
FT TURN 201..205
FT /evidence="ECO:0007829|PDB:5X6B"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:5X6B"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:5X6B"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:5X6B"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:5X6B"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:3WKR"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:5X6B"
FT HELIX 258..273
FT /evidence="ECO:0007829|PDB:5X6B"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:5X6B"
FT HELIX 277..292
FT /evidence="ECO:0007829|PDB:5X6B"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:5X6B"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:5X6B"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:5X6B"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:5X6B"
FT HELIX 314..320
FT /evidence="ECO:0007829|PDB:5X6B"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:5X6B"
FT HELIX 329..336
FT /evidence="ECO:0007829|PDB:5X6B"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:5X6B"
FT HELIX 359..375
FT /evidence="ECO:0007829|PDB:5X6B"
SQ SEQUENCE 377 AA; 42764 MW; 791842FF733C72BA CRC64;
MDKYKNLTRS LTREFINLNP IQRGGILPKE AKKAVYEYWD GYSVCDYCHG RLDEVTCPPI
KDFLEDIAKF LNMDCARPTH GAREGKFIVM HAICKEGDYV VLDKNAHYTS YVAAERAKLN
VAEVGYEEEY PTYKINLEGY KEVIDNLEDK GKNVGLILLT HVDGEYGNLN DAKKVGKIAK
EKGIPFLLNC AYTVGRMPVN GKEVKADFIV ASGHKSMAAS APCGILAFSE EFSDKITKTS
EKFPVKEIEM LGCTSRGLPI VTLMASFPHV VERVKKWDEE LKKTRYVVDE LEKIGFKQLG
IKPKEHDLIK FETPVLDEIA KKDKRRGFFF YDELKKRGIG GIRAGVTKEI KMSVYGLEWE
QVEYVVNAIK EIVESCK
