ID A0A1J6IUH1_NICAT Unreviewed; 792 AA.
AC A0A1J6IUH1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=CCR4 {ECO:0000313|EMBL:OIT04240.1};
GN ORFNames=A4A49_13677 {ECO:0000313|EMBL:OIT04240.1};
OS Nicotiana attenuata (Coyote 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=49451 {ECO:0000313|EMBL:OIT04240.1, ECO:0000313|Proteomes:UP000187609};
RN [1] {ECO:0000313|EMBL:OIT04240.1, ECO:0000313|Proteomes:UP000187609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UT {ECO:0000313|Proteomes:UP000187609};
RC TISSUE=Leaves {ECO:0000313|EMBL:OIT04240.1};
RA Xu S., Brockmoeller T., Gaquerel E., Navarro A., Kuhl H., Gase K., Ling Z.,
RA Zhou W., Kreitzer C., Stanke M., Tang H., Lyons E., Pandey P., Pandey S.P.,
RA Timmermann B., Baldwin I.T.;
RT "The genome of Nicotiana attenuata.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:OIT04240.1}.
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DR EMBL; MJEQ01037185; OIT04240.1; -; Genomic_DNA.
DR RefSeq; XP_019242944.1; XM_019387399.1.
DR AlphaFoldDB; A0A1J6IUH1; -.
DR STRING; 49451.A0A1J6IUH1; -.
DR EnsemblPlants; OIT04240; OIT04240; A4A49_13677.
DR GeneID; 109223189; -.
DR Gramene; OIT04240; OIT04240; A4A49_13677.
DR KEGG; nau:109223189; -.
DR OMA; NSHVCGL; -.
DR OrthoDB; 404991at2759; -.
DR Proteomes; UP000187609; Chromosome 3.
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:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
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; 1.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46146; SERINE/THREONINE-PROTEIN KINASE-LIKE PROTEIN CCR4; 1.
DR PANTHER; PTHR46146:SF4; SERINE_THREONINE-PROTEIN KINASE-LIKE PROTEIN CCR4; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13540; RCC1_2; 2.
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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OIT04240.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000187609};
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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..792
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013380730"
FT TRANSMEM 387..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 484..782
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 351..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 792 AA; 86916 MW; 62D5E6497B3BBBE0 CRC64;
MAILDQKTHL FFSLVFLCFL ISFSPISSLS TVSISKTSNQ TLICALISSS SSFPQQSSLN
CTSFPQGIQI PLNPSVSFSG IVGGNGFLCG LTSSYSSSTS IMVCWRFSNN GTNLSYKRIY
LGPLITNLDS GNSHICGIVN NRLECWQWHE FNSSNRSLMS SNLAVGEDFV CGLLEFGEIQ
CLGSFRNVTD AIPSGNYSEI ASGSQHVCAI SKNNSLICWG NMVGEKPIGQ FKSLALGDNR
SCALRINGTV VCWGETGFSL PSSLSEEFFE TLEAKQDIFC GIVTSNYSLF CWGNDIFNSN
PVVFNGVQVV PGPCTTSCPC VPLPNYETFC GEGLMICTHC VWQESGVNPP IVNGSGPAPP
PLPPQPMPPS TPSQTSGRSD PWSRRNVAFL VVGCIGSLMM LSVLVILFFK YCKIRGCRVH
DSGRLDEAGS PPQQGSQTSG VQDQQGTPQP PVLKKRLSQL ISIGNGGHLE EFSLQVLLQV
TKNFSDEHKI GSGSFGSVYH ARLEDGREVA IKRAEASASS SYAGGTKYRQ EDKDNAFLNE
LEFLSRLNHK NLVRLLGYCE DNNERVLIFE YMNNGTLHDH LHRLESSPLM SWPGRIKVAL
DAARGIEYLH EYAVPPVIHR DIKSSNILLD ATWNAKVSDF GLSLMGPQDD ETHLSMRAAG
TVGYMDPEYY RLQQLTTKSD VYSFGVMLLE LLSGYKAIHK NENRVPRNVV DFVVPYIVQD
EIHRVLDHRV PPPTPFEIES VAYVGYLAAD CTTLEGRDRP TMTQVVNTLE RALKACLATP
IFSRSNTDDS ST
//
