ID A0A2K3E1A8_CHLRE Unreviewed; 2639 AA.
AC A0A2K3E1A8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=CHLRE_02g090700v5 {ECO:0000313|EMBL:PNW86537.1};
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:PNW86537.1, ECO:0000313|Proteomes:UP000006906};
RN [1] {ECO:0000313|EMBL:PNW86537.1, 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; CM008963; PNW86537.1; -; Genomic_DNA.
DR STRING; 3055.A0A2K3E1A8; -.
DR PaxDb; 3055-EDP06947; -.
DR EnsemblPlants; PNW86537; PNW86537; CHLRE_02g090700v5.
DR Gramene; PNW86537; PNW86537; CHLRE_02g090700v5.
DR InParanoid; A0A2K3E1A8; -.
DR OrthoDB; 316695at2759; -.
DR Proteomes; UP000006906; Chromosome 2.
DR ExpressionAtlas; A0A2K3E1A8; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR23257:SF703; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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 Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1221..1245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2330..2597
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 96..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1442..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1508..1534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1637..1663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1703..1779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1878..1930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1957..1977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2075..2124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2247..2311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2601..2639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..189
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1060
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1744..1760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1878..1897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2093..2114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2281..2305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2606..2629
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2639 AA; 255142 MW; 8C208A61349FFEE9 CRC64;
MWRSAFPSQW QASHTQPAIA LRQHHTHTII TRLDDLSHLR SPPVKYRHSP SFCCRVGPAS
ARSRRLDPPS LESPPLLQTR RALLCAAASL STSVIDLSSS SSSSTSSSSS SSSTSSGRGA
PSSAAASEAA RAHQSQMTSS TAATRAEADP AETVVVTAAT TAADATWAHR QRVGSELRQR
RHPHHHHCKI GRDAACGDSR GSRHTRSIDT SSGSGSGSGV LFLQGCIIKQ QVSAAAAAAV
GPRLVALLAA PQLPAGTGGV CTVRRGQRAR RYLALVLMLA LMLATGCAVG TMPPSRAAAA
AAATAAADAN GMDDISTAVG PAAARPHGGG LLSQPFVARV AAPGAGGAVA TSSSALLPDA
AGGASEEGEQ MAEEAHAPHH HNNNNNSPRH SQQAQHASMG AQQAAAAVAP HGSQATEEAA
AEASSSGSSA SAEHMRRRGL QGAAGSSSNI WRAHGVAGAG KGQGPQIAGR NSASSGVQHQ
QHRRNLQNQQ PPGKPKTKSA GGGSSSSSGN NSGAAAGGDS GNAGGVGPAA AVAPRCSAAA
PLQLPAAFRQ QQGLQSCPLV VGYLVKQGTA RTDPAAAAAA IAASIQSAGG AAGGGGGGDG
SAGGGGGGSA RRLHGVDDSG TKGSGGGDGG GGGGGGGGDG SGGDAGPAGG SGADMGGSGS
QAGGGEGDDD SPLCATAAII NNGRAVMYGW QLVWRFADPR AFSAGDVRGA VLVTGGDGSP
VRVVNSAEAA TIPAAGGAAN FSLALAPNTS AGPGWRRADT LEWSAVFVNG QRCVQLPSSS
LGLPGCGLPY SQLAADPAAA DPVLDPAGMD PGESAINTST RPSFPPQAMA PPPPPSDLAC
ASVFCCGDLD GGGEPEAASG TGGSSTYGSG ISSGSAGGGG PATAETAPPP PPAPDAITAL
STALTQLTRM VAALTPAPPL PPGGGGSSSS SSSGSSTGGG SSSPVLTPDV VARLHELLTA
AAAGADVSVD LLATLQEIAQ QGGFNAYDSK SLSNPGGGGG LTVNTTVNAS SGSSGATNLT
AVLQQLRDAI TARQAALQPP PPPPAPPLTP PPPPPAAASL PSPSVGASDG PPDAGMAPGG
VGGSGSDGAA GGGHNDGGPA HSDGSGGGDG GGDPSSTSAA PGVGGGGASS AAQAVIPKPL
PRPDITPPTS SQQADGKDTP DSSGGGGSAD AAATAAAATV AAVAAAAAAP AAAAGGDSSG
GGGGGEGQAV SRPGRKSGGG VIVGGSAAAG ALVLLAVALT ATLMFRRRRR LQQQHLLKQQ
QQQRVMAEGG CKPPTATATG NADGNDGDGN GATTAIYAAA AGTAAAASRC LARTGSGTSA
TGEQTWRRDP LLPVPPSAFA SRRQPVLDGI VELESPVQAA NAGATPAAAN GGFSKGADRG
GGGSIVGGGG IGVSGVVVGV GGGGQALRRA SGASGSGSSA VVREVDVRRS CSPPLSLSSL
QWHKAKRVDS GGRPQPPQSH MAGGGALVAE SRGPPVLLPS QGSLGQYGFG GGNGGVGGGG
VLGEVRSAGC SSGGGGSRGR SSGGGGGVTG GGGGGGATGS VVQVLLASSS SLPQMLMAPP
PPAATAAAGT AGGAYGSGVA YRVDAWPGGG GGSGLAAAVA AAQVPSLHPL QRALYGPSAG
SWPPRWLVPA GGVGSMGAGN SSSSGSGGGG SGGGSGAAAA AAGGPAGGVH GLTLGALLGV
RRMPYMTTAA AAGPSCRPKA QRVAAAGAAV AHGEDEEGEE EDGHDQEGEE VAGARGGVAT
GGRGSGSGSG SGSGSGWTAV PSASPAVCLD EGDGEAESDA LPQHLSGISA GGTGGAGVST
GAAAAVAAAG SGPAGAVQKL SPSRMWQSHQ HHQQHHQQHQ QHQRPLLPLL PRHATHAAFL
GRARSDAAAL VPPHTLYHPA ASTSNSTTTT TTAVGPGLPS AGASAGASPG THSLGGRNPH
VRPHAAVSSS ASGRPAAAAA VAAGAGRLLP STAAAATASR ADGRCNGGGG RLQPSRSSPA
QLLGRLALLA ATSSVGVVGS LAGAADGVAA PAATAATRRS RPQSHTPDAD MHTGADVAAE
AEAETDVAAE AAEAAEVEAV EAAERGTCRR MAPRPALLEG LGPPESASEA AAASTGLHAQ
SPATWQQGQS RLSPPQPAAA FAPSTSARYS VGAASTLGGG GGSTRVGATA TAAAGGCGSS
STRDAMAVSL APTSLFSASV LSSGSYATSS IAAAAATAAS RRPPVAAEVA AAAATGSPPM
KAAVAGVQQP AAAAAVAGPQ GAAAAAGAAS GARPRDSPRG LAAPAATTAK AARSSAAAGA
AMPPNPPPST SPTAPTVPTV PTTPAAAAPT PHGLPAAAAS WVAIDFARDV VLQRRLGSGA
HGTVYQGLWV GRPVAVKVVP LLDGDGGAVC PQALESIRQE VQVLSRLSHP HIVQFFGACL
APPHVCIVEE LAAAGSLHHR LHARRRGSSV KLHPAMSYGE VLQLGLDVSS AMCYLHPHVV
HRDLKPQNVL LDGSGRAKVC DFGIAKIKDR TLLSTRNAHA GTPAYMAPEQ FEGRPVSEKV
DVYAFAMTLY ECLTGEQPWR DLQNPMQVIF VVGVQCQRPP LPPACPAGLA DLVCACWADS
PEERPTFAAV VERLRRLQAE AVEAEAEGEE GKEGEEGEEG EEGEEGEEGE AGGLGCRRE
//
