ID A0A2U1M8J3_ARTAN Unreviewed; 1197 AA.
AC A0A2U1M8J3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=CTI12_AA410620 {ECO:0000313|EMBL:PWA57552.1};
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:PWA57552.1, ECO:0000313|Proteomes:UP000245207};
RN [1] {ECO:0000313|EMBL:PWA57552.1, 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:PWA57552.1};
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 -!- 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:PWA57552.1}.
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DR EMBL; PKPP01006133; PWA57552.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1M8J3; -.
DR STRING; 35608.A0A2U1M8J3; -.
DR Proteomes; UP000245207; Unassembled WGS sequence.
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 CDD; cd06410; PB1_UP2; 1.
DR CDD; cd13999; STKc_MAP3K-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000270; PB1_dom.
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; PTHR23257:SF957; KINASE SUPERFAMILY WITH OCTICOSAPEPTIDE_PHOX_BEM1P DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54277; CAD & PB1 domains; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000245207};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 917..1182
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 948
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1197 AA; 132981 MW; 40DBA81EB5BE88CA CRC64;
MDPSKNDNHV QYNHGQYNSV QPESTDSLPS SQSFQNVNPG PPSVKPVLNY SIRTGEEFAL
EFMRDRVNTR MPYVQYPAGD PSRASGYMEL KGILGISHTG SESGSDISMV NIVERGPSGL
ENHNSSLYET TSNSSRVLEY ASSGASDSAS KIKILCSFGG KILPRPSDGK LRYVGGNTRI
IRIRRDIFWQ ELRQKMLEIY IETYAVKYQL PGEDLDALVS VSSDEDLQNM MEECNVLGIG
EGSQKLRLFL FSLSDLEDTN LTHANSGGDN EFQFVVAVNG MDMGSRRESS MHGLMRSSGN
NLSELDGQNI PISRAATEFV GSNTSPLNLS DLNSSISMPE LSNAYENPNQ MHHIEPSYNI
QQHLAPETSV PLNPNGFVDR QGEFTEGHPY RAPVMQNRHL QNPNGLVDRQ GDFTEGHPSR
APVMQNRQPQ NPNGLVDRQG EFTEVHPSRA PVMQNRQPQN PNGLVDRQGE FTEGQPSRAP
VMQNRQPQNP NGLVDRQGDF TEGHPSRAPV MQNRQPQKEE KPKGDNSAQQ EVKQTNIRSP
RDDVASSTLP SEGKLPPKPK MNEERHQEHI QSKVVASNDN DSVTSSSAAA PDNSGSDLID
LSYLEPPPRV YHSEIIPRGQ VEKNRLTKSD DSLGSQLLAS HLQSDVEPHD YFSESVGNLH
NENLPAEDRT AVKNDQVPEA ANTSDVKMKN DKKVKFDKSA ETGSQKMHHP YPAPNSQAAT
GVTGGGVKVQ EEILIDINDR FPSNFLSDVF TRAMAEDGPG MGVLPQDGVG MSMNIANHEP
KHWSFFQKLA GDEFRQKDVS LIDQDHLAYL SRLQNVQEEV SVGYNASQFP DDVDSRNTYV
EDEGKEIPGS ESTSMQPHYN PSHKSIEGMQ FDDPSENTRM PDSEYEVSAR NDGLPSVDSS
LGDLDISSLQ IIRNEDLEEL RELGSGTFGT VYHGKWRGTD VAIKRIKKSC FAGRSSEQER
LTIEFWREAD ILSKLHHPNV MAFYGVVQDG PDGTLATVTE FMVDGSLRHV LLRKDRHLDH
RKRLIIAMDA AFGMEYLHSK NIVHFDLKCD NLLVNMKDSS RPICKVGDFG LSKIKRNTLV
SGGVRGTLPW MAPELLNGGS NKVSEKVDVF SFGIVLWEIL TREEPYANMH YGAIIGGIVN
NTLRPTIPSD CDPEWRRLME LCWSPDPAVR PSFTEITNQL RVMSAACQSK GHAHKAT
//
