ID A0A2U1MVC6_ARTAN Unreviewed; 1012 AA.
AC A0A2U1MVC6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=CTI12_AA336260 {ECO:0000313|EMBL:PWA65190.1};
OS Artemisia annua (Sweet wormwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Artemisiinae; Artemisia.
OX NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA65190.1, ECO:0000313|Proteomes:UP000245207};
RN [1] {ECO:0000313|EMBL:PWA65190.1, ECO:0000313|Proteomes:UP000245207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC TISSUE=Leaf {ECO:0000313|EMBL:PWA65190.1};
RX PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT "The genome of Artemisia annua provides insight into the evolution of
RT Asteraceae family and artemisinin biosynthesis.";
RL Mol. Plant 11:776-788(2018).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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:PWA65190.1}.
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; PKPP01004271; PWA65190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1MVC6; -.
DR STRING; 35608.A0A2U1MVC6; -.
DR Proteomes; UP000245207; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0006952; P:defense response; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
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; PTHR27008:SF616; OS02G0211800 PROTEIN; 1.
DR PANTHER; PTHR27008; OS04G0122200 PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 5.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS51450; LRR; 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|EMBL:PWA65190.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000245207};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 656..680
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 718..1012
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 748
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1012 AA; 110834 MW; 16E6339CB8216AA3 CRC64;
MKSPQAIIYL SSFTRISIIF YGLAIICLTS TTVFASNGGN ETDYLALLSF KSKITQDPYK
VLTSWNHSFH FCDWSGISCG KRHKRVTAVQ LSSKGLKGSL SPHVGNLSFL RHLSLWNNSF
QGTIPHELGR LSRLRILYLY ENKFSGVIPA NLSGCSNLEI LWLAQNNLSG SIPKEMSLLL
KLADLVIHTN KLTGGIPPFL GNITSMEVFS AEGNPLGGSI PDTVGLWKSL TGFYCGGCNL
YGQIPPSIFN LSLLVTFSLP ENHLTGSLPT KMGNQLQNLE LLQLSGNKLT GILPPSISNC
SKLGYLEMSI NDFSGKLTID FSKLRNIYKI NLQHNNFHGR GEADDTRFID SLKNCTRLVT
LNLYNCNLIG VLPISIGNLS DQLNHLILAE NQLFGSLPSS IGSLVGLTYV DLGPNLFKGK
IPATIGKLQR LQILDLSRNQ FSGPIPNAIG NLSLLTELYL DINKLEGHIP SNLGNCTKLN
GLELANNRLS GKIPNQILQL PSLNYFLDLS YNGLSGSIPS EIKDLKMLSH LDLSYNNLSG
IITSSLGECI SLTTLNLRGN QFQGTIPSSL SSLGGLGVLD ISQNNLSGKI PQFLEKWKSL
EYLNLSFNDF EGDVPAVGVF ANASAFSVLG NNRLCGGLDM LELPKCKETG SKKKRFPLFV
LLILIAPALL VVLYCVHLFC KKKRNSQQSQ SSGNEQSSGN ERLLKVSYNQ LIKATDGFSI
ANLIGEGGFS SVYKGILDSN GDKYVAVKVL NLQNRGAHKS FLAECEAWRN IRHRNLLKII
TSCSSVDFQG NDFKALVYEF MPNGSVHDWL HSSAKRLKLN LVQRINILRD VATALDYLHN
RSQTTIVHGD LKPSNILLDD DMVAHVGDFG LARLLGADLN QNSSTGVKGT IGYTPPEYGI
GSAMTSIGDV YSFGILLLEV MTGKKPTDDM FNDGLSLHKF AYMALPDHVI GVIDRDAIVL
QSMEANAKKV EECLVATIKI GVSCSVDSPQ QRMQIEFVVN ELQRILDVLH HI
//
