ID A0A2H5PMZ2_CITUN Unreviewed; 912 AA.
AC A0A2H5PMZ2;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=CUMW_151230 {ECO:0000313|EMBL:GAY53720.1};
OS Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=55188 {ECO:0000313|EMBL:GAY53720.1, ECO:0000313|Proteomes:UP000236630};
RN [1] {ECO:0000313|EMBL:GAY53720.1, ECO:0000313|Proteomes:UP000236630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Miyagawa wase {ECO:0000313|Proteomes:UP000236630};
RX PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA Fujiyama A., Kaminuma E., Nakamura Y.;
RT "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT unshiu Marc.) using a hybrid assembly approach.";
RL Front. Genet. 8:180-180(2017).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAY53720.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BDQV01000096; GAY53720.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5PMZ2; -.
DR Proteomes; UP000236630; 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; 4.
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; OS04G0122200 PROTEIN; 1.
DR PANTHER; PTHR27008:SF567; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 5.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000236630};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..912
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014198405"
FT DOMAIN 728..912
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 767
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 912 AA; 99707 MW; A29C00E1FF28FF36 CRC64;
MERNFSLSMI TVSLTHFLLL CLVVAAAAAA SNNITTDQQA LLALKDHIIY DPTNLLAHNW
TSNTSVCTWI GITCDVNSHR VTALDISQFN LQGTIPPQLG NLSSLTTLNL SHNKLSGSVP
SSIYTMHTLK FLDFTDNQLS GSVSSFVFNM SSILDIRLTN NRLSGELPKN ICNYLPHLKA
LFLDKNMFHS KIPSALSKCK QLQQLNLQFN NLSGAIPKEI GNLTRLKGIY LGANKLHGEI
PHEIANLRNL EVLVLGMNNL VGVLPAPIFN MSTLKVIILM NNSLSGSLPS RIDLSLPTVE
FLELSHNRFS GTIPSSITNA SKLTVLALGD NKFSGFIPNT IGNLRNLERL SLPNNYLKSS
TSKLSFLSSL ANCKKLRDIV LIGNPLDGFL PSSIGNLSKS LETLVIANCS ISGNIPQAIS
NLSNLLTLVL EGNKLTGPIP ITFGRLQKLQ GLYLAFNKLV GSFPDELCHL ARLDQLVLFG
NKLSGSIPSC LSNLTSLRSL YLGSNSLKDI LFFDFSSNFL VGPLSLDIEN LKVLLGINLS
KNNLSGDIPA TIGGLKDLQF MDLAYNRLEG PIPKSFGDLI SLEVLNLSNN KMSGSIPTSM
EKLFYLGELN LSFNKLEGEI PSGGTFANFT AESFMGNEFL CGLPNLQVQP CKVSKPRTEH
KSRKKILLIV IVLPLSIALT IAITLALKSK PIECGERSTV LSNDSILSSQ ATLRRFSYLE
LLQATDNFAE NSIIGRGGFG SVYGARLEDG MKIAIKVFHR QCASALKSFE AECEVLKKIR
HRNLIKVISS CSNDDFKALV LEYMSNGSLG DWLHSSNYVM NIFQRLNIMI DVASALEYLH
FDHSTPIIHC DLKPSNVLLD ENMVAHLSDF GIAKLLSGED ESTMRTKTLA TIGYMAPEYG
IGGEVSTKSD VW
//