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Q59PR3 (DBP8_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
ATP-dependent RNA helicase DBP8

EC=3.6.4.13
Gene names
Name:DBP8
ORF Names:CaO19.13973, CaO19.6652
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

ATP-binding RNA helicase involved in 40S ribosomal subunit biogenesis and is required for the normal formation of 18S rRNAs through pre-rRNA processing at A0, A1 and A2 sites. Required for vegetative growth By similarity.

Catalytic activity

ATP + H2O = ADP + phosphate.

Subcellular location

Nucleusnucleolus By similarity.

Domain

The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.

Sequence similarities

Belongs to the DEAD box helicase family. DDX49/DBP8 subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Ontologies

Keywords
   Biological processRibosome biogenesis
rRNA processing
   Cellular componentNucleus
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processrRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 440440ATP-dependent RNA helicase DBP8
PRO_0000232283

Regions

Domain32 – 208177Helicase ATP-binding
Domain247 – 387141Helicase C-terminal
Nucleotide binding45 – 528ATP By similarity
Motif1 – 2929Q motif
Motif154 – 1574DEAD box

Sequences

Sequence LengthMass (Da)Tools
Q59PR3 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 5A2483E47C9368DB

FASTA44048,832
        10         20         30         40         50         60 
MSFNDLGVAK WLSESLDAMK IYTPTAIQSA CIPAILKGHD CIGGAKTGSG KTIAFAAPML 

        70         80         90        100        110        120 
TQWSEDPFGI FGLILTPTRE LALQIAEQFA ALGANMNIKV AVVVGGEDFV QQTLALQRKP 

       130        140        150        160        170        180 
HFVIATPGRL ADHILNSGEE TISGLRRVKY LVLDEADRLL SNSFGSDLQR CFDVLPTSDK 

       190        200        210        220        230        240 
RQTLLFTATI TDAVRALKEK PPTPGKPPVF MHEVETVDKV AIPSTLQISY VFVPSYVKEA 

       250        260        270        280        290        300 
YLNSILHLEQ FKDSTAVIFV NRTTTAEVLR RMLRKLDFRV ASLHSEMPQS ERTNSLHRFK 

       310        320        330        340        350        360 
AGAARILIAT DVASRGLDIP TVELVINFDI PADPDDFIHR VGRTARAGRK GDAVSIIGEK 

       370        380        390        400        410        420 
DIDRIQSIEE RINKKMELLE DVNDDNVIKE SLSATSVAKR ESLMEMDKEN FGERKKINRK 

       430        440 
KHGLDKVKPE RVTKPKKSKK 

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References

[1]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACQ01000165 Genomic DNA. Translation: EAK92999.1.
AACQ01000186 Genomic DNA. Translation: EAK92496.1.
RefSeqXP_711718.1. XM_706626.1.
XP_712192.1. XM_707099.1.

3D structure databases

ProteinModelPortalQ59PR3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1229785. 1 interaction.
STRING5476.CAL0004058.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3646191.
3646692.
KEGGcal:CaO19.13973.
cal:CaO19.6652.

Organism-specific databases

CGDCAL0004058. DBP8.

Phylogenomic databases

eggNOGCOG0513.
KOK14778.
OrthoDBEOG7FR7R5.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDBP8_CANAL
AccessionPrimary (citable) accession number: Q59PR3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 26, 2005
Last modified: April 16, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Candida albicans

Candida albicans: entries and gene names