ID U5W5N1_9ACTN Unreviewed; 752 AA.
AC U5W5N1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AGZ44449.1};
GN ORFNames=AFR_30945 {ECO:0000313|EMBL:AGZ44449.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ44449.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ44449.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ44449.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP006272; AGZ44449.1; -; Genomic_DNA.
DR AlphaFoldDB; U5W5N1; -.
DR STRING; 1246995.AFR_30945; -.
DR KEGG; afs:AFR_30945; -.
DR PATRIC; fig|1246995.3.peg.6264; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_346706_0_0_11; -.
DR Proteomes; UP000017746; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:AGZ44449.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000017746};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AGZ44449.1};
KW Transferase {ECO:0000313|EMBL:AGZ44449.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..288
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 506..613
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 315..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..729
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 752 AA; 76662 MW; 720CA3A984D05962 CRC64;
MSTTDLPGSS LLAGRYRLVE RLGAGGMSVV WRGFDEVLGR QVAVKVLPPS TSTDPSFRRR
LRAEAQAAAR LSHPHITNVY DYGEATTVDG EPVPYVVMEL VDGESLAAVL ARVRRLPWPA
AVRICSEVSA ALAAAHSRGI VHRDVTPANV MLTPAGAKVV DFGISALIGE NDIDPDGSLL
GTPAYLAPER LEGGQVSPAT DVYAVGLLIY RTLIGQLPWD VGTTTALLRA HQYTEPEPLP
PVEGLPSAVS ALIARCLEKR PSDRPSSAEL AHVLGTVSAG VPSARAFVPD WADSGEDTTI
LPSAHDDHTD TMGRVRPGQA RVPQNAPAPG RGVAAVPAAA AGRDAPVSPA PAGAAVPQVS
VAEVEAAVGP VSAPPQRGGN RNSRFGPVPP VPPVASSPAA ADVAPSGPIG PPPSHNPSLR
PAFGADGPDR APAQAGGAGA PPKRPGPPGA GRGAPGPGRG PGSTQRRRIF FVGGAGVVLA
VVAMTAVFAN GAGPKNDAAK GVEPTTLTGS NKCVVSYAVW SDSNNRFKAA VTIANRDTKA
IKDWKLWFVM PGDQVVSGNG KLKLDQQGQG VTVSSKTVLS PQQTQTLQFS GRYVSSNAAP
MLFELGGTTC QTFVSPAPGE PSRPVEHLTN GTVRLGPVPT KDTPIPGISI NPSGVAVPVP
VTSSNPAGGV VVPTTAPTTA ATPGPTGTGD DDDDNTGGDG AVVPGPPDPP TTPPTTQPTT
EPPTSPPTTA PEQTYTEPSD QIPVPPGPPP FG
//
