ID A0A1S3XD33_TOBAC Unreviewed; 767 AA.
AC A0A1S3XD33;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=LOC107763853 {ECO:0000313|RefSeq:XP_016437845.1};
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_016437845.1};
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_016437845.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00206}.
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 RefSeq; XP_016437845.1; XM_016582359.1.
DR AlphaFoldDB; A0A1S3XD33; -.
DR SMR; A0A1S3XD33; -.
DR STRING; 4097.A0A1S3XD33; -.
DR PaxDb; 4097-A0A1S3XD33; -.
DR GeneID; 107763853; -.
DR KEGG; nta:107763853; -.
DR OMA; VDCWDIV; -.
DR OrthoDB; 1205577at2759; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:UniProt.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR044815; CCR1-4.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR PANTHER; PTHR46146:SF20; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46146; SERINE/THREONINE-PROTEIN KINASE-LIKE PROTEIN CCR4; 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 SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50050; TNFR_NGFR_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00206};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_016437845.1};
KW Membrane {ECO:0000256|SAM:Phobius};
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 Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..767
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010277480"
FT TRANSMEM 429..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 340..395
FT /note="TNFR-Cys"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT DOMAIN 340..395
FT /note="TNFR-Cys"
FT /evidence="ECO:0000259|PROSITE:PS50050"
FT DOMAIN 511..761
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 539
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 377..395
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
SQ SEQUENCE 767 AA; 83076 MW; 4F066F0BAEE2DF46 CRC64;
MNTLFNLSFF HLLPFILFLK SASGFGSMGP ISAAFGKNGF FCAIDASGKQ DVICWGNKTN
SSAAVPNSSS DVPPMAALSG GDGFLCGILA NTSQAFCWDS LGSRSDLVPT LFKSNAYSHI
AAGRSHVCAI RGPYYSESDW GSVDCWDIIR KSNDNDTFIS RESSLFYNQY TNSAAFKKIV
SGDGFSCGGV RDGGIFCWGP NSSGLGISSI SENVHVLTAG IDSVCGVLEE SNEVKCWGGN
NASFGSPPVG VPFVSLAAGV HHFCGIRKDN HGIQCWGNYN SSLIPKGSGF LAIASSDFIT
CGIRESDLVL DCWYTNVSSQ VDYDPPLQLC SPGLCTPTSS CGEGKFSFNA SLLNEPDLIN
LCVRKDLKIC SPCGANCSEG FFPSSSCTEN ADRVCTPCSL CQNSSCSDVC RLQNSEMMKH
QHQHQLRQLL LIVGSSALGF LLCLVGLCLL IRMIGSRTKQ GGKNQFASCI RKPEKETDAN
TDPHPPVSVS PCPGEAQVFR LSELKDATNG FKEFNELGRG SYGFVYKAVL ADGRQVAVKR
ANAATIIHTN SREFEMELEI LCSVRHSSIV NLLGYCAEMG EQILVYELMP HGTLHDHLHG
GLSPLSWNLR LKIAMQAAKG LEYLHKEVSP PIVHRDVKSS NILLDADWGA RIADFGLLTP
NEKDLNGDVT TDVYNFGIVL LEILSGRKAY DRDCTPPSII DWALPLIRQG KAAVIIDRYV
ALPRNVEPLL KLAEIAEQAL RENPAERPDM SQLALLLEQL VKDVMIS
//
