ID A0A1U8B4E0_NELNU Unreviewed; 949 AA.
AC A0A1U8B4E0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=LOC104606902 {ECO:0000313|RefSeq:XP_010270626.1,
GN ECO:0000313|RefSeq:XP_010270628.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010270626.1};
RN [1] {ECO:0000313|RefSeq:XP_010270626.1, ECO:0000313|RefSeq:XP_010270628.1}
RP IDENTIFICATION.
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};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR RefSeq; XP_010270626.1; XM_010272324.2.
DR RefSeq; XP_010270628.1; XM_010272326.2.
DR STRING; 4432.A0A1U8B4E0; -.
DR GeneID; 104606902; -.
DR KEGG; nnu:104606902; -.
DR eggNOG; ENOG502QPPH; Eukaryota.
DR OrthoDB; 728091at2759; -.
DR Proteomes; UP000189703; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009882; F:blue light photoreceptor activity; IEA:UniProt.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 2.
DR CDD; cd05574; STKc_phototropin_like; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45637; FLIPPASE KINASE 1-RELATED; 1.
DR PANTHER; PTHR45637:SF22; FLIPPASE KINASE 1-RELATED; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
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}; Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000189703};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 138..211
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 212..266
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 415..488
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 489..543
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 616..902
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 102..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 949 AA; 106995 MW; ADD776112407ADC0 CRC64;
MDYVGQCSQS AHVKFQSSDH IQEGELMTLS GREPTDKWMA FERDYKPENN GCGQGDTDLL
ESNKAVEQNS NRNQILSEAS MAERVAEWGL VVKSEMGIGN SKAIGVRSSG DRSKNSSDRT
TESTRTSEEG SESGFPRVSQ ELKDALATLQ QTFVVSDATK PDCPIMYASA GFFTMTGYSS
KEVIGRNCRF LQGPETDQNE VAKIRKTVKT GESYCGRLLN YKKDGTPFWN LLTITPIKDD
TGKVIKYIGM QVEVSKYTEG LSDKAMRPNG LPKSLIRYDA RQKEQALGSI TEVVQTVKHP
RAHIQSADDE IPAKTEEQDK FNLDYFLPKS AELSNFSTPG RETPQMDDMS RRSSGHDLSN
KSRKSGRISL MGFRGRSQSS AEKPQPSIEP EVLMTKDVKH SDSWDRVERE RDIRQGIDLA
TTLERIEKNF VITDPRLPDN PIIFASDSFL ELTEYTREEI LGRNCRFLQG PETDQGTVSK
IRDAIREQRE ITVQLINYTK SGKKFWNLFH LQPMRDQKGE LQYFIGVQLD GSDHVEPLRN
RLSEKTELQS AKLVKATAEN VDEAVRELPD ANLRPEDLWA IHSQPVFPRP HKKHSPSWLA
IQKIISHGEQ IGLKHFKPIR PLGCGDTGSV HLVELIGTGE LYAMKAMDKS IMLNRNKVHR
ACIEREIVSL LDHPFLPTLY ASFQTDTHVC LITDFCPGGE LFALLDRQPM KIFKEESARF
YAAEVVVGLE YLHCLGIIYR DLKPENVLLQ KDGHVVLTDF DLSFLTSSKP QVIKHPMPTK
RRSRSQPPPM FVAEPVTQSN SFVGTEEYIA PEIITGSGHS SAIDWWALGI LLYEMLYGRT
PFRGKNRQKT FANILHKDLT FPSSIPVSLA ARQLIHGLLH RDPANRLGST NGANEIKQHP
FFRGVIWPLI RCMSPPPLEV PLQLIGKDSK SKDVEWDDEG VLVQSIDIF
//
