ID A0A1S2XHG3_CICAR Unreviewed; 511 AA.
AC A0A1S2XHG3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=LOC101497668 {ECO:0000313|RefSeq:XP_004489425.1};
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_004489425.1};
RN [1] {ECO:0000313|RefSeq:XP_004489425.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004489425.1};
RG RefSeq;
RL Submitted (NOV-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};
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DR RefSeq; XP_004489425.1; XM_004489368.3.
DR AlphaFoldDB; A0A1S2XHG3; -.
DR STRING; 3827.A0A1S2XHG3; -.
DR PaxDb; 3827-XP_004489425-1; -.
DR GeneID; 101497668; -.
DR KEGG; cam:101497668; -.
DR eggNOG; KOG0583; Eukaryota.
DR OrthoDB; 5388562at2759; -.
DR Proteomes; UP000087171; Chromosome Ca2.
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-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd12122; AMPKA_C; 1.
DR CDD; cd14079; STKc_AMPK_alpha; 1.
DR CDD; cd14335; UBA_SnRK1_plant; 1.
DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR001772; KA1_dom.
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; IPR015940; UBA.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF82; SERINE_THREONINE-PROTEIN KINASE MARK-A-RELATED; 1.
DR Pfam; PF02149; KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF103243; KA1-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50032; KA1; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_004489425.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000087171};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..270
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 291..331
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 463..510
FT /note="KA1"
FT /evidence="ECO:0000259|PROSITE:PS50032"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 511 AA; 58276 MW; 506538FD7F8E4024 CRC64;
MDGTAGPGGS ANGFLRNYKM GKTLGIGSFG KVKIAEHVLT RHKVAIKILN RRKIKNMEME
EKVRREIKIL RLFMHHHIIR LYEVVETPTD IYVVMEYVKS GELFDYIVEK GRLQEDEARS
FFQQIISGVE YCHRNMVVHR DLKPENLLLD SKCNVKIADF GLSNIMRDGH FLKTSCGSPN
YAAPEVISGK LYAGPEVDVW SCGVILYALL CGTLPFDDEN IPNLFKKIKG GIYTLPSHLS
PGARDLIPRL LVVDPMKRMT IPEIRQHPWF QVRLPRYLAV PPPDTLQQAK KIDEEILQEV
VNKGFDRNQL VESLSNRIQN EGTVTYYLLL DNRFRVSTGY LGAEFQETMD SGLNHVHSSE
VASPVVGHRF SGYMDYQGVG TRQQFPVERK WALGLQSRAQ PREIMAEVLK ALQELNVCWK
KIGHYNMKCR WVVSIPDNHG GMVNNSVHSN NYLGNVSIIE NEAVPKSNVV KFEVQLYKTQ
EKYLLDLQRV EGPQFLFLDL CAAFLAQLRV L
//
