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Database: UniProt
Entry: A0A1U7ZU50_NELNU
LinkDB: A0A1U7ZU50_NELNU
Original site: A0A1U7ZU50_NELNU 
ID   A0A1U7ZU50_NELNU        Unreviewed;      1044 AA.
AC   A0A1U7ZU50;
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=LOC104597322 {ECO:0000313|RefSeq:XP_010257102.1};
GN   ORFNames=HUJ06_028153 {ECO:0000313|EMBL:DAD26685.1};
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_010257102.1};
RN   [1] {ECO:0000313|EMBL:DAD26685.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:DAD26685.1};
RX   PubMed=32343808;
RA   Shi T., Rahmani R.S., Gugger P.F., Wang M., Li H., Zhang Y., Li Z.,
RA   Wang Q., Van de Peer Y., Marchal K., Chen J.;
RT   "Distinct Expression and Methylation Patterns for Genes with Different
RT   Fates following a Single Whole-Genome Duplication in Flowering Plants.";
RL   Mol. Biol. Evol. 37:2394-2413(2020).
RN   [2] {ECO:0000313|RefSeq:XP_010257102.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR   EMBL; DUZY01000002; DAD26685.1; -; Genomic_DNA.
DR   RefSeq; XP_010257102.1; XM_010258800.2.
DR   GeneID; 104597322; -.
DR   KEGG; nnu:104597322; -.
DR   eggNOG; ENOG502QPYS; Eukaryota.
DR   OrthoDB; 382073at2759; -.
DR   Proteomes; UP000189703; Unplaced.
DR   Proteomes; UP000607653; 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:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
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; PTHR27008:SF616; OS02G0211800 PROTEIN; 1.
DR   PANTHER; PTHR27008; OS04G0122200 PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 10.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00369; LRR_TYP; 8.
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_010257102.1};
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_010257102.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189703};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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        663..685
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          726..993
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         753
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1044 AA;  114331 MW;  C29719DCA84024D5 CRC64;
     MEFSPLRCVT LSLTMITHVL ILFSLNLFGL ESATAATTSG NDTDWLALLE FKKQITDDPL
     GVLSSWNGSV HLCDWHGVTC GRRRRQRIIG LNLEGKKLVG TLSPHIGNLS LLSFINLQNN
     SFHGSIPQEV SRLSMLRDIL LNNNSFGGEI PHNLSHCSNL KHLTLHYNRI EGKIPVELGS
     LTHLVNLSLG SNNLTGGIPY SIGNLTSLEH LSFEGNSLGG NIPNIFNQMK RLKHLEFELN
     DFFGIIPPSV YNLSSLTLIA LTGNKLNGSL RPNIGLAFPN LQFLWVGDNQ FSGPIPFSLS
     NASGLIEIDI PGNNFTGPVP MDLGSIQTLQ WLGLGENPIG RGEADDLNFI TSLINCSDLW
     TLSLYDCNFG GMLPSSIANL STQLIQLSFT GNQIIGGIPI GIENLVKLIS LEMDNNLLTG
     SIPDSIGRLS KLQLLSLSGN RLTGQIPPSL GNMTQLVYLD LYNNNLRGRI PPSLVNCQGL
     QEVYLSHNKL NGTIPKEVIG LSSLSIILDV SHNSLTGSLP LEVGSLKNLG HLDVSYNRMT
     GEIPSTLGNC LSLEHLYMQG NFFQGTIPSS LSNLKAIQDL DLSNNNLSGS IPKSLGGLPL
     LQYLNLSFNS FEGEVPVVGV FLNVTAVSVD GNRGLCGGIP ELKLQPCPME ESMKKGKSLT
     FKLVTAIVSV ILGLTLILAL FFVCWRRKPK GISSSEPLVE ECSTPPFGEW YLKVSYRDLF
     KATEGFSSGN LIGSGGYGTV YKGILHNNTI AVKVLNTQQR GASKSFMTEC EAVRNIRHRN
     LIKIITACSS MDLNGNDFKA LVFEFMPNGS LEEWLHPGEE KNSQSRKLNF LVRLNIAIDV
     ASALHYLHYQ CEAPIVHCDL KSSNVLLDND MTACVSDFGM SRLLSNSTKK LTQKQFSSFA
     IKGTIGYAAP EYGMGAEVST HGDVYSYGIL LLEMFTGKRP TAEIFKDGLN LHNYCKMALS
     ERVMEIADPL LLLYGEEIEQ NGEKETATNN EYLSGSGHKM QECLIFVIRI GVACSAELPR
     ERMDMNEVTR EMNSIRNTFL GARY
//
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