ID A0A251SMJ5_HELAN Unreviewed; 1080 AA.
AC A0A251SMJ5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Putative bulb-type lectin domain-containing protein {ECO:0000313|EMBL:OTG00065.1};
GN ORFNames=HannXRQ_Chr13g0386821 {ECO:0000313|EMBL:OTG00065.1};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG00065.1, ECO:0000313|Proteomes:UP000215914};
RN [1] {ECO:0000313|Proteomes:UP000215914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RX PubMed=28538728; DOI=10.1038/nature22380;
RA Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA Vincourt P., Rieseberg L.H., Langlade N.B.;
RT "The sunflower genome provides insights into oil metabolism, flowering and
RT Asterid evolution.";
RL Nature 546:148-152(2017).
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DR EMBL; CM007902; OTG00065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251SMJ5; -.
DR InParanoid; A0A251SMJ5; -.
DR OMA; PWITSED; -.
DR Proteomes; UP000215914; Chromosome 13.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00028; B_lectin; 1.
DR CDD; cd01098; PAN_AP_plant; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47976; G-TYPE LECTIN S-RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD2-5; 1.
DR PANTHER; PTHR47976:SF30; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF01453; B_lectin; 2.
DR Pfam; PF08276; PAN_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00108; B_lectin; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50927; BULB_LECTIN; 2.
DR PROSITE; PS50948; PAN; 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}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lectin {ECO:0000313|EMBL:OTG00065.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000215914};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1080
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012670952"
FT TRANSMEM 713..736
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..162
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 296..426
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 616..694
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 769..1053
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 797
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1080 AA; 121638 MW; D4136E3D98B97F5E CRC64;
MRKLRICSFL FAIFLVLVFS PAAESYSATA DLSTTWTTNY SAVNPILRRE SNVAVFTCGF
FCEDNCTSYY FAIFISPTTE SPGQYKHVWS AKKNYDYLNP THRENPILNF TAAGDLVLED
VDGFIYWKTD TAGKSVAGMN LTDTGNLVLF DHRNSVVWQS FDDPTDSLLP GQKLFQGQEL
QSRDGASSLQ LTDKGLFGYA YYNELYYRWL VYGKGTNKGR RYMKFSNGSL SICIEYSSEP
SDPVGVIGIP EASSAQYMKL MPDGHLQVFE WQLEEWKVIK DLTTLFQSYS YTANLSTTWN
TNYSYAQPIL FTETNGTQFA CGFLCEGNCT NGKSLHHIFA VFIYPTTYHK AYKVVWSANR
DYPVRENSIL NFTSAGDLVL KDGDGSIVWT TNTAGKSGLF AGMNLTDTGN LVLFDNQNSV
VWQSFDHPTD SLLPGQKLYQ GQKLKSSVSL SNSSGQEGMY SIGITDIGLF AYVESNPPQA
FYRMLVYPNG NDTHKGRRYI RFLNGSLSLF IRSSEPSDPD VSVYIPTASS VQYMKLMSDG
HLKVFEYQSG GWIEVADLLN VGNCSYPLTC GRNSICLAGQ QQCSPPLCSC AGREHFRPVN
DRQPNLGCSE ITPLTCNSTQ DQDLITLENV KYFTSTADME GVNMETCKQA CRKNCSCKAA
FYQYYSHVSS GDCFLLSELF TMKTVDPLYY NASAFIKVQY ATSHRLPHQV ARLVGYIVGS
FVLLLVVALG VVYVFYKRKR DIEMEEENLD QLPGMPNRYS YEELKTATEN FSKKLGEGGF
GMVFEGTLRD GTKIAVKCLE GLAHVKKSFL AEVQSIGSIH HVNLVRLRGF CTWKSQRFLV
YDFMSNGSLD SWIYLGVRKC VLEWECRKKI VLDIAKGLAY LHEECRQKIV HLDIKPQNIL
LDSDFSAKVS DFGLSKLIDK NQTEVMTNIK GTPGYLAPEW RSSIITEKVD VYSYGIVLLE
ILCGRKVLDR SQPEESGHLL FVFEKSWEQG TLLEMVDRQS EDMRVHSTEV VEMMKVAAWC
LQTNFKRRPS MSSVVKVLEG GMGVESKLDY NFIDPIIQET EDGDGKYFTQ LSAYLLSGPR
//
