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D3ZEG9 (D3ZEG9_RAT) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 35. Feed History...

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

Protein attributes

Sequence length760 AA.
Sequence statusComplete.
Protein existencePredicted

General annotation (Comments)

Catalytic activity

ATP + H2O = ADP + phosphate. SAAS SAAS013020

Sequence similarities

Contains helicase ATP-binding domain. SAAS SAAS013020

Ontologies

Keywords
   Cellular componentNucleus SAAS SAAS014013
   LigandATP-binding
Nucleotide-binding
   Molecular functionHelicase SAAS SAAS013020
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processUV protection

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

bone mineralization

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from electronic annotation. Source: Ensembl

central nervous system myelin formation

Inferred from electronic annotation. Source: Ensembl

chromosome segregation

Inferred from electronic annotation. Source: Ensembl

embryonic cleavage

Inferred from electronic annotation. Source: Ensembl

erythrocyte maturation

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Inferred from electronic annotation. Source: Ensembl

hair cell differentiation

Inferred from electronic annotation. Source: Ensembl

hair follicle maturation

Inferred from electronic annotation. Source: Ensembl

hematopoietic stem cell differentiation

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

nucleotide-excision repair, DNA incision

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA binding

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

regulation of mitotic cell cycle phase transition

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from expression pattern PubMed 9763211. Source: RGD

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

spinal cord development

Inferred from electronic annotation. Source: Ensembl

transcription-coupled nucleotide-excision repair

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentMMXD complex

Inferred from electronic annotation. Source: Ensembl

cyclin-dependent protein kinase activating kinase holoenzyme complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_function5'-3' DNA helicase activity

Inferred from electronic annotation. Source: Ensembl

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent DNA helicase activity

Inferred from electronic annotation. Source: InterPro

DNA binding

Inferred from electronic annotation. Source: InterPro

RNA polymerase II carboxy-terminal domain kinase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
D3ZEG9 [UniParc].

Last modified April 20, 2010. Version 1.
Checksum: AC4316E1F21BCF67

FASTA76086,814
        10         20         30         40         50         60 
MKLNVDGLLV YFPYDYIYPE QFSYMLELKR TLDAKGHGVL EMPSGTGKTV SLLALIVAYQ 

        70         80         90        100        110        120 
RAYPLEVTKL IYCSRTVPEI EKVIEELRKL LSFYEQQEGE KLPFLGLALS SRKNLCIHPE 

       130        140        150        160        170        180 
VTPLRFGKDV DGKCHSLTAS YVRAQYQQDA SLPHCRFYEE FDTHGRQVPL PAGIYNLDDL 

       190        200        210        220        230        240 
KALGQRQGWC PYFLARYSIL HANVVVYSYH YLLDPKIADL VSKELARKAV VVFDEAHNID 

       250        260        270        280        290        300 
NVCIDSMSVN LTRRTLDRCQ SNLDTLQKTV LRIKETDEQR LRDEYRRLVE GLREASAARE 

       310        320        330        340        350        360 
TDAHLANPVL PDEVLQEAVP GSIRTAEHFL GFLRRLLEYV KWRLRVQHVV QESPPAFLSG 

       370        380        390        400        410        420 
LAQRVCIQRK PLRFCAERLR SLLHTLEIAD LADFSPLTLL ANFATLVSTY AKGFTIIIEP 

       430        440        450        460        470        480 
FDDRTPTITN PILHFSCMDA SLAIKPVFER FQSVIITSGT LSPLDIYPKI LDFHPVTMAT 

       490        500        510        520        530        540 
FTMTLARVCL CPMIIGRGND QVAISSKFET REDIAVIRNY GNLLLEMSAV VPDGIVAFFT 

       550        560        570        580        590        600 
SYQYMESTVA SWYEQGILEN IQRNKLLFIE TQDGAETSVA LEKYQEACEN GRGAILLSVA 

       610        620        630        640        650        660 
RGKVSEGIDF VHHYGRAVIM FGVPYVYTQS RILKARLEYL RDQFQIREND FLTFDAMRHA 

       670        680        690        700        710        720 
AQCVGRAIRG KTDYGLMVFA DKRFARADKR GKLPRWIQEH LTDSNLNLTV DEGVQVAKYF 

       730        740        750        760 
LRQMAQPFHR EDQLGLSLLS LEQLQSEETL QRIEQIAQQL 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Rat Genome Sequencing Project Consortium
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway Ensembl ENSRNOP00000024247.
[2]"Gene and alternative splicing annotation with AIR."
Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M., Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z., Istrail S., Li P., Sutton G.
Genome Res. 15:54-66(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BN EMBL EDM08205.1.
[3]Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M., Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F. expand/collapse author list , Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BN EMBL EDM08205.1.
[4]Ensembl
Submitted (JUL-2011) to UniProtKB
Cited for: IDENTIFICATION.
Strain: Brown Norway Ensembl ENSRNOP00000024247.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR06003883 Genomic DNA. No translation available.
CH473979 Genomic DNA. Translation: EDM08205.1.
RefSeqNP_001166280.1. NM_001172809.1.
UniGeneRn.41871.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000024246; ENSRNOP00000024247; ENSRNOG00000017753.
GeneID308415.
KEGGrno:308415.

Organism-specific databases

CTD2068.
RGD1309109. Ercc2.

Phylogenomic databases

GeneTreeENSGT00550000075092.
KOK10844.
OMADEVWKYK.
OrthoDBEOG70W3CM.
PhylomeDBD3ZEG9.
TreeFamTF101232.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR006555. ATP-dep_Helicase_C.
IPR010614. DEAD_2.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR013020. DNA_helicase_DNA-repair_Rad3.
IPR010643. DUF1227.
IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3.
IPR006554. Helicase-like_DEXD_c2.
IPR027417. P-loop_NTPase.
IPR001945. XPGD_DNA_repair.
[Graphical view]
PfamPF06733. DEAD_2. 1 hit.
PF06777. DUF1227. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view]
PRINTSPR00852. XRODRMPGMNTD.
SMARTSM00488. DEXDc2. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 4 hits.
TIGRFAMsTIGR00604. rad3. 1 hit.
PROSITEPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51193. HELICASE_ATP_BIND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio658821.

Entry information

Entry nameD3ZEG9_RAT
AccessionPrimary (citable) accession number: D3ZEG9
Entry history
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: April 20, 2010
Last modified: July 9, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)