ID V4NK38_EUTSA Unreviewed; 869 AA.
AC V4NK38;
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_v10027637mg {ECO:0000313|EMBL:ESQ46716.1};
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:ESQ46716.1, ECO:0000313|Proteomes:UP000030689};
RN [1] {ECO:0000313|EMBL:ESQ46716.1, 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|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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
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DR EMBL; KI517416; ESQ46716.1; -; Genomic_DNA.
DR RefSeq; XP_006405263.1; XM_006405200.1.
DR AlphaFoldDB; V4NK38; -.
DR EnsemblPlants; ESQ46716; ESQ46716; EUTSA_v10027637mg.
DR GeneID; 18022410; -.
DR Gramene; ESQ46716; ESQ46716; EUTSA_v10027637mg.
DR KEGG; eus:EUTSA_v10027637mg; -.
DR eggNOG; ENOG502QU6U; Eukaryota.
DR OMA; VQGKKDF; -.
DR OrthoDB; 364069at2759; -.
DR Proteomes; UP000030689; 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: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 CDD; cd00028; B_lectin; 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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR PANTHER; PTHR47974:SF27; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR47974; OS07G0415500 PROTEIN; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000641; SRK; 1.
DR SMART; SM00108; B_lectin; 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; PS51257; PROKAR_LIPOPROTEIN; 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 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..869
FT /note="Receptor-like serine/threonine-protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004723579"
FT TRANSMEM 439..463
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..153
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 512..811
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 835..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 541
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 869 AA; 96117 MW; 32F6A0A7AEB069AF CRC64;
MRSKFLVLFL CLYLLLVSVS CASFTEFVYP NFTASNLRFI DSSNGAFLFS RNSIFKAGLF
SPGGDSSTHF YFSIIHVDSD STIWSSNSDS PVSSSGKMNL SPLGLSVIED GKGQIPVWST
PVLASPVYSL RLTDAGNLLL LDRFNASIWE SFRFPTDTIV LGQKLPLGMS LSGSTSLYNF
STGDYKFVVV ESGGFMMWKG HNYWKLRMHT RANVDSNFPV EFLTVTTSGL ALMGQNGTTV
IIRVALPPSS DFRLAKMDSS GKFIIRRFSG KKMVTEFSGP TDLCQIPFVC GTLGICHLDN
DSENKSCSCP DEMQLDAGKK TCVPVSQSLS LPVSCEESKF SYLELELGVS YFATHFTDPV
EHGFELSACH DLCSKNCSCV GVFYENTSRS CYLVKDSFGS LSLVKNSPDN HDLIGYVKLS
FNKNSIAQSP GNKNRGSNFP LIALVLLPCS GFFLLIALGF LWWRRCAVMR YSSIREKQVT
RPGSFGSGDL GSFHIPGLPQ KFEFEELEQA TDNFKMQIGS GGFGAVYKGT LPDETLVAVK
KITNHGLHGR QEFCTEIAVI GNIRHTNLVK LRGFCARGRQ LLLVYEYMNH GSLEKTLFGA
NGPVLEWQER FDIALGTARG LAYLHSGCDQ KIIHCDVKPE NILLHDHFQP KLSDFGLSKL
LSQEESSLFT TMRGTRGYLA PEWITNTAIS EKADVYSYGM VLLELVSGRK NCSFRSRSNS
VTEENHQQCS STTTSSSGLV YFPLYALDMH EQGRYMELAD PRLEGRVTSQ EIGKLVRIAL
CCVHEEPALR PTMAAVVGMF EGTIPLGNPR MESLNFLRFY GLRFAESSMV EGQNGESENM
VFHRRESSNS GGSRLSSSYV ASQEVSGPR
//
