ID A0A388LRM9_CHABU Unreviewed; 675 AA.
AC A0A388LRM9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CBR_g39450 {ECO:0000313|EMBL:GBG84986.1};
OS Chara braunii (Braun's stonewort).
OC Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae;
OC Chara.
OX NCBI_TaxID=69332 {ECO:0000313|EMBL:GBG84986.1, ECO:0000313|Proteomes:UP000265515};
RN [1] {ECO:0000313|EMBL:GBG84986.1, ECO:0000313|Proteomes:UP000265515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S276 {ECO:0000313|EMBL:GBG84986.1,
RC ECO:0000313|Proteomes:UP000265515};
RX PubMed=30007417; DOI=10.1016/j.cell.2018.06.033;
RA Nishiyama T., Sakayama H., Vries J.D., Buschmann H., Saint-Marcoux D.,
RA Ullrich K.K., Haas F.B., Vanderstraeten L., Becker D., Lang D.,
RA Vosolsobe S., Rombauts S., Wilhelmsson P.K.I., Janitza P., Kern R.,
RA Heyl A., Rumpler F., Villalobos L.I.A.C., Clay J.M., Skokan R., Toyoda A.,
RA Suzuki Y., Kagoshima H., Schijlen E., Tajeshwar N., Catarino B.,
RA Hetherington A.J., Saltykova A., Bonnot C., Breuninger H., Symeonidi A.,
RA Radhakrishnan G.V., Van Nieuwerburgh F., Deforce D., Chang C., Karol K.G.,
RA Hedrich R., Ulvskov P., Glockner G., Delwiche C.F., Petrasek J.,
RA Van de Peer Y., Friml J., Beilby M., Dolan L., Kohara Y., Sugano S.,
RA Fujiyama A., Delaux P.-M., Quint M., TheiBen G., Hagemann M., Harholt J.,
RA Dunand C., Zachgo S., Langdale J., Maumus F., Straeten D.V.D., Gould S.B.,
RA Rensing S.A.;
RT "The Chara Genome: Secondary Complexity and Implications for Plant
RT Terrestrialization.";
RL Cell 174:448-464(2018).
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:GBG84986.1}.
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DR EMBL; BFEA01000500; GBG84986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A388LRM9; -.
DR STRING; 69332.A0A388LRM9; -.
DR EnsemblPlants; GBG84986; GBG84986; CBR_g39450.
DR Gramene; GBG84986; GBG84986; CBR_g39450.
DR Proteomes; UP000265515; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblPlants.
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 GO; GO:0009409; P:response to cold; IEA:EnsemblPlants.
DR GO; GO:0009408; P:response to heat; IEA:EnsemblPlants.
DR GO; GO:0009651; P:response to salt stress; IEA:EnsemblPlants.
DR CDD; cd05123; STKc_AGC; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045270; STKc_AGC.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000265515};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 329..586
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 587..655
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 16..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 675 AA; 73218 MW; 89592A3271649057 CRC64;
MAKPILPVGT TVAVDIPLGS AGAGAGRGAK KTLQPLRRSH PSLERPGGGG GVLGNQQHTS
SDADEDGSSS GNVDSRGIGE EFCFEDLFGP LPSPRVDQRA ANDSIATCKG RIAPQISSPS
HHLESVVEGE DSVSWAKCSL DREVPPTPLA AMHVNELSSS WTGSAPVTLR RSHSLVGPSH
AEPSPKCSSY GGGAVGRNPF GGPQSLTKGG ERCGEEVCDE GKNHHHHHHH CGDGIVVNGA
KPVVEGRERR EEMEREAGYG QNGVEATVGG DESEEEVRGD HSRERLVPAA EAGENGLHTS
DEAIRPAANG VRNGEVQNGE SKKIGPQDFE ILRVVGQGSF GKVFQVQRKA TGEIMAMKVM
RKEKIVEKNH EEYMKAERDI LTSVVHPFIV QLKCSFQTKS KLYLLLEFIN GGHLFFQLDR
QGMFSEDLAR IYTAEIVLAL SHLHQQDIIH RDLKPENILL DADGHVKITD FGLAKANVSS
MVASNSICGT MEYMAPEIIL AKGHGKAADW WSVGILMFEM VTGMPPYLSN NRQKLQAKIV
KDKVKLPSYL TSQCHSLLKG LLQKEPAKRL GSGPRGSEEI KGHPFFKGIN WKKLEAKEIQ
PGFRPNVADK RCTANFDEMW TKLPPNDSPA GTPKKSSEVF RGYTFVASKN WTPSGYDSDT
ESGHSSGEED SPFSE
//
