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O94567 (SYNC_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable asparagine--tRNA ligase, cytoplasmic
EC=6.1.1.22
Alternative name(s):
Asparaginyl-tRNA synthetase
Short name=AsnRS
Gene names
ORF Names:SPBC1773.10c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length568 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn).

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processasparaginyl-tRNA aminoacylation

Inferred by curator. Source: GeneDB_Spombe

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_Spombe

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

asparagine-tRNA ligase activity

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 568568Probable asparagine--tRNA ligase, cytoplasmic
PRO_0000176499

Sequences

Sequence LengthMass (Da)Tools
O94567 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 934483A10962BCAC

FASTA56863,870
        10         20         30         40         50         60 
MAGLESKVSD MKIKSDVVFY IDEASGNDET GNGSQTSPFK TAIHALETDA NCTIFVKKNG 

        70         80         90        100        110        120 
SEEFEPITTN ALKKAKKGVE QAAKKKAKAA EAEAAAAARA AAAKEAEAKR LEAAKNIVLK 

       130        140        150        160        170        180 
EPKDAPAAKK IAIIDSTNFR DSRVRVNGWV HRMRTQKGII FIILRDGTGF LQCVLSGKVY 

       190        200        210        220        230        240 
DRASYDFINL GPESTVCLYG VIKELPEGKS APGNHELVVD YYQILHAAPT GEEAFTNRLN 

       250        260        270        280        290        300 
AEAEPSYLLD QRHLVIRGET ASSVLKVRAR ALRAMRDTFE NLKMTEVTPP CMVQTQVEGG 

       310        320        330        340        350        360 
ATLFKFNYYG QDAYLTQSSQ LYLEAALPAL GSVYTIQESF RAEKSLTRRH LSEFTHVEFE 

       370        380        390        400        410        420 
LPFVNFGEFL EIIEEFICQT IDRLLDDPIA TPLIKQLNPD FVKPSRPFMR LSYEDAIKYL 

       430        440        450        460        470        480 
NEHNILTPEG EQHKFGDDIA EAAERKMTDQ INRPIFLTYF PLEIKSFYMK RVVDRPELTE 

       490        500        510        520        530        540 
SVDCLMPNVG EIVGGSMRIS DIQELLAAYK REGIDPAPYY WFTEQRKYGT TEHGGCGLGL 

       550        560 
ERFLAWLCDR YTVRECCLFP RFTERCTP

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329671 Genomic DNA. Translation: CAA21915.1.
PIRT39675.
RefSeqNP_595125.1. NM_001021032.1.

3D structure databases

ProteinModelPortalO94567.
ModBaseSearch...

Protein-protein interaction databases

STRINGO94567.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC1773.10c.1; SPBC1773.10c.1:pep; SPBC1773.10c.
GeneID2540046.
KEGGspo:SPBC1773.10c.
NMPDRfig|4896.1.peg.991.

Organism-specific databases

GeneDB_SpombeSPBC1773.10c.

Phylogenomic databases

eggNOGfuNOG07411.
GeneTreeEFGT00050000003411.
HOGENOMHBG745843.
OMACMVQTQV.
OrthoDBEOG47WRX6.

Gene expression databases

ArrayExpressO94567.

Family and domain databases

InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004522. Asn-tRNA-synth_IIb.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR004365. NA-bd_OB_tRNA-helicase.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KOK01893.
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PTHR22594:SF6. PTHR22594:SF6. 1 hit.
PfamPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMsTIGR00457. AsnS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYNC_SCHPO
AccessionPrimary (citable) accession number: O94567
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: May 1, 1999
Last modified: January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents