[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. DOI=10.1128/MCB.20.23.8696-8708.2000; PubMed=11073971 [NCBI, ExPASy, EBI, Israel, Japan] Chen J., Zhou S., Wang Q., Chen X., Pan T., Liu H.; "Crk1, a novel Cdc2-related protein kinase, is required for hyphal development and virulence in Candida albicans."; Mol. Cell. Biol. 20:8696-8708(2000).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=SC5314; DOI=10.1073/pnas.0401648101; PubMed=15123810 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The diploid genome sequence of Candida albicans."; Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).

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). Required for pseudohyphal growth and virulence in mice.
CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
SUBCELLULAR LOCATION: Nucleus (By similarity).
SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.
SIMILARITY: Contains 1 protein kinase domain.
SEQUENCE CAUTION:
- Sequence=EAK95842.1; Type=Frameshift; Positions=364; Note=Produces 2 separate ORFs
- Sequence=EAK95843.1; Type=Frameshift; Positions=364; Note=Produces 2 separate ORFs

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U92261; AAD25159.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AACQ01000094; EAK95843.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AACQ01000094; EAK95842.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AACQ01000093; EAK95905.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_714882.1; -.
XP_714883.1; -.
XP_714945.1; -.

3D structure databases

HSSP

Q07785; 1OB3. [HSSP ENTRY / PDB]

ModBase

Q9Y7W4.

Organism-specific databases

CGD

CAL0073553; CRK1.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004693;	Molecular function: cyclin-dependent protein kinase activity (inferred from electronic annotation from EC).
GO:0008353;	Molecular function: RNA polymerase subunit kinase activity (inferred from electronic annotation from EC).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.

Pfam

PF00069; Pkinase; 1.
Pfam graphical view of domain structure.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00220; S_TKc; 1.
SMART graphical view of domain structure.

PROSITE

PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q9Y7W4.

Genome annotation databases

GeneID

3643350; -.
3643413; -.
3643414; -.

KEGG

cal:CaO19.11006; -.
cal:CaO19.3523; -.
cal:CaO19.3524; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Kinase; Nucleotide-binding; Nucleus; Serine/threonine-protein kinase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 746`	`746`	`Serine/threonine-protein kinase BUR1.`	`PRO_0000085679`
`DOMAIN`	`44 349`	`306`	`Protein kinase.`
`NP_BIND`	`50 58`	`9`	`ATP (By similarity).`
`ACT_SITE`	`179 179`		`Proton acceptor (By similarity).`
`BINDING`	`73 73`		`ATP (By similarity).`
`VARIANT`	`68 68`	`1`	`S -> L (in allele CaO19.3523/3524).`
`VARIANT`	`101 101`	`1`	`K -> Q (in allele CaO19.3523/3524).`
`VARIANT`	`189 189`	`1`	`Q -> H (in allele CaO19.3523/3524).`
`VARIANT`	`412 412`	`1`	`Missing (in allele CaO19.3523/3524).`
`VARIANT`	`463 463`	`1`	`S -> L (in allele CaO19.3523/3524).`
`VARIANT`	`505 505`	`1`	`S -> L (in allele CaO19.3523/3524).`
`VARIANT`	`516 516`	`1`	`V -> I (in allele CaO19.3523/3524).`
`VARIANT`	`529 529`	`1`	`S -> L (in allele CaO19.3523/3524).`
`VARIANT`	`578 578`	`1`	`R -> G (in allele CaO19.3523/3524).`
`VARIANT`	`649 651`	`3`	`SLS -> LLL (in allele CaO19.3523/3524).`
`CONFLICT`	`249 250`		`LW -> QR (in Ref. 1; AAD25159).`
`CONFLICT`	`493 493`		`A -> G (in Ref. 1; AAD25159).`
`CONFLICT`	`506 506`		`K -> Q (in Ref. 1; AAD25159).`

Sequence information

Length: 746 AA [This is the length of the unprocessed precursor]

Molecular weight: 83396 Da [This is the MW of the unprocessed precursor]

CRC64: 2E5B86F5EA624D85 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVIAGHHVP RSNDQRQYDT PSVPINIAPD SEGHIHEMSR LKDYEVIEKL GQGTFGVVQK 

        70         80         90        100        110        120 
AKSKKDGSLV AIKQLINHSA KEGFPITAMR EITILKQLNH KNILTIQDMI FEEPKMSNRT 

       130        140        150        160        170        180 
DIITMRGSFY TVTPYMSSDL VGLLENPKIK LELGQIKCIM QQLLKGIQYV HNQKFLHRDI 

       190        200        210        220        230        240 
KAANILIGQD GVLKIADFGL ARIYHGNVPR LGMGPGGGEK AYTGLVVTRW YRPPEILLGE 

       250        260        270        280        290        300 
RKYTTAVDLW GIGCVFAELF TGKPILVGKS DSHQAQIVFE LVGSPLTWTD AAKLPNKNEY 

       310        320        330        340        350        360 
SCGLACKRSL EAKFASIMPT EAIDLLSGLL TLDPFKRLNA LDALNHKFFS TDPLPLLPTQ 

       370        380        390        400        410        420 
MPKFEESHEI DKERFKKLKD KEQAVSELKP PTEIRYDNHS ESRYNADHST FGGGGVGGKE 

       430        440        450        460        470        480 
TSFSSGKSDY IDHYEPRARR DHYEPRIRND NKDSNDVRGE FESATRQEQR RRDIQNRLDA 

       490        500        510        520        530        540 
GGMDTYIPKT TTAKLREHSG TESLSKKYDN YQPINVSRGS KSPSPSKLSS ISQSKADLIS 

       550        560        570        580        590        600 
KPSAPKVASR ESSLERKQVS NGIRTTTDVE PPRARARRPT DMFGRPLTSN STQAQPTRNK 

       610        620        630        640        650        660 
SVERPKDLEK PTNGVTEDRN KKPVLEEKKE VVKPNLAIPK IKKSSSLVSL SSRSSTTPVI 

       670        680        690        700        710        720 
SNPSKVTKRA ASSVTPPVLP KKPKISKTSS ESEVSDLEED SDFTGENATV FERFMALEQL 

       730        740 
QKSPVYKRII NEKMRFEKLS GGHKSM

Q9Y7W4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools