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Database: UniProt
Entry: A0A0D3DXZ4_BRAOL
LinkDB: A0A0D3DXZ4_BRAOL
Original site: A0A0D3DXZ4_BRAOL 
ID   A0A0D3DXZ4_BRAOL        Unreviewed;       829 AA.
AC   A0A0D3DXZ4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo8g108940.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo8g108940.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo8g108940.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000641};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|PIRNR:PIRNR000641};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
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DR   AlphaFoldDB; A0A0D3DXZ4; -.
DR   EnsemblPlants; Bo8g108940.1; Bo8g108940.1; Bo8g108940.
DR   Gramene; Bo8g108940.1; Bo8g108940.1; Bo8g108940.
DR   eggNOG; ENOG502QSUU; Eukaryota.
DR   HOGENOM; CLU_000288_116_5_1; -.
DR   OMA; GANEQDC; -.
DR   Proteomes; UP000032141; Chromosome C8.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0060320; P:rejection of self pollen; IEA:UniProtKB-KW.
DR   CDD; cd00028; B_lectin; 1.
DR   CDD; cd01098; PAN_AP_plant; 1.
DR   Gene3D; 2.90.10.10; Bulb-type lectin domain; 1.
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; IPR021820; S-locus_recpt_kinase_C.
DR   InterPro; IPR000858; S_locus_glycoprot_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR024171; SRK-like_kinase.
DR   PANTHER; PTHR32444; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR32444:SF219; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF11883; DUF3403; 1.
DR   Pfam; PF08276; PAN_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00954; S_locus_glycop; 1.
DR   PIRSF; PIRSF000641; SRK; 1.
DR   SMART; SM00108; B_lectin; 1.
DR   SMART; SM00473; PAN_AP; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50927; BULB_LECTIN; 1.
DR   PROSITE; PS50948; PAN; 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|PIRNR:PIRNR000641};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000641}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000641};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW   Self-incompatibility {ECO:0000256|ARBA:ARBA00022471};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|PIRNR:PIRNR000641};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000641};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..829
FT                   /note="Receptor-like serine/threonine-protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002270678"
FT   TRANSMEM        443..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          28..153
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          348..433
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          522..797
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   829 AA;  92625 MW;  1DB1746F6E5B015A CRC64;
     MIVIPNIRIL LFVLATVSCF SLKLCFGEDR ITFSTPIKDS ETLLSKSGVF RFGFFSPVNS
     TGLLRYVGIW YDKVPVQTVV WVANKDTPIN NTSGVISISD DGNLVVTDGR NRLVWSTNVT
     VTVASNATWV QLMDNGNLRL QDNRNNVETL WESFKHPYNS FLPRMTLGTS TKTGENLKLT
     SWRSYVDPST GSYTAGLASF TFPELMFPEL LIWNKNVPIW RSGPWNGQVF IGLPDVDSLL
     FLDGFNLIND NQGTFSMSFA NDSFMYHFNL DPDGAIYQRD WSARGWRIGV RFPSTGCDAF
     GRCGPYGICN SREDPTCKCV KGFVPRNSTE WNARNWSNGC VRRVSLQCER QRNVSNGGGG
     KGDGFLKLQK MKVPIIAEQS LANVQACPKV CSDNCSCTAY AYDRGIGCML WSGELVDMQS
     FLGSGIDLYV RVAHSELKTH SKLAVMITAP VLGVVFVAAF CVLLACRRFK KRPAPEKDRS
     AELLYKRMEE LTSGNESASN QVKLKDLPLF EFKVLATSTD SFSPGNKLGQ GGFGPVYKGI
     LPEGQEIAVK RLSRASGQGL EELMNEVVVI SKLQHRNLVK LLGCCIEGEE RLLVYEYMPK
     KSLDAYLFDP LKQKILDWRT RFNIMEGICR GLLYLHRDLK ASNILLDDNL NPKISDFGLA
     RVFQVNEDEA NTTRVVGTYG YMSPEYAMEG FFSEKSDVFS LGVIFLEIIS GRKNSHKEDN
     NLNLLAYAWK LWNDGEASSL ANSIVFDECF EKEITKCVQI GLLCVQEFAN DRPNVSTVIW
     MLTTENTNLP EPKQPAFIAR RGFSIAESSD QSSQKVSIND VSLTAVTGR
//
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