UniProt: W9SEU6

Database: UniProt
Entry: W9SEU6_9ROSA

LinkDB:  W9SEU6_9ROSA 
Original site:  W9SEU6_9ROSA

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (22)   
   InterPro (10)   
   Pfam (4)   
   PROSITE (5)   
   SMART (3)   
All databases (34)   

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ID   W9SEU6_9ROSA            Unreviewed;       845 AA.
AC   W9SEU6;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641};
GN   ORFNames=L484_005004 {ECO:0000313|EMBL:EXC29551.1};
OS   Morus notabilis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX   NCBI_TaxID=981085 {ECO:0000313|EMBL:EXC29551.1, ECO:0000313|Proteomes:UP000030645};
RN   [1] {ECO:0000313|Proteomes:UP000030645}
RP   NUCLEOTIDE SEQUENCE.
RA   He N., Zhao S.;
RT   "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
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DR   EMBL; KE346192; EXC29551.1; -; Genomic_DNA.
DR   RefSeq; XP_010111023.1; XM_010112721.1.
DR   AlphaFoldDB; W9SEU6; -.
DR   STRING; 981085.W9SEU6; -.
DR   GeneID; 21388489; -.
DR   KEGG; mnt:21388489; -.
DR   eggNOG; ENOG502QUDG; Eukaryota.
DR   OrthoDB; 1218926at2759; -.
DR   Proteomes; UP000030645; 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:0030246; F:carbohydrate 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:0048544; P:recognition of pollen; IEA:InterPro.
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; 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; IPR017441; Protein_kinase_ATP_BS.
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:SF63; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF01453; B_lectin; 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; 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|PIRNR:PIRNR000641};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000641};
KW   Lectin {ECO:0000313|EMBL:EXC29551.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000641}; Receptor {ECO:0000313|EMBL:EXC29551.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030645};
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|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000641};
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..845
FT                   /note="Receptor-like serine/threonine-protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004931983"
FT   TRANSMEM        459..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          28..154
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          357..438
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          528..812
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         556
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   845 AA;  94732 MW;  19BC578A52205C6F CRC64;
     MKSCEALLNT IQILLIFLAP PLCMSLVFDT ITPNHPIKDG DVLLSGQKTF ALGFFSPGKP
     LNRYVGVWYN KISEKTVVWV ANRDNPINDT SGVLAINSKG RLSIYAKYQN SPIWSANLSV
     FTAKTSSTFI AKLLDVGNLV LMKKDDSFGQ SSVIWQSFDY PTNTYLPFLK LGLNRKTGLD
     RFITSWKSAD DPGTGNCTYR MNLTGYPQMI LYKGQVPFWR AGCWTGRRWT GVPTMIGMIN
     GFIFNVSYTN NKDETSIMYG INNDTNSVFS RLVIDESGTA RRSTWQDQRK EWVEFSYVPA
     ERCDNYGICG RNGKCNQSDA SQLECVCLPG FEPHSRDSWD LRDRSGGCMR KGGARTCGDG
     EGFAKVTRVK LPDTFNARGE MGLNLRECEE KCLKDCNCTA YTSLDETRDG AGCLSWHGDL
     VDIRTFTNAG QDLYVRVDAV TLAQYAKKSN GSISKTGKLA ILLCSVVIFF LLVFIAYWLA
     NRKRISGKER RNTKRSNFSE EGELDDGKTD SDVPLFDLHT IAIATANFSA ENKLGQGGFG
     SVYKGMLSNG KEIAVKRLSR CSRQGSTEFR NEVQLVAKLQ HKNLVRILGC CFHEEERMLV
     YEYLPNKSLD SFIFDEEKRK SLDWRRRFDI ICGIARGILY LHQDSILRII HRDLKASNVL
     LDAALNPKIS DFGLARIFGE DQSEACTNRV VGTYGYMAPE YAMEGLFSTK SDVYSFGVLL
     LEIITGRKNI DYYEEKSESN LLGHVWDLWK EGRASEIVDP FLDESFVDEA LRCIQIGLLS
     VQEHANDRPT MSAIVLMLGN DSALPSPKQP AFILNRCWAG TGDRASSEGV YNSINIVSCT
     MVEAR
//

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