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Q7KN90 (SYCC_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. Feed History...

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

Names and origin

Protein namesRecommended name:
Cysteine--tRNA ligase, cytoplasmic
EC=6.1.1.16
Alternative name(s):
Cysteinyl-tRNA synthetase
Short name=CysRS
Gene names
Name:Aats-cys
ORF Names:CG8431
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length741 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys).

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 741741Cysteine--tRNA ligase, cytoplasmic
PRO_0000348218

Regions

Motif48 – 5811"HIGH" region By similarity
Motif398 – 4025"KMSKS" region By similarity

Sites

Metal binding461Zinc By similarity
Metal binding3401Zinc By similarity
Metal binding3651Zinc By similarity
Metal binding3691Zinc By similarity
Binding site4011ATP By similarity

Amino acid modifications

Modified residue2971Phosphoserine Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q7KN90 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 73D758634149385F

FASTA74184,258
        10         20         30         40         50         60 
MSKRGQPAWQ APEAVDRPKL KLFNSLTRQK EDFVPLDGNN VTWYSCGPTV YDASHMGHAR 

        70         80         90        100        110        120 
SYISFDILRR ILSDYFGYNI HYVMNITDID DKIIRRARQN HLFDEYAAEA QKLPLDELLG 

       130        140        150        160        170        180 
QQKEVLQRFQ DTCAKNTDPD KKIMLDKTLQ RMNDAVEALT KAVGKGDERE ISEKRLLYLN 

       190        200        210        220        230        240 
EAKDPISDWL DSLKGAQIND NAVFEALPRY WEDQFHNDMK SLNILPPDVL TRVSEYVPQI 

       250        260        270        280        290        300 
VTFIQKIIDN GLAYAANNSV YFDVNGFDKR EKHHYAKLVP EAYGDTKSLQ EGEGDLSIAE 

       310        320        330        340        350        360 
DRLSEKRSAN DFALWKASKA GEPWWDSPWG KGRPGWHIEC SAMASDIFGP TFDIHTGGVD 

       370        380        390        400        410        420 
LKFPHHDNEL AQSEAAFNES EWVKYFLHTG HLTIAGCKMS KSLKNFVTIQ EALKKHSATQ 

       430        440        450        460        470        480 
LRLAFLLHSW KDTLDYSENT MEMATQYEKF LNEFFLNVKD LTRHVLSEEP RRQFDAWTEV 

       490        500        510        520        530        540 
EAALQKKFSN AQVQVHASLC DNIDTRSALD AIRELVSVSN VYIRDNKTRL NSLLLRNVAT 

       550        560        570        580        590        600 
YITDLLHVFG AISGPRGGIG FPVSGGSGAQ AAGADLETTV LPYVQSLAEF RYLVREQAKT 

       610        620        630        640        650        660 
LKAFDILKLC DDLRDNVLPN LGVRLEDKDI GKYAVKLVDR DSLLREREAK LAAEAEKAAE 

       670        680        690        700        710        720 
KERKKQAAAE AAAAKEAQRR VNPKEMFLAE TEKYSAFDEN GLPTHDKEGK EVSKGQIKKL 

       730        740 
QKLQQQQEQR YNEYLASIEK A

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"A Drosophila complementary DNA resource."
Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M., Harvey D.A.
Science 287:2222-2224(2000) [PubMed: 10731138] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[4]"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
Mol. Biosyst. 3:275-286(2007) [PubMed: 17372656] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE013599 Genomic DNA. Translation: AAF58057.1.
AF132160 mRNA. Translation: AAD34748.1.
RefSeqNP_611087.1. NM_137243.2.
UniGeneDm.1572.

3D structure databases

ProteinModelPortalQ7KN90.
SMRQ7KN90. Positions 17-636.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7KN90.

Proteomic databases

PRIDEQ7KN90.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0087234; FBpp0086373; FBgn0027091.
GeneID36784.
KEGGdme:Dmel_CG8431.
NMPDRfig|7227.3.peg.5523.
UCSCCG8431-RA. d. melanogaster.

Organism-specific databases

CTD36784.
FlyBaseFBgn0027091. Aats-cys.

Phylogenomic databases

eggNOGinNOG04916.
GeneTreeEMGT00050000004322.
InParanoidQ7KN90.
OMAEALCDNV.
OrthoDBEOG4CFXQ9.
PhylomeDBQ7KN90.

Gene expression databases

ArrayExpressQ7KN90.
BgeeQ7KN90.

Family and domain databases

InterProIPR015803. Cys-tRNA-synt.
IPR024909. Cys-tRNA/MSH_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 3 hits.
KOK01883.
PANTHERPTHR10890. Cys_tRNA-synt_1a. 1 hit.
PfamPF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSPR00983. TRNASYNTHCYS.
SUPFAMSSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMsTIGR00435. CysS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio800374.

Entry information

Entry nameSYCC_DROME
AccessionPrimary (citable) accession number: Q7KN90
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: October 3, 2006
Last modified: January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

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