ID A0A067GGE5_CITSI Unreviewed; 1002 AA.
AC A0A067GGE5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=CISIN_1g001867mg {ECO:0000313|EMBL:KDO77710.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO77710.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO77710.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; KK784879; KDO77710.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067GGE5; -.
DR STRING; 2711.A0A067GGE5; -.
DR PaxDb; 2711-XP_006468213-1; -.
DR eggNOG; KOG1187; Eukaryota.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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 GO; GO:0099402; P:plant organ development; IEA:UniProt.
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; IPR025875; Leu-rich_rpt_4.
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; PTHR48055; LEUCINE-RICH REPEAT RECEPTOR PROTEIN KINASE EMS1; 1.
DR PANTHER; PTHR48055:SF48; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 6.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 6.
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, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1002
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001641950"
FT TRANSMEM 628..650
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 685..972
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 977..1002
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"
FT BINDING 714
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1002 AA; 109926 MW; 74C17D2C4EE12E2A CRC64;
MELLTGMLVL VAFLLSPLPS LSLNQEGLYL ERVKLSLSDP DSALSSWGRN PRDDSPCSWR
GVECDPRSHS VASIDLSNAN IAGPFPSLLC RLENLTFLTL FNNSINSTLP DDISACQNLQ
HLDLSQNLLT GTLTPALADL PNLKFLDLTG NNFSGDIPES FGRFQKLEVI SLVYNLLDGT
IPAFLGNIST LKMLNLSYNP FLPGRIPPEL GNLTNLEILW LTECNLVGEI PDSLGRLAKL
VDLDLALNNL VGAIPSSLTE LASVVQIELY NNSLTGDLPT GWSNLTSLRL LDASMNDLTG
PIPDDLTRLP LESLNLYENR LEGSLPATIA DSPGLYELRL FRNRLNGTLP GDLGKNSPLR
WVDLSNNQFT GEIPASLCEK GELEELLMIY NSFTGQLPDG LGHCQSLTRV RLGYNRLTGK
VPPLLWGLPH VYLLELTDNF LSGEISKNIA GAANLSLLII SKNNLSGSLP EEIGFLKSLV
VLSGSENKFT GSLPESLTNL AELGSLDLHA NDLSGELPSS VSSWKKLNEL NLADNLFYGN
IPEDIGNLSV LNYLDLSNNR LSGRIPVGLQ NLKLNQLNVS NNRLSGELPS LFAKEMYRNS
FLGNPGLCGD LEGLCDGRGE EKNRGYVWVL RSIFILAGLV FVFGLVWFYL KYRKFKNGRA
IDKSKWTLMS FHKLGFSEYE ILDGLDEDNV IGSGSSGKVY KVVLSNGEAV AVKKLWRGMS
KECESGCDVE KGQVQDQVQD DGFQAEVETL GKIRHKNIVK LWCCCTTRDC KLLVYEYMPN
GSLGDLLHSC KGGLLDWPTR YKIIVDAAEG LSYLHHDCVP SIVHRDVKSN NILLDGDFGA
RVADFGVAKV VDASGKPKSM SVIAGSCGYI APEYAYTLRV NEKSDIYSFG VVILELVTGR
LPVDPEFGEK DLVKWVCSTL DQKGVDHVLD PKLDCCFKEE ICKVLNIGLL CTSPLPINRP
AMRRVVKLLQ EVGAENRSKT GKKDGKLSPY YHEDASDQGS VA
//
