ID K9W6Y3_9CYAN Unreviewed; 663 AA.
AC K9W6Y3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AFZ16120.1};
GN ORFNames=Mic7113_0184 {ECO:0000313|EMBL:AFZ16120.1};
OS Allocoleopsis franciscana PCC 7113.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ16120.1, ECO:0000313|Proteomes:UP000010471};
RN [1] {ECO:0000313|EMBL:AFZ16120.1, ECO:0000313|Proteomes:UP000010471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ16120.1,
RC ECO:0000313|Proteomes:UP000010471};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Microcoleus sp. PCC 7113.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003630; AFZ16120.1; -; Genomic_DNA.
DR AlphaFoldDB; K9W6Y3; -.
DR STRING; 1173027.Mic7113_0184; -.
DR KEGG; mic:Mic7113_0184; -.
DR PATRIC; fig|1173027.3.peg.199; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG3103; Bacteria.
DR HOGENOM; CLU_000288_135_5_3; -.
DR Proteomes; UP000010471; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR003646; SH3-like_bac-type.
DR PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24363:SF0; SERINE_THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08239; SH3_3; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AFZ16120.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000010471};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AFZ16120.1};
KW Transferase {ECO:0000313|EMBL:AFZ16120.1}.
FT DOMAIN 24..286
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 291..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 549..576
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 477..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 663 AA; 72681 MW; F6E5E60264CA37E9 CRC64;
MPRLENELCE RVTPMLGKLL DRRYEVTQVL GAGGFGRTYL AQDTRRPGNP TCVVKQLKPL
SSDPNFLETA RRLFNSEAET LEQLGHHDQI PRLLAYFEED QEFYLVQEFI EGHTLSQELQ
PGQRWEESRV MTLLEEVLGI LDFVHSHGVI HRDIKPDNLI RRNSDHKLVL VDFGAVKQIR
TQFAATQGRA SNTVAIGTPG YMASEQALGQ PRPTSDIYAL GIIAIQALTG LMPINFQEDL
STGEILWQHL VPISRGLATI LSKMVRYHFK DRYQSAAEAL ESLRLLNNTY SPPTPYPAVP
RTPSANDAPP FGQREQVSPP PYPPASISER QTLAASPGVP PRQPVATPVS TPRGGSSDKM
PLLVGIGMAI AVGAVGMAFA LRDGSLSSNY SGNGTQVADT SPGRCTVASR GLNIRSGPKG
SVVATVKQGT SLSLTGAEQN GWVEISAPKK GWVFNDSQYI KCTSANQTPI ETAQVNPKPI
ETTVSPKPVE TTVTQKPIET PQPKPSTTPP KPVDNSSKTL DTAADKYENG DLQGAIADAR
KVLPGSEAYK EAQAKIQKWQ DDWKAAEAKY NELQKAVDEG DWKKVLIVTT DPKFFEQRYW
RDKFTQLIEE AKKRKAEADA EANKNPTTPP EEPQQQKPLP DAKSSGNVSP TPAGETQDNP
TNQ
//