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Q4I5U9 (BUR1_GIBZE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Protein attributes

Sequence length539 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Serine/threonine-protein kinase involved in transcription regulation. Phosphorylates the UBC2/RAD6 ubiquitin-conjugating enzyme (E2), leading to monoubiquitination of histone H2B and the silencing of telomeric-associated genes. Also required for histone H3 methylation. Necessary for the recovery from pheromone-induced growth arrest in the cell cycle G1 phase By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Sequence caution

The sequence ESU13671.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 539539Serine/threonine-protein kinase BUR1
PRO_0000085683

Regions

Domain37 – 339303Protein kinase
Nucleotide binding43 – 519ATP By similarity
Compositional bias411 – 539129Arg-rich
Compositional bias432 – 49362Pro-rich

Sites

Active site1691Proton acceptor By similarity
Binding site661ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4I5U9 [UniParc].

Last modified October 31, 2012. Version 2.
Checksum: 1320870273F2BD61

FASTA53961,614
        10         20         30         40         50         60 
MEKLSETTPN GTSPRTFALN HSRPRSSFKG CSRISDYELL GKLGEGTFGE VHRARLRKTG 

        70         80         90        100        110        120 
ALVALKKIIM HHEKDGFPIT ALREIKLLKL LSHKNILRLE DMAIEHPTRQ TDKRKKPIVY 

       130        140        150        160        170        180 
MATPYMDHDL SGLLDNPSVQ FKEPQIKCYM LQLLEGLRYL HDSRILHRDM KAANLLINNK 

       190        200        210        220        230        240 
GILQIADFGL ARHYDGRTPE SGVPMGEGKR DYTGLVVTRW YRPPELLLQL RQYTPAIDVW 

       250        260        270        280        290        300 
GVGCVFGEML YGKPILAGES DAAQLDIIWD LMGSPNEENM PRWKSLPGAD HLTPRPRTGN 

       310        320        330        340        350        360 
LETRFRQYGS GAVSLLKELL RLDWRTRINA VDALQHPWFK MQPLPLEPHE IPTYEESHEL 

       370        380        390        400        410        420 
DRRKFHDRKA ALPPAPKGGT VGVGPDANGA TAGFNSNEPY GNGRNGVNGG RYRNGPDDRR 

       430        440        450        460        470        480 
PAWQRERGAG LPPRPPPNND DADFRERGPP RARGPPGPRG PDVDTYIPAY NRDDPGRRRD 

       490        500        510        520        530 
DRPPPPRDDR PPPRDDRRRR NSREDRRFDR DRGTMSRSRS PRHDRSRDRD RPDHNGYRR 

« Hide

References

« Hide 'large scale' references
[1]"The Fusarium graminearum genome reveals a link between localized polymorphism and pathogen specialization."
Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S. expand/collapse author list , Goswami R.S., Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M., Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.
Science 317:1400-1402(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084.
[2]"Comparative genomics reveals mobile pathogenicity chromosomes in Fusarium."
Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R., Antoniw J., Baker S.E. expand/collapse author list , Bluhm B.H., Breakspear A., Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C., Rep M.
Nature 464:367-373(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS231666 Genomic DNA. Translation: ESU13671.1. Sequence problems.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5518.FG07409.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiFGSG_07409T0; FGSG_07409P0; FGSG_07409.

Phylogenomic databases

eggNOGCOG0515.
OrthoDBEOG7K3TWD.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBUR1_GIBZE
AccessionPrimary (citable) accession number: Q4I5U9
Secondary accession number(s): I1RTA8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: October 31, 2012
Last modified: June 11, 2014
This is version 65 of the entry and version 2 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