NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(95)00771-7; PubMed=8635757 [NCBI, ExPASy, EBI, Israel, Japan]
Ueda K., Umeyama T., Beppu T., Horinouchi S.;
"The aerial mycelium-defective phenotype of Streptomyces griseus resulting from A-factor deficiency is suppressed by a Ser/Thr kinase of S. coelicolor A3(2).";
Gene 169:91-95(1996).

Comments

FUNCTION: Component of the afsK/afsR system involved in the response of aerial mycelium formation to glucose.
CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
SUBUNIT: Interacts (via the N-terminal kinase domain) with kbpA; the interaction prevents autophosphorylation of afsK (By similarity).
PTM: Autophosphorylated mainly on threonine residues. Some phosphorylation on serine residues. Autophosphorylation on Thr-168 is the major site enhancing kinase activity towards afsR, and is regulated though interaction with kbpA (By similarity).
SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
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

D45246; BAA08203.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P71584; 1MRU. [HSSP ENTRY / PDB]

ModBase

P54742.

PTM databases

PhosSite

P54742; -.

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:0006468;	Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR002372; PQQ_repeat.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR011047; Quino_AlcDHase-like.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
Graphical view of domain structure.

Gene3D

G3DSA:2.140.10.10; Quinoprotein_alc_DH-like; 2.

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

SM00564; PQQ; 8.
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).

Other

ProtoNet

P54742.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 807`	`807`	`Serine/threonine-protein kinase afsK.`	`PRO_0000171235`
`DOMAIN`	`16 272`	`257`	`Protein kinase.`
`NP_BIND`	`22 30`	`9`	`ATP (By similarity).`
`ACT_SITE`	`138 138`		`Proton acceptor (By similarity).`
`BINDING`	`44 44`		`ATP (By similarity).`
`MOD_RES`	`71 71`		`Phosphoserine; by autocatalysis (By similarity).`
`MOD_RES`	`168 168`		`Phosphothreonine; by autocatalysis (By similarity).`

Sequence information

Length: 807 AA [This is the length of the unprocessed precursor]

Molecular weight: 85232 Da [This is the MW of the unprocessed precursor]

CRC64: 66C274219155D091 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVEQLTQHDP RRIGPFEVLG RLGAGGMGLV YLARSASGRR VAIKTVRTEL AEDQLFRVRF 

        70         80         90        100        110        120 
TREVEAARAV SGFYTAAVVD ADPRAAVPWL ATAYVPAPSL EEIVNECGPM PTQAVRWLAA 

       130        140        150        160        170        180 
GIAQALQSIH GAGLVHRDLK PSNVLVVEDG PRVIDFGIAS GVSNTRLTMT NVAVGTPAYM 

       190        200        210        220        230        240 
SPEQARDSRS VTGASDIFSL GSTLVFAATG HAPFHGANPV ETVFMLVREG PDLEGLPDDL 

       250        260        270        280        290        300 
RPLIESCMQM DATHPAAEPR DLQAQLAPHL FASGSDDSGT ASAWLPVPAT AMIERRRGGR 

       310        320        330        340        350        360 
RTARRPPRPR PRRLRAAPQG PGAGHRLAQR GRPAFALPAV LALAAVRRVR TAAGPSAAPD 

       370        380        390        400        410        420 
GGPVQLPGAK VPIGPGRRAG EGRGAAAAAP RRRDRLGPAA RRSERFLGGH GPHRTVPAST 

       430        440        450        460        470        480 
LRPGTPSPAP DRWRPWRFRM SNDVWGTPVV SGDLLYVTSF EVHALDVGNG RRQFKTRDVA 

       490        500        510        520        530        540 
WAMAVEGGRI HASDGPSLYA LDAASGAEQW RLATDAWVYA LKADRGTVLT ATRGGGVQGW 

       550        560        570        580        590        600 
EASNGEKLWE VTGAQSDFET AEAGPVIHDG TVYLWQDARL RALDARTGLE RWSYPIGDAA 

       610        620        630        640        650        660 
SCGGVPVRVT PATDGYVYVA AGTRVLAVET GSGPVRWHFE APAVFLSPPA FAPGPAVTGG 

       670        680        690        700        710        720 
GVYLADYLGT VYALDATTGK DRWRIATEAR SSIEPVLVAV GNVHVGSGSA LYTLDAVTDT 

       730        740        750        760        770        780 
PKWRFAAGGD VVGAPWWRRP GPLRLGGPRA LHPGRGGRPA ALKLATGGEI TGSPVAQAGV 

       790        800 
VYACSKDRCV YALDALKGTG TGNRART

P54742 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