[1]	NUCLEOTIDE SEQUENCE. STRAIN=CW15; DOI=10.1034/j.1399-3054.2002.1150416.x; PubMed=12121468 [NCBI, ExPASy, EBI, Israel, Japan] Huang K., Merkle T., Beck C.F.; "Isolation and characterization of a Chlamydomonas gene that encodes a putative blue-light photoreceptor of the phototropin family."; Physiol. Plantarum 115:613-622(2002).
[2]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 17-125. PubMed=12668455 [NCBI, ExPASy, EBI, Israel, Japan] Fedorov R., Schlichting I., Hartmann E., Domratcheva T., Fuhrmann M., Hegemann P.; "Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii."; Biophys. J. 84:2474-2482(2003).

Comments

CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.

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

AJ416556; CAC94940.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1N9L; X-ray; 1.90 A; A=17-125.	[ExPASy / RCSB / EBI]
1N9N; X-ray; 2.30 A; A=17-125.	[ExPASy / RCSB / EBI]
1N9O; X-ray; 2.80 A; A=17-125.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1N9L; -.
1N9N; -.
1N9O; -.

ModBase

Q8LPE0.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004674;	Molecular function: protein serine/threonine kinase activity (inferred from electronic annotation from InterPro).
GO:0004872;	Molecular function: receptor activity (inferred from electronic annotation from UniProtKB-KW).
GO:0000155;	Molecular function: two-component sensor activity (inferred from electronic annotation from InterPro).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0006355;	Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from InterPro).
GO:0000160;	Biological process: two-component signal transduction system (phosphorelay) (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000961; AGC-kinase_C.
IPR001610; PAC.
IPR000014; PAS.
IPR000700; PAS-assoc_C.
IPR013655; PAS_fold_3.
IPR000719; Prot_kinase_core.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.

Pfam

PF08447; PAS_3; 2.
PF00069; Pkinase; 1.
Pfam graphical view of domain structure.

ProDom

PD000001; Prot_kinase; 2.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00086; PAC; 2.
SM00091; PAS; 2.
SM00220; S_TKc; 1.
SMART graphical view of domain structure.

TIGRFAMs

TIGR00229; sensory_box; 2.

PROSITE

PS51285; AGC_KINASE_CTER; 1.
PS50113; PAC; 2.
PS50112; PAS; 2.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).

Proteomics databases

PRIDE

Q8LPE0; -.

Other

UniRef

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

Keywords

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

Features

None

Sequence information

Length: 750 AA

Molecular weight: 81480 Da

CRC64: E5B649BC8732C2A1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGVPAPASQ LTKVLAGLRH TFVVADATLP DCPLVYASEG FYAMTGYGPD EVLGHNCRFL 

        70         80         90        100        110        120 
QGEGTDPKEV QKIRDAIKKG EACSVRLLNY RKDGTPFWNL LTVTPIKTPD GRVSKFVGVQ 

       130        140        150        160        170        180 
VDVTSKTEGK ALADNSGVPL LVKYDHRLRD NVARTIVDDV TIAVEKAEGV EPGQASAVAA 

       190        200        210        220        230        240 
AAPLGAKGPR GTAPKSFPRV ALDLATTVER IQQNFCISDP TLPDCPIVFA SDAFLELTGY 

       250        260        270        280        290        300 
SREEVLGRNC RFLQGAGTDR GTVDQIRAAI KEGSELTVRI LNYTKAGKAF WNMFTLAPMR 

       310        320        330        340        350        360 
DQDGHARFFV GVQVDVTAQS TSPDKAPVWN KTPEEEVAKA KMGAEAASLI SSALQGMAAP 

       370        380        390        400        410        420 
TTANPWAAIS GVIMRRKPHK ADDKAYQALL QLQERDGKMK LMHFRRVKQL GAGDVGLVDL 

       430        440        450        460        470        480 
VQLQGSELKF AMKTLDKFEM QERNKVARVL TESAILAAVD HPFLATLYCT IQTDTHLHFV 

       490        500        510        520        530        540 
MEYCEGGELY GLLNSQPKKR LKEEHVRFYA SEVLTALQYL HLLGYVYRDL KPENILLHHT 

       550        560        570        580        590        600 
GHVLLTDFDL SYSKGSTTPR IEKIGGAGAA GGSAPKSPKK SSSKSGGSSS GSALQLENYL 

       610        620        630        640        650        660 
LLAEPSARAN SFVGTEEYLA PEVINAAGHG PAAVDWWSLG ILIFELLYGT TPFRGARRDE 

       670        680        690        700        710        720 
TFENIIKSPL KFPSKPAVSE ECRDLIEKLL VKDVGARLGS RTGANEIKSH PWFKGINWAL 

       730        740        750 
LRHQQPPYVP RRASKAAGGS STGGAAFDNY

Q8LPE0 in FASTA format

View entry in original UniProtKB/TrEMBL format
View entry in raw text format (no links)
Request for annotation of this UniProtKB/TrEMBL entry

	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