ID V4MUM3_EUTSA Unreviewed; 871 AA.
AC V4MUM3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=EUTSA_v10006766mg {ECO:0000313|EMBL:ESQ35711.1};
OS Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Eutremeae; Eutrema.
OX NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ35711.1, ECO:0000313|Proteomes:UP000030689};
RN [1] {ECO:0000313|EMBL:ESQ35711.1, ECO:0000313|Proteomes:UP000030689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23518688; DOI=10.3389/fpls.2013.00046;
RA Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., Jenkins J.,
RA Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A.,
RA Mitchell-Olds T., Schumaker K.S., Wang X.;
RT "The Reference Genome of the Halophytic Plant Eutrema salsugineum.";
RL Front. Plant Sci. 4:46-46(2013).
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|ARBA:ARBA00001433,
CC 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|ARBA:ARBA00000775,
CC ECO:0000256|PIRNR:PIRNR000641};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI517683; ESQ35711.1; -; Genomic_DNA.
DR RefSeq; XP_006417358.1; XM_006417295.1.
DR AlphaFoldDB; V4MUM3; -.
DR STRING; 72664.V4MUM3; -.
DR EnsemblPlants; ESQ35711; ESQ35711; EUTSA_v10006766mg.
DR Gramene; ESQ35711; ESQ35711; EUTSA_v10006766mg.
DR KEGG; eus:EUTSA_v10006766mg; -.
DR eggNOG; ENOG502QUDG; Eukaryota.
DR OMA; DKFECSC; -.
DR Proteomes; UP000030689; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0048544; P:recognition of pollen; IEA:InterPro.
DR CDD; cd00028; B_lectin; 1.
DR CDD; cd00054; EGF_CA; 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; IPR000742; EGF-like_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PS50026; EGF_3; 1.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|PIRNR:PIRNR000641}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000641};
KW Reference proteome {ECO:0000313|Proteomes:UP000030689};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..871
FT /note="Receptor-like serine/threonine-protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004725287"
FT TRANSMEM 471..493
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..147
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 283..321
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 341..424
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 549..834
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 837..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 98670 MW; 94C6776F01682D81 CRC64;
MKIFSIFFFV LFSLLIQSCF SDNMIMRRQS LRDGDVLFSE GKRFAFGFFS LRNSNLRYVG
IWYAQVSEQT IVWVANRDHP INDTSGHVKF SSRGNLCVYA SVNGTEPVWS TDVLDTIAEP
ALVAKLSDLG NLVLLDPVTG KSFWESFNHP TNTLLPFMKF GFTRQDGLDR FMTSWRSPSD
PGFGNVTYRI DRRGFPQMMM FKGPTLWWRT GSWTGQRWSG VPEMTNKFIF NISFVNTPDE
VSITYGVLNP LVITRMVLNE TGILQRFTWN GRDKKWIGFW SAPEEKCDSY NHCGLNGYCD
STSPDKFECS CLPGYEPKKP QEWSFRDASG GCMRRDTASI CNGREGFARL KRVKVPNTSA
VSVDMNITLK ECGKRCLRNC SCVAYASAYH ESEDGAIGCL TWHGDMLDTR TYLSAGQDFY
LRVDKAELGT YIHKLCNLFC LIATKEEFQV LICLLVTARW NGNGSSGKRR LALILISLIV
VVMLLMTILF CFMRKRRQSN RHRKPPSIFA PSSFDLEDSF ILEDLEDKSR NRDLPIFELS
TIAAATDNFS FQNKLGTGGF GPVYKGVLQN GMEIAVKRLS RNSGQGMEEF KNEVKLISKL
QHRNLVRILG CCVELEEKML IYEYLPNKSL DYFIFREEHR AELDWPKRMG IIRGIARGIL
YLHQDSRLRI IHRDLKASNV LLDNEMIPKI ADFGMARIFG GNQVEGSTNR VVGTYGYMSP
EYAMDGQFSI KSDVYSFGIL ILEIITGKKN STICEESSNL VGHIWDLWEK GEATKIIDTL
MDVETYDESE VMKCIHIGLL CVQESASDRP DMSSVVFMLG HNAIDLPSPK HPAFTVGRKR
NFKNGGSSGN WPSGETGSSV NDVTLTDVQG R
//