ID A0A2K3DW86_CHLRE Unreviewed; 683 AA. AC A0A2K3DW86; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 29-MAY-2024, entry version 20. DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011}; GN ORFNames=CHLRE_03g159016v5 {ECO:0000313|EMBL:PNW84796.1}; OS Chlamydomonas reinhardtii (Chlamydomonas smithii). OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae; OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas. OX NCBI_TaxID=3055 {ECO:0000313|EMBL:PNW84796.1, ECO:0000313|Proteomes:UP000006906}; RN [1] {ECO:0000313|EMBL:PNW84796.1, ECO:0000313|Proteomes:UP000006906} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906}; RX PubMed=17932292; DOI=10.1126/science.1143609; RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J., RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L., RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H., RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M., RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L., RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H., RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M., RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A., RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L., RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C., RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G., RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L., RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L., RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C., RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J., RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P., RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R., RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P., RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y., RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L., RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.; RT "The Chlamydomonas genome reveals the evolution of key animal and plant RT functions."; RL Science 318:245-250(2007). 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; CM008964; PNW84796.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2K3DW86; -. DR EnsemblPlants; PNW84796; PNW84796; CHLRE_03g159016v5. DR Gramene; PNW84796; PNW84796; CHLRE_03g159016v5. DR OrthoDB; 5474002at2759; -. DR Proteomes; UP000006906; Chromosome 3. DR ExpressionAtlas; A0A2K3DW86; baseline. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:TreeGrafter. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd13999; STKc_MAP3K-like; 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; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR44329:SF214; ANKYRIN REPEAT-CONTAINING PROTEIN KINASE A-RELATED; 1. DR PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1. DR Pfam; PF00069; Pkinase; 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. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000006906}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 44..71 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 399..665 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 1..35 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 81..167 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 202..266 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..17 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 146..167 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 218..244 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 426 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 683 AA; 70157 MW; 22CA776A6785072B CRC64; MAAILAQQQQ QQQPSVPPGF HTPSPGPAGL LDNGSSDAGG GSTAVLVGAI VAGVLGAAAL VGAAGAILWY VRRRSSGAAQ SSLQLDASTG QPKCAVGLDS SSGRGASLQE HAAAQQDGKA SRLADYSEHA TLMSLTDRDG HGSVETAAAT SGNRQDPAGI QAQGSENSNR MLPDLVIHAS PFREGLSTNL VVLVPLRGTP TTAGGGVSLP RTPAAAAPAS VSSASRPSSG ARSFGGSSAA QNGAGGSAPP GIQKEAGGAA AAGQRQARPS SAAAACGAGG SDRGTIYVSA GNEPEITRRA AAYASKVAAM LLHTSSDVDS LLHIAYGSGL RPLAAGTPVA AGAAGMEAAA GAAHSGTAMP VNAEAMAGMR AVGTPAAAVS LLPLPEACEE QNVQVEVVEL LPIKLGRGSF GRVQEGRYRG QRVAVKQALD QHDGLSMPTG KLVASFLQEV EVMGRCDHPN ICKLLAACLA PPKLCLVMEL MDTSLESLIK GQTPGQLLPL PKLLHIAIQV AQGLEYLHPT VLHRDLKPAN VLISNPESGT PIVKLTDFGL SKITEMTLQT ANAEAGTPAY MAPECFDVTN DKLTHKVDMY AFGVILWAML TGEEPWKGYP LVSVAYSVHC GRRLPLDDIP DSRCPRKMRK LVEQCWEPTP RRRPAAAEAV KELLLLREQL LTDGAAPSST EIS //