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Database: UniProt
Entry: A0A1U8ARI4_NELNU
LinkDB: A0A1U8ARI4_NELNU
Original site: A0A1U8ARI4_NELNU 
ID   A0A1U8ARI4_NELNU        Unreviewed;      1109 AA.
AC   A0A1U8ARI4;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Cysteine-rich receptor-like protein kinase 10 {ECO:0000313|RefSeq:XP_010265354.2};
GN   Name=LOC104603105 {ECO:0000313|RefSeq:XP_010265354.2};
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_010265354.2};
RN   [1] {ECO:0000313|RefSeq:XP_010265354.2}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR   RefSeq; XP_010265354.2; XM_010267052.2.
DR   AlphaFoldDB; A0A1U8ARI4; -.
DR   GeneID; 104603105; -.
DR   KEGG; nnu:104603105; -.
DR   eggNOG; ENOG502RXD9; Eukaryota.
DR   InParanoid; A0A1U8ARI4; -.
DR   OrthoDB; 1205584at2759; -.
DR   Proteomes; UP000189703; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14066; STKc_IRAK; 2.
DR   Gene3D; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR002902; GNK2.
DR   InterPro; IPR038408; GNK2_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR27002:SF427; OS07G0628700 PROTEIN; 1.
DR   PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR   Pfam; PF01657; Stress-antifung; 2.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS51473; GNK2; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_010265354.2};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Receptor {ECO:0000313|RefSeq:XP_010265354.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189703};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          48..318
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          455..558
FT                   /note="Gnk2-homologous"
FT                   /evidence="ECO:0000259|PROSITE:PS51473"
FT   DOMAIN          564..669
FT                   /note="Gnk2-homologous"
FT                   /evidence="ECO:0000259|PROSITE:PS51473"
FT   DOMAIN          784..1059
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1078..1109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1093..1109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         77
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         813
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1109 AA;  122615 MW;  DD2D08C382F7DC1B CRC64;
     MEFLDIFCGC LKRKREKGAE GGEEPDDYRD SSGLIFELRS LQVATNFFSD LNQLGHGGFG
     SVFKGLLPSG QEVAVKKLAL NSRQGLREFM NEVKLLIKIQ HKNLVTLLGC CAEGPEKMLI
     YEYLPNKSLD NFLFDKTKSA SLDWSKRFEI ITGITRGLLY LHEEAPERII HRDIKASNIL
     LDGRMNPKIS DFGLARLFPG DDTHVNTFRI SGTHGYMAPE YAIHGYLSVK TDVFSFGILV
     LEIVSGRKNH VQKLNDEKAD LLSYTWNLFQ QKRTLDLVDP TLSNCNPDEA ALCIQIGLLC
     CQANVADRPD MNSVHLMLSS DSFTLPKPGK PGIQGRVGRW TTTSSALTAT NATDSTTGTN
     KLSTTSTMVE DCSRNSISVS FVDEGRMTPA SAVSNHRDSK ILQSPDKNMG TLAICSGITL
     SSFISPSQMT HLSFLSLISS FLFLSLNPAA LAYELPRWDD CDGATNYTAN STFAANLGQA
     LDALSNSTAP TGFNATIVGN GTESVTALAL CRADTTQAGC RVCIDAAVVD IRQKNCPMKR
     FAQIWYNDCM LRYADVNFLS RADVSVVLSI WNTMEVSNQD VYDQSVRMLM RNLSNMAGES
     QTLHAVGWTR VPDNRILYGY VECTRDLSAD NCSRCLSNAR IGIENCCMGQ WAAWVATPSC
     SVQFSMDPGF FDNTTAAVPE ILAEPPLPPP PTWAPESDIQ TDLTRVKRNG GGGRGMVIGI
     SGAASGTVIL TVGCSWMVMK GKKKVKRSGS RMEDDEVGET VTESVGTRSF LYDLETLMAA
     TDNFSTANRL GCGGFGTVYK GKMPNGEKIA VKKLTVGSAQ GTEEFTNEVR LLQKMQHRNL
     VKLFGCCIQG QEKILVYEYL SNRSLDHFLF DKSKSALLDW PKRFNIIIGI ARGLLYLHED
     SQYRIIHRDI KASNILLDEH MNPKISDFGL AKLFPDERSQ LRTRRIAGTF GYMAPEYAAR
     GFMSAWSDVY SFGVLILEII SGRRNYDSQL EEQRQVLLNL TWRLEQQGKL IDLVDVTIGS
     FPQDEVLRCI RVGLLCCQQR TRERPIMSSA LVMLSNQSVS VPTPVRLGYQ GSRVNSLEIS
     ESSSRDSSNH ENENASHNNS VTISVVSGR
//
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