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Database: UniProt
Entry: A0A1U7ZG31_NELNU
LinkDB: A0A1U7ZG31_NELNU
Original site: A0A1U7ZG31_NELNU 
ID   A0A1U7ZG31_NELNU        Unreviewed;       997 AA.
AC   A0A1U7ZG31;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-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=LOC104589770 {ECO:0000313|RefSeq:XP_010246505.1};
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_010246505.1};
RN   [1] {ECO:0000313|RefSeq:XP_010246505.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   RefSeq; XP_010246505.1; XM_010248203.2.
DR   AlphaFoldDB; A0A1U7ZG31; -.
DR   GeneID; 104589770; -.
DR   OrthoDB; 991910at2759; -.
DR   Proteomes; UP000189703; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
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; IPR032675; LRR_dom_sf.
DR   InterPro; IPR021720; Malectin_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48006; LEUCINE-RICH REPEAT-CONTAINING PROTEIN DDB_G0281931-RELATED; 1.
DR   PANTHER; PTHR48006:SF105; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 2.
DR   Pfam; PF11721; Malectin; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|RefSeq:XP_010246505.1};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000313|RefSeq:XP_010246505.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189703};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|RefSeq:XP_010246505.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..997
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010582059"
FT   TRANSMEM        579..602
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          640..900
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          965..997
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        977..991
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   997 AA;  110663 MW;  8445BFD2A7539A20 CRC64;
     MAVLADSSKI LSALLCFLVL NCFAGFRSEA RVLPDEEVQA LRKISAKLNN KYWTIKSTSC
     SGGFINSYNY ARNIISNITC DCSYNAFTVC HITKFKMEGM NLTGILPDEF GDLPYLTEID
     LIRNYINGTI PVSWTRIPLV TINLIGNRIS GSIPAEFGSV ETLEELVLED NQLGGTLPPQ
     LGNLTRLRRL LLSANNITGP LPETFGKLKN LTDFRIDGNS ISGRIPNFIG NWTKINILNM
     QGTSLEGPIP SEISFLTNLI QLRVSDLNGS NMSFPDLSGM KSITDLILRN CMITGQIPDY
     ISEMKNIIRL YLTNNSLTGS VPSWIIDNKK YIDISYNNFT GYSPQPGCEQ TNVKTVASYS
     SPEGNLVNWC LKKDLSCSSK PRYHSLFINC GGPKVVIHGE EYEEDLSPMS SSAFHASNER
     WACSTTGDYL YSDPPNFKVQ ANTALNVTDS ELYSTARLSP LSLKYYGLCL RKGSYTVKLH
     FAEIIYTEDR TFSSLGERIF DVLIQGEIRL KDFNIAKEAN GVGKSNIQEF KDVFVDGSTL
     EIHLYWSGKG TTAIPDRGVY GPLISAITVT PNFNPDTGLS VGAIVGIVAA ACVVLILILV
     TLRMNGYLGR KDLEDNELGG LEIQSGYFSL KQIKSATGNF DPENKIGEGG FGPVYKGILP
     DGTVIAVKQL SSKSKQGSRE FLNEIGMISA LQHPNLVKLF GCCVEGNQLL LIYEYMENNS
     LARALFGSEE HRLELNWPVR RKICLGIARG LAYLHEESRL KIVHRDIKAT NVLLDKDLNA
     KISDFGLAKL DEEGNTHIST RIAGTIGYMA PEYAMRGYLT DKADVYSFGV VLLEIVSGKS
     NTSYRPKEDF VYLLDWAYVL QEEDNLLELV DPTLESRYSK EEALRMLSLA LLCTGPSPFL
     RPTMSSVVSM LEGKIPVQAP LNQSSMNDEL RLRAFEKFSQ DSQSYISGTS QESWVQKSIS
     ADDPRFGSTT SFPYNEENEH QSDERKLIHD VNDISLN
//
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