ID A0A1S3ZU63_TOBAC Unreviewed; 668 AA.
AC A0A1S3ZU63;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Probable serine/threonine-protein kinase At1g54610 {ECO:0000313|RefSeq:XP_016467950.1};
GN Name=LOC107790533 {ECO:0000313|RefSeq:XP_016467950.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016467950.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016467950.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily.
CC {ECO:0000256|ARBA:ARBA00006485}.
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DR RefSeq; XP_016467950.1; XM_016612464.1.
DR AlphaFoldDB; A0A1S3ZU63; -.
DR SMR; A0A1S3ZU63; -.
DR STRING; 4097.A0A1S3ZU63; -.
DR PaxDb; 4097-A0A1S3ZU63; -.
DR GeneID; 107790533; -.
DR KEGG; nta:107790533; -.
DR OMA; PKQPYDS; -.
DR OrthoDB; 10753at2759; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07840; STKc_CDK9_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; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR PANTHER; PTHR24056:SF188; CYCLIN-DEPENDENT KINASE C-2 C; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_016467950.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000084051};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 125..409
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 668 AA; 74956 MW; F6217EE5E6DFAF62 CRC64;
MGCVSSKQAT SHSPVHDSSS VTVVDNGDHL LHIKAAGFAP LEKIKEEPDK EGEDNSVHRS
RFSGNLRRAS SSSKKGANSE KRATFSIKFG RLNEGEHLAA GWPAWLTAVA GEAIEGWVPL
RSNMFQKLEK IGQGTYSSVY RARDIESGKM VALKKVRFDN FQPDSVRFMA REIAILRKLD
HPNIMKLEGI ITSRLSCSIY LVFEYMEHDL SGLLSCPDIK FTDSQIKCYM QQLLSGLEHC
HSRGIMHRDI KVSNILVNNE GILKIADFGL ANFLSSRHKQ PLTSRVVTLW YRPPELLLGS
TNYGVTVDLW SVGCVFAELF FGRPLLKGRT EVEQLHKIFK LCGTPPDDYW KKSKLPLATM
FKPKQPYDST LRDRCKELPK TAVNLIETLL SIDPYKRGTA SSALNSEYFN TKPYACDPSS
LPKYPPNKEI DAKFREEARR KRASSTAQAS ETSRKSRKAL QEPSSFCKVV PSEEVEANVH
GSRRNHGGSV HISKGRRATV SRISMKPLYD TVSEVSQMTD ESQGDSTILS VSVQMPESSG
FAWAKRGKQD SATTRLYPPA NSTSQKLSTV DPSGVLHAED TWDSNMQDNY ELLSRAHTVK
HSIHRQHGHH ERSDSFDSSD QEPSVDYNGQ QGRVAYSGPL LYQSQKFDTK QDSQSRKAGH
RSRFYRDL
//
