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Protein

O-phospho-L-seryl-tRNA:Cys-tRNA synthase 1

Gene

AF_0028

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L-cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)).1 Publication

Catalytic activityi

O-phospho-L-seryl-tRNA(Cys) + sulfide = L-cysteinyl-tRNA(Cys) + phosphate.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791Sulfur donor or Sep-tRNA(Cys)
Binding sitei103 – 1031Sulfur donor or Sep-tRNA(Cys)
Binding sitei104 – 1041Sulfur donor or Sep-tRNA(Cys)
Binding sitei183 – 1831Pyridoxal phosphate
Binding sitei267 – 2671Sulfur donor or Sep-tRNA(Cys)
Binding sitei270 – 2701Sulfur donor or Sep-tRNA(Cys)

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-28-MONOMER.
BRENDAi2.5.1.73. 414.

Names & Taxonomyi

Protein namesi
Recommended name:
O-phospho-L-seryl-tRNA:Cys-tRNA synthase 1 (EC:2.5.1.73)
Alternative name(s):
Sep-tRNA:Cys-tRNA synthase 1
Short name:
SepCysS 1
Gene namesi
Ordered Locus Names:AF_0028
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
Proteomesi
  • UP000002199 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 371371O-phospho-L-seryl-tRNA:Cys-tRNA synthase 1PRO_0000107477Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei209 – 2091N6-(pyridoxal phosphate)lysine

Interactioni

Subunit structurei

Homodimer. Probably interacts with SepRS.1 Publication

Protein-protein interaction databases

STRINGi224325.AF0028.

Structurei

Secondary structure

1
371
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 174Combined sources
Helixi23 – 319Combined sources
Helixi55 – 606Combined sources
Helixi62 – 665Combined sources
Beta strandi69 – 779Combined sources
Helixi78 – 8912Combined sources
Beta strandi95 – 995Combined sources
Helixi104 – 1129Combined sources
Beta strandi116 – 1205Combined sources
Turni125 – 1273Combined sources
Helixi132 – 14211Combined sources
Turni143 – 1453Combined sources
Beta strandi148 – 1569Combined sources
Turni158 – 1603Combined sources
Helixi166 – 1749Combined sources
Turni175 – 1773Combined sources
Beta strandi180 – 1834Combined sources
Turni185 – 1873Combined sources
Helixi195 – 1984Combined sources
Beta strandi201 – 2066Combined sources
Helixi207 – 2104Combined sources
Beta strandi218 – 2225Combined sources
Turni224 – 2318Combined sources
Helixi242 – 2443Combined sources
Helixi252 – 26716Combined sources
Helixi268 – 2703Combined sources
Helixi271 – 28717Combined sources
Beta strandi291 – 2977Combined sources
Beta strandi300 – 3067Combined sources
Helixi308 – 3169Combined sources
Beta strandi317 – 3193Combined sources
Helixi320 – 3223Combined sources
Helixi323 – 3308Combined sources
Beta strandi342 – 3476Combined sources
Helixi353 – 36917Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E7IX-ray3.00A/B1-371[»]
2E7JX-ray2.40A/B1-371[»]
ProteinModelPortaliO30207.
SMRiO30207. Positions 8-371.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO30207.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni78 – 792Pyridoxal phosphate binding
Regioni206 – 2083Pyridoxal phosphate binding

Sequence similaritiesi

Belongs to the SepCysS family.Curated

Phylogenomic databases

eggNOGiarCOG00091. Archaea.
COG1103. LUCA.
KOiK06868.
OMAiWDGYSVC.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
HAMAPiMF_01675. Sep_Cys_tRNA_synth.
InterProiIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR013375. Sep_Cys-tRNA_synth_arc.
IPR008829. SepSecS/SepCysS.
[Graphical view]
PfamiPF05889. SepSecS. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR02539. SepCysS. 1 hit.

Sequencei

Sequence statusi: Complete.

O30207-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKRETKDFI NIDPLQTGGK LTEEARQALL EWGDGYSVCD FCTTGRLDEI
60 70 80 90 100
KTPPIHDFIH NQLPKFLGCD VARVTNGARE AKFAVMHSLA KKDAWVVMDE
110 120 130 140 150
NCHYSSYVAA ERAGLNIALV PKTDYPDYAI TPENFAQTIE ETKKRGEVVL
160 170 180 190 200
ALITYPDGNY GNLPDVKKIA KVCSEYDVPL LVNGAYAIGR MPVSLKEIGA
210 220 230 240 250
DFIVGSGHKS MAASGPIGVM GMKEEWAEIV LRRSEKYKNK EVELLGCTAR
260 270 280 290 300
GATIITLMAS FPHVRERIKR WDEEVEKARR FAAEMEKLGI KQLGDNPHNH
310 320 330 340 350
DLMFFHAEVL YEISKKAKGG RFFLYRELKS RKIHGIKPGL TRYFKLSTYG
360 370
LSDEEVDYVL NAFKEIIEKY S
Length:371
Mass (Da):41,930
Last modified:January 1, 1998 - v1
Checksum:iB22056D00437BEAA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB91200.1.
PIRiD69253.
RefSeqiWP_010877542.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB91200; AAB91200; AF_0028.
GeneIDi1483238.
KEGGiafu:AF_0028.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB91200.1.
PIRiD69253.
RefSeqiWP_010877542.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E7IX-ray3.00A/B1-371[»]
2E7JX-ray2.40A/B1-371[»]
ProteinModelPortaliO30207.
SMRiO30207. Positions 8-371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224325.AF0028.

Protocols and materials databases

DNASUi1483238.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB91200; AAB91200; AF_0028.
GeneIDi1483238.
KEGGiafu:AF_0028.

Phylogenomic databases

eggNOGiarCOG00091. Archaea.
COG1103. LUCA.
KOiK06868.
OMAiWDGYSVC.

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-28-MONOMER.
BRENDAi2.5.1.73. 414.

Miscellaneous databases

EvolutionaryTraceiO30207.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
HAMAPiMF_01675. Sep_Cys_tRNA_synth.
InterProiIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR013375. Sep_Cys-tRNA_synth_arc.
IPR008829. SepSecS/SepCysS.
[Graphical view]
PfamiPF05889. SepSecS. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR02539. SepCysS. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
    Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
    , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
    Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
  2. "Structural insights into the second step of RNA-dependent cysteine biosynthesis in archaea: crystal structure of Sep-tRNA:Cys-tRNA synthase from Archaeoglobus fulgidus."
    Fukunaga R., Yokoyama S.
    J. Mol. Biol. 370:128-141(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL-5'-PHOSPHATE, FUNCTION, PYRIDOXAL PHOSPHATE AT LYS-209, SUBUNIT.

Entry informationi

Entry nameiSPSS1_ARCFU
AccessioniPrimary (citable) accession number: O30207
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: November 11, 2015
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.