[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=SAS56; Schulze Gronover C., Tudzynski P., Tudzynski B.; "bpk3, a clk-like serine-threonine protein kinase from Botryotinia fuckeliana."; Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Serine/threonine protein kinase probably involved in the cytoplasm to vacuole transport (Cvt) and in autophagy, where it may be required for the formation of autophagosomes (By similarity).
CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. APG1/unc-51/ULK1 subfamily.
SIMILARITY: Contains 1 protein kinase domain.

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

AJ608273; CAE55218.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q6H9I1.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
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:0006914;	Biological process: autophagy (inferred from electronic annotation from UniProtKB-KW).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0015031;	Biological process: protein transport (inferred from electronic annotation from UniProtKB-KW).
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

Q6H9I1.

Other

UniRef

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

Keywords

ATP-binding; Autophagy; Cytoplasm; Kinase; Nucleotide-binding; Protein transport; Serine/threonine-protein kinase; Transferase; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 952`	`952`	`Serine/threonine-protein kinase ATG1.`	`PRO_0000085640`
`DOMAIN`	`23 329`	`307`	`Protein kinase.`
`NP_BIND`	`29 37`	`9`	`ATP (By similarity).`
`ACT_SITE`	`166 166`		`Proton acceptor (By similarity).`
`BINDING`	`52 52`		`ATP (By similarity).`

Sequence information

Length: 952 AA [This is the length of the unprocessed precursor]

Molecular weight: 105041 Da [This is the MW of the unprocessed precursor]

CRC64: 90AEAE54056440EB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASTTTSTSS LSSRRQKTGV GSFTINEQIG KGSFATVYRG THMPSGNLVA IKSVNLSRLN 

        70         80         90        100        110        120 
KKLKDNLYVE IEILKSLYHP HIVALIDCRE SASHIHLMME YCELGDLSYF IKKRDRLADN 

       130        140        150        160        170        180 
PTLYDMVQKY PMPVEGGLNQ VVVRHFFKQL SSAMEFLRER DFVHRDVKPQ NLLLIPSPEW 

       190        200        210        220        230        240 
IAKRAKGGPE AMKASKESVV AMVGINSLPM LKLADFGFAR SLPSTSLAET LCGSPLYMAP 

       250        260        270        280        290        300 
EILRYEKYDA RADLWSIGTV LYEMMTGRPP FKAINHVQLL QKIEKNQDEI RFPSRGIYSR 

       310        320        330        340        350        360 
DLKDIVRRLL KKKPEDRITF PEYFAHPVVT EPIPGLVGDD RPKEKSPETS IVRQPSLRDR 

       370        380        390        400        410        420 
QRESPTVKHI DTAYESLITR DIGEQSPRTP NIESNQPFGT PGRSSGRPDS RDRPSPVSAA 

       430        440        450        460        470        480 
TAPNVDTLPR QRDRKDRTEP NYAPIVRTGS TKQRYDEQAN LQPKNEVQSS NSITEAEQDV 

       490        500        510        520        530        540 
RDAREYVLVE KKAVEVNAFA DEMAANPRLG RANSAPKQLP RRHTSMGEPN STTGAVAVPP 

       550        560        570        580        590        600 
SRIVQRASGR AQPDTSSARN SYGSYGKTGS SPSTASAIAK ALQGASVRVF GVSWSPTLIG 

       610        620        630        640        650        660 
KGPSPPQLYN PYPAYPTPNA GLIGDGRPID EDQRVVNIIE DSATRSDVVY GFAEVKYRQL 

       670        680        690        700        710        720 
IPLAPSMNHG LGGPNPERTG DAMDEDDGLT VEAIVNLSEE ALVLYVKSLS LLSKSMDIAG 

       730        740        750        760        770        780 
AWWSRKQRGG IVSGGHTPGS DSSSAAQAGN RINGAVQWVR TRFNEVLEKA ELVRLKLVEA 

       790        800        810        820        830        840 
QKRLPEDHPG HPNNRSTASR LVGGSSTTDG VVLSSGITAE KLMYDRALEM SRTAAINELA 

       850        860        870        880        890        900 
NEDLPGCEIS YTTAIRMLEA VLENDEELIP RKRSSSLRED KEKSEGGEVN GINFGDRKDV 

       910        920        930        940        950 
LKVLQMIRTR LQVLKKKMTA IAKHQSMPPP SSSPRRSYSG GTTPTINNTP PK

Q6H9I1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot 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