ID A0A4P1QU70_LUPAN Unreviewed; 930 AA.
AC A0A4P1QU70;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TanjilG_22216 {ECO:0000313|EMBL:OIV95019.1};
OS Lupinus angustifolius (Narrow-leaved blue lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3871 {ECO:0000313|EMBL:OIV95019.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIV95019.1, ECO:0000313|Proteomes:UP000188354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC TISSUE=Whole plant {ECO:0000313|EMBL:OIV95019.1};
RX PubMed=27557478; DOI=10.1111/pbi.12615;
RA Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT an emerging health food: insights into plant-microbe interactions and
RT legume evolution.";
RL Plant Biotechnol. J. 15:318-330(2017).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; CM007377; OIV95019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P1QU70; -.
DR Proteomes; UP000188354; Chromosome LG17.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01335; Radical_SAM; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002902; GNK2.
DR InterPro; IPR038408; GNK2_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27002:SF589; CYSTEINE-RICH RECEPTOR-KINASE-LIKE PROTEIN; 1.
DR PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF01657; Stress-antifung; 2.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51473; GNK2; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000188354};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 522..545
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 124..345
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 280..390
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 394..499
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 585..868
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 614
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 930 AA; 104675 MW; 19F57A3E8AC1329F CRC64;
MGIRSVFDGG EMRIEFEKYG IDTKFIAIIW KHVFLKFNLK EEEEEKDEWD WEKQVPSLPS
AAYSFLDSKF KNKPLSSSLH SVFHSCDNLT TKLLIKLESG AFVEAVIMRY DTRLGRYAGK
PRPGGLRATL CISSQVGCKM GCKFCATGSM GFKTNLSSGE IVEQLVHAST FSQIRNVVFM
GMGEPLNNYS AVIESVRAMT ALPFQLSLKR ITVSTVGIIH AIKKLHNDLP GLNLAVSLHA
PAQDIRCQIM PAARAFPLEK LMDSLQEYQR KSLQKILIEY IMLDGVNDEE QHAHQLGKLL
ETFEVVVNLI PFNSIGTLSQ FKPTSEEKVS NFQKIMRVNG LFLCRGDINT TLCQHCVNNS
STQITKHCPN QTEAVIWYDE CLLRYTNKYF KYYSIQPRVN YQHGNKISDV DFNQSLFLFL
DSLATNAANS MTAKKFATGQ VEVTRSVTVY GLAQCSSTDM ANSQCQICLR NAIGTLPAAQ
QGGAAMLASC VVRYELFPFY NTTGTGTGTG TPYSGGKKIQ SLLVVIMVVL PIVLVILLCS
ACYYVRKRLM KKRRTILIEN FGDEVTAMES LQFSLGTIEA ATNKFSVENK IGRGGFGVVY
KGILSDGRQI AVKKLSTSSG QGSAEFKNEV LLIAKLQHRN LVTLTGFCLE EQEKILIYEY
VPNKSLDYFL FVAYDEYVEE PQKQRVLQWF ERYKIIGGIA QGIHYLHEHS RLKVIHRDLK
PSNVLLDDNM NPKISDFGMA RIVAIDQERG NTNRIVGTYG YMSPEYAMHG QFSEKSDVFS
FGVIVLEIVS AKRNARPIES HDYDDLLSMA WREWRNQTPL EIMDSSLRES FSESEVIRCI
QIGLLCVNEN PEDRPTMSKV VSYLGSLLVE LPIPQETGYC MKQNITTGES SSGWSMLVVK
LDSSVPIHPI NRKCPTSYHG FEMYVILDER
//
