ID A0A0D6KMW6_9CYAN Unreviewed; 777 AA.
AC A0A0D6KMW6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Kinase domain protein {ECO:0000313|EMBL:EKF01105.1};
GN ORFNames=FDUTEX481_08281 {ECO:0000313|EMBL:EKF01105.1};
OS Tolypothrix sp. PCC 7601.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1188 {ECO:0000313|EMBL:EKF01105.1, ECO:0000313|Proteomes:UP000032761};
RN [1] {ECO:0000313|EMBL:EKF01105.1, ECO:0000313|Proteomes:UP000032761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX PubMed=25953173;
RA Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA Kehoe D.M., Weinstock G.M.;
RT "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT PCC 7601.";
RL Genome Announc. 3:0-0(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKF01105.1}.
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DR EMBL; AGCR01000044; EKF01105.1; -; Genomic_DNA.
DR RefSeq; WP_045871270.1; NZ_JH930362.1.
DR AlphaFoldDB; A0A0D6KMW6; -.
DR STRING; 1188.FDUTEX481_08281; -.
DR PATRIC; fig|1188.3.peg.5289; -.
DR HOGENOM; CLU_334888_0_0_3; -.
DR OrthoDB; 428645at2; -.
DR Proteomes; UP000032761; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR007890; CHASE2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24363:SF0; SERINE_THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR Pfam; PF05226; CHASE2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM01080; CHASE2; 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 Kinase {ECO:0000313|EMBL:EKF01105.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Transferase {ECO:0000313|EMBL:EKF01105.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 356..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 482..744
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 513
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 777 AA; 85986 MW; 487FFC594DF5A7A6 CRC64;
MAEEPTSTVT KKYVSAANSQ LGKPTKATST ALTYHTQLMS WFGHLLTGVS AIGAALLSSS
GLGIVQLMES QALSTFFQLR GPIAPPENIV ILAIDNQSIS VPEQYYKTDP QQYAYLEPLK
SFPFKRAAYA DVIRKLMQAG AKSVAVDVIF DTESAYGAAD DRQLQAVLQK YGSKVTLASV
YETSESHQGT FNKLTLPQPM FRIGAVSTGT VNFPLEVDGK IHRLASEFNK SLAQDNLIDK
VPSFDEAALR AARIKYSRPK GDRIHFWGPE GTFEAIPFWY VLDPQNWKNY LQQGKVFKNK
IVVIGATAQL GNDYHPVVAG KNWLYPERMS GVEIHANAIA TLIENKAIAQ GISSPPLQGV
FVLGLVGGVG IICARRKRGI SRLIVSIGFA TLWGGISYVL FVHYQLIYPT TVPMVAIAWI
GLSYLGTEIA RESIKKRQLV DIFQKYKTSP VVQEIISQQQ DLQDLLQQRD LAVAGKILGG
RYRIVKVLGS GGFSETYIAE DLQRPGHPQC VVKQLKPANS KATGLQLARR LFNSEAQTLE
KLGKHHQIPQ LLAYFEQQEE FYLVQEFIIG HPLSKELPAG QSLLETTVIE LLRDLLQTLA
FVHQNGVIHR DIKPSNIIRR HSDWKLVLID FGAVKEVSTI QTENHEQTPF TIGIGTKGYA
PNEQCFGRPQ YSSDIYAVGM IGIRALTGIA PHELARDADG ELQWREHTVA NPALAEILSK
MVLEDYKQRY QSASAALKAV EQLIGVSNRN FIPQHNPIED ITAAIDDPDA PTTPWEV
//
