SPSS1_ARCFU
ID SPSS1_ARCFU Reviewed; 371 AA.
AC O30207;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=O-phospho-L-seryl-tRNA:Cys-tRNA synthase 1;
DE EC=2.5.1.73;
DE AltName: Full=Sep-tRNA:Cys-tRNA synthase 1;
DE Short=SepCysS 1;
GN OrderedLocusNames=AF_0028;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2] {ECO:0007744|PDB:2E7I, ECO:0007744|PDB:2E7J}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH
RP PYRIDOXAL-5'-PHOSPHATE, FUNCTION, PYRIDOXAL PHOSPHATE AT LYS-209, AND
RP SUBUNIT.
RX PubMed=17512006; DOI=10.1016/j.jmb.2007.04.050;
RA Fukunaga R., Yokoyama S.;
RT "Structural insights into the second step of RNA-dependent cysteine
RT biosynthesis in archaea: crystal structure of Sep-tRNA:Cys-tRNA synthase
RT from Archaeoglobus fulgidus.";
RL J. Mol. Biol. 370:128-141(2007).
CC -!- FUNCTION: Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L-
CC cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)). {ECO:0000269|PubMed:17512006}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homodimer. Probably interacts with SepRS.
CC {ECO:0000269|PubMed:17512006}.
CC -!- SIMILARITY: Belongs to the SepCysS family. {ECO:0000305}.
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DR EMBL; AE000782; AAB91200.1; -; Genomic_DNA.
DR PIR; D69253; D69253.
DR RefSeq; WP_010877542.1; NC_000917.1.
DR PDB; 2E7I; X-ray; 3.00 A; A/B=1-371.
DR PDB; 2E7J; X-ray; 2.40 A; A/B=1-371.
DR PDBsum; 2E7I; -.
DR PDBsum; 2E7J; -.
DR AlphaFoldDB; O30207; -.
DR SMR; O30207; -.
DR STRING; 224325.AF_0028; -.
DR DNASU; 1483238; -.
DR EnsemblBacteria; AAB91200; AAB91200; AF_0028.
DR GeneID; 1483238; -.
DR KEGG; afu:AF_0028; -.
DR eggNOG; arCOG00091; Archaea.
DR HOGENOM; CLU_060476_0_0_2; -.
DR OMA; HKSMAAS; -.
DR OrthoDB; 24071at2157; -.
DR PhylomeDB; O30207; -.
DR BRENDA; 2.5.1.73; 414.
DR EvolutionaryTrace; O30207; -.
DR Proteomes; UP000002199; 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..371
FT /note="O-phospho-L-seryl-tRNA:Cys-tRNA synthase 1"
FT /id="PRO_0000107477"
FT BINDING 78..79
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17512006,
FT ECO:0007744|PDB:2E7I, ECO:0007744|PDB:2E7J"
FT BINDING 183
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17512006"
FT BINDING 206..208
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17512006,
FT ECO:0007744|PDB:2E7I, ECO:0007744|PDB:2E7J"
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:17512006,
FT ECO:0007744|PDB:2E7I, ECO:0007744|PDB:2E7J"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:2E7J"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:2E7J"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:2E7J"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:2E7J"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:2E7J"
FT HELIX 78..89
FT /evidence="ECO:0007829|PDB:2E7J"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:2E7J"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:2E7J"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:2E7J"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:2E7J"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:2E7J"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:2E7J"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:2E7J"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:2E7J"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:2E7J"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:2E7J"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:2E7J"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:2E7J"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:2E7J"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:2E7J"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:2E7J"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:2E7J"
FT TURN 224..231
FT /evidence="ECO:0007829|PDB:2E7J"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:2E7J"
FT HELIX 252..267
FT /evidence="ECO:0007829|PDB:2E7J"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:2E7J"
FT HELIX 271..287
FT /evidence="ECO:0007829|PDB:2E7J"
FT STRAND 291..297
FT /evidence="ECO:0007829|PDB:2E7J"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:2E7J"
FT HELIX 308..316
FT /evidence="ECO:0007829|PDB:2E7J"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:2E7J"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:2E7J"
FT HELIX 323..330
FT /evidence="ECO:0007829|PDB:2E7J"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:2E7J"
FT HELIX 353..369
FT /evidence="ECO:0007829|PDB:2E7J"
SQ SEQUENCE 371 AA; 41930 MW; B22056D00437BEAA CRC64;
MFKRETKDFI NIDPLQTGGK LTEEARQALL EWGDGYSVCD FCTTGRLDEI KTPPIHDFIH
NQLPKFLGCD VARVTNGARE AKFAVMHSLA KKDAWVVMDE NCHYSSYVAA ERAGLNIALV
PKTDYPDYAI TPENFAQTIE ETKKRGEVVL ALITYPDGNY GNLPDVKKIA KVCSEYDVPL
LVNGAYAIGR MPVSLKEIGA DFIVGSGHKS MAASGPIGVM GMKEEWAEIV LRRSEKYKNK
EVELLGCTAR GATIITLMAS FPHVRERIKR WDEEVEKARR FAAEMEKLGI KQLGDNPHNH
DLMFFHAEVL YEISKKAKGG RFFLYRELKS RKIHGIKPGL TRYFKLSTYG LSDEEVDYVL
NAFKEIIEKY S
