ID A0A1S2Y2T9_CICAR Unreviewed; 662 AA.
AC A0A1S2Y2T9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=LOC101514267 {ECO:0000313|RefSeq:XP_004497890.1};
OS Cicer arietinum (Chickpea) (Garbanzo).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004497890.1};
RN [1] {ECO:0000313|RefSeq:XP_004497890.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004497890.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 leguminous lectin family.
CC {ECO:0000256|ARBA:ARBA00007606}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. Ser/Thr protein kinase family.
CC {ECO:0000256|ARBA:ARBA00010217}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the leguminous lectin
CC family. {ECO:0000256|ARBA:ARBA00008536}.
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DR RefSeq; XP_004497890.1; XM_004497833.3.
DR AlphaFoldDB; A0A1S2Y2T9; -.
DR STRING; 3827.A0A1S2Y2T9; -.
DR PaxDb; 3827-XP_004497890-1; -.
DR GeneID; 101514267; -.
DR KEGG; cam:101514267; -.
DR eggNOG; ENOG502QSBD; Eukaryota.
DR OrthoDB; 363215at2759; -.
DR Proteomes; UP000087171; Chromosome Ca4.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
DR InterPro; IPR001220; Legume_lectin_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27007; -; 1.
DR PANTHER; PTHR27007:SF252; L-TYPE LECTIN-DOMAIN CONTAINING RECEPTOR KINASE S.5-RELATED; 1.
DR Pfam; PF00139; Lectin_legB; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 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|PROSITE-
KW ProRule:PRU10141}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_004497890.1};
KW Lectin {ECO:0000256|ARBA:ARBA00022734}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Receptor {ECO:0000256|ARBA:ARBA00023170,
KW ECO:0000313|RefSeq:XP_004497890.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087171};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 270..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 335..623
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 662 AA; 74465 MW; 4303CE8B7778D5AE CRC64;
MNMSMLHKYQ FLAFVFSIIF LTKVTSFYFN FPTFQPNDEA NLLLSKNSKI YLDAIQITPD
IRGIIVNYSG RAFYNKPYKL WNKKKIASFN TTFVLNITPQ TSPGGEGVAF ILTPNTNLPE
NSEGKWLGIV NASTNGTSKA EILAVEFDTK QSSTQDGPSN HVGININSIN SIKQTSLTNT
KVNLSSGTSV TIRIQYFNDV ISVFGSMSET SHDSMETLLV SPPLNLSSYL KQEVFVGFSG
STSNYTELNC VKAWEFIGLD IGDNNKNNLL WVWIIIPMVI LIIGLVTFLI YYWQKRRNIE
IQEDAYPRIE DQIQHSSMSP KKYTLKELIK ATNGFNHQNK LGEGGFGTVY KGILGNNNKE
IAVKRVSKNS RQGKQEFVAE VTTIGSLHHK NLVKLIGWCY EKKELLLVYE YMPNGSLDKY
LFFHPNQNSY ATLNWETRHS VIHGVAQALD YLHNGCEKRV LHRDIKASNI MLDLEFNAKL
GDFGLARTIQ KKNETHHSTK EIAGTPGYMA PETFLTGRAT VETDVYGFGV LVLEVVCGKR
PGNNIYAQDD YKNSIVYWVW ELYGKGNILS ALDKRVISSS EMDDEEIEIV LVLGLACCHP
NPHERPTMRS VLQVLNGEAN PPMVPIDRPA FVWPAMPSSF KENEDSSLIN GTLTPFTEIS
GR
//
