ID A0A1S2YZM9_CICAR Unreviewed; 1028 AA.
AC A0A1S2YZM9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-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=LOC101498568 {ECO:0000313|RefSeq:XP_004512441.1};
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_004512441.1};
RN [1] {ECO:0000313|RefSeq:XP_004512441.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004512441.1};
RG RefSeq;
RL Submitted (SEP-2023) 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|ARBA:ARBA00001433};
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR RefSeq; XP_004512441.1; XM_004512384.3.
DR AlphaFoldDB; A0A1S2YZM9; -.
DR PaxDb; 3827-XP_004512441-1; -.
DR GeneID; 101498568; -.
DR KEGG; cam:101498568; -.
DR eggNOG; ENOG502QPYS; Eukaryota.
DR OrthoDB; 376508at2759; -.
DR Proteomes; UP000087171; Chromosome Ca8.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48053; LEUCINE RICH REPEAT FAMILY PROTEIN, EXPRESSED; 1.
DR PANTHER; PTHR48053:SF37; LEUCINE-RICH REPEAT PROTEIN KINASE FAMILY PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 7.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00365; LRR_SD22; 8.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_004512441.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Receptor {ECO:0000313|RefSeq:XP_004512441.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087171};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
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 657..680
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 712..1017
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 741
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1028 AA; 113885 MW; A44C5A0BCBEA5F5C CRC64;
MKSFLHMLHA FFLICLYILQ LYTLNLLWFG PNKTAYALGN DTDFLALLKF KKSISNDPFG
ILDSWNGSTH FCKWHGITCM HQRVTELYLA GNQLHGSISP HVGNLTFLTN FNLMNNSFYG
TIPQELCSLV KLQQLYLNNN SLVGEIPSNL TSLLNLKSLY LSRNNLVGTI PIEIGSLKKL
QRIFIWNNNL TGEIPPTIGN LSFLINFNVG SNNLEGNIPQ EICHLKNLET ISVGINKLSG
KLPLCLYNMS SLTLIAVDLN QFNGSLPPKM FHTLPNLKTL FIGGNQISGL IPTSITNASY
LRAFDITQNQ FIGHVPSLGK LKDLQLIGLS QNNLGSNSTN DLEFVKSLEN CSKLYVIDIS
YNNFGGLLPN TLGNMSKQLN SIYLGGNHIS GKIPAELGNL VNLYLFTVEN NRFEGMIPTT
FVKVQKLQVL ELRGNKLSGS IPAFIGNLSQ LFYLGLGHNK LEGNIPPSIG NCQKLYYLDL
SQNNLRGTIP IEVFNLFSLT KLLDLSRNAL SGSLPQEVGR LENIGMLNFS ENHLSGDIPK
TIGKCESLEY LHLQGNSFHG VIPTSLVSLK SLQHLDLSRN RLSGSIPKGL QNISFLEYFN
VSFNMLEGEV PTEGVFQNAS EVVVTGNNNL CGGISKLHLP PCPLKGKKQA KHHYLKLIAV
VVSVASFLLI LLFILTIYCI KKRNMKPSSD SPRIDLLVKI SYEDLHNGTD GFSTRNLIGS
GSFGSVYLGT LELDDKVVAV KVLKLQKKGA HKSFMVECNA LKNIRHRNLV KILTSCSSTD
FKGQEFKALV FEYMRNGSLE SWLHPEKEIA GPQKTLNLAQ RLNIIIDVAS AFHYLHHECD
QPVIHCDLKP SNVLLDDSMV AHVSDFGIAK LLPSIGVSLT QNSTVGIKGT IGYAPPEYGM
GSKLSIEGDV YSFGILILEI LTGRRPTDEM FEDSHSLHNF VKISISSDLL QIVDPTIVHN
ELEQTIDSEN VGAMHSNVEK CLLSLFSIAL ACSVESPKER MSMVEVMREL NIIKSFFPTE
DLMEANLH
//