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Q8TYR3 (SPSS_METKA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
O-phospho-L-seryl-tRNA:Cys-tRNA synthase
EC=2.5.1.73
Alternative name(s):
Sep-tRNA:Cys-tRNA synthase
Short name=SepCysS
Gene names
Ordered Locus Names:MK0229
OrganismMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Taxonomic identifier190192 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanopyri › Methanopyrales › Methanopyraceae › Methanopyrus

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L-cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)) By similarity. HAMAP MF_01675

Catalytic activity

O-phospho-L-seryl-tRNA(Cys) + sulfide = L-cysteinyl-tRNA(Cys) + phosphate. HAMAP MF_01675

Cofactor

Pyridoxal phosphate By similarity. HAMAP MF_01675

Subunit structure

Homodimer. Interacts with SepRS By similarity. HAMAP MF_01675

Sequence similarities

Belongs to the SepCysS family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   LigandPyridoxal phosphate
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processtranslation

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionSep-tRNA:Cys-tRNA synthase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 392392O-phospho-L-seryl-tRNA:Cys-tRNA synthase HAMAP MF_01675
PRO_0000359456

Regions

Region84 – 852Pyridoxal phosphate binding By similarity
Region214 – 2163Pyridoxal phosphate binding By similarity

Sites

Binding site851Sulfur donor or Sep-tRNA(Cys) By similarity
Binding site1091Sulfur donor or Sep-tRNA(Cys) By similarity
Binding site1101Sulfur donor or Sep-tRNA(Cys) By similarity
Binding site1911Pyridoxal phosphate By similarity
Binding site2831Sulfur donor or Sep-tRNA(Cys) By similarity
Binding site2921Sulfur donor or Sep-tRNA(Cys) By similarity

Amino acid modifications

Modified residue2171N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8TYR3 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 28CFB3206D0621BA

FASTA39244,252
        10         20         30         40         50         60 
MNLDRYRNIV RETERKYINV NPIQRGGVLT PEARKALLEF GDGYSVCDFC EGLLHEIEKP 

        70         80         90        100        110        120 
PIRQFHEDLA EFLGMDVVRI TAGARYAKEA VMSALCEEGD VVVADSLAHY TTFVAAEKAG 

       130        140        150        160        170        180 
ATVREVPNTG HPEYKVKVDE YARVIDEVED ERGDPPALAL LTHVDSEYGN LADAEKFVKI 

       190        200        210        220        230        240 
CRKKGVPALL NCAYTMGRMD LSNLSPKPDF MVGSGHKGMA ACAPCGVLAM REEWEEEVLR 

       250        260        270        280        290        300 
GSSLRGDVSG REWPHKEVEM LGCTVMGAPI VTMMASFPHV VERVKRWKEE VRKTRWFVKE 

       310        320        330        340        350        360 
MERIEGVRQL GERPKRHDLV KFETPGFHEV AEDHPRRGYF LYEELKKRGV IGIQPGQTET 

       370        380        390 
IKASVYGLTD EQVEHVVRAF HEIAEEYGLE VS

« Hide

References

[1]"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens."
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed: 11930014] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE009439 Genomic DNA. Translation: AAM01446.1.
RefSeqNP_613516.1. NC_003551.1.

3D structure databases

ProteinModelPortalQ8TYR3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1477532.
GenomeReviewsGene locus MK0229 in contig AE009439_GR.
KEGGmka:MK0229.
NMPDRfig|190192.1.peg.229.

Phylogenomic databases

HOGENOMHBG539014.
OMALILNTAY.
ProtClustDBPRK09331.

Enzyme and pathway databases

BioCycMKAN190192:MK0229-MONOMER.

Family and domain databases

HAMAPMF_01675. Sep_Cys_tRNA_synth.
[Tree]
InterProIPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR013375. Sep_Cys-tRNA_synth_arc.
IPR008829. SLA/LP_auto_ag.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
KOK06868.
PfamPF05889. SLA_LP_auto_ag. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR02539. SepCysS. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSPSS_METKA
AccessionPrimary (citable) accession number: Q8TYR3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: June 1, 2002
Last modified: November 16, 2011
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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