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Database: UniProt
Entry: A0A2H5Q3H2_CITUN
LinkDB: A0A2H5Q3H2_CITUN
Original site: A0A2H5Q3H2_CITUN 
ID   A0A2H5Q3H2_CITUN        Unreviewed;       690 AA.
AC   A0A2H5Q3H2;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=CUMW_192680 {ECO:0000313|EMBL:GAY59187.1};
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:GAY59187.1, ECO:0000313|Proteomes:UP000236630};
RN   [1] {ECO:0000313|EMBL:GAY59187.1, 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. CMGC Ser/Thr
CC       protein kinase family. CDC2/CDKX subfamily.
CC       {ECO:0000256|ARBA:ARBA00006485}.
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:GAY59187.1}.
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DR   EMBL; BDQV01000205; GAY59187.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H5Q3H2; -.
DR   STRING; 55188.A0A2H5Q3H2; -.
DR   Proteomes; UP000236630; Unassembled WGS sequence.
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   CDD; cd07840; STKc_CDK9_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR   PANTHER; PTHR24056:SF397; OS11G0242500 PROTEIN; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000236630};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          138..422
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          424..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..511
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..605
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..628
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..671
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..690
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   690 AA;  76439 MW;  D57FA624ABF2FB14 CRC64;
     MGCICSKAIR AKKYIAKNNA KEKELTKRTN KRLGSFEKEN VTVVVETDGI GNESTTRLIN
     DQSVADDDVG SSDDGEKKVK LQRRSTINVQ VAQPRMTRIV SVSNGERGAQ VVAGWPSWLT
     AVAGEAINGW VPRKADSFEK LDKIGQGTYS SVYKARDLEN NKLVALKKVR FTNMDPESVR
     FMAREIIILR RLDHPNIMKL EGLITSRVSG SLYLVFEYME HDLAGLAATP GVKFTEAQIK
     CYMKQLLHGL EHCHSRGILH RDIKGSNLLI DYNGILKIGD FGLANFFKCS QKQPLTSRVV
     TLWYRPPELL LGSTDYGASV DLWSSGCILA ELFAGKPIMP GRTEVEQLHK IFKLCGSPSE
     EYWKRSKLPH ATIFKPQQPY KRCVAETFKD IPSSALSLLD ILLSTEPEVR GTASSALQNE
     FFTTKPLPCD PSSLPKYSPS KEFDVKLRDD DRRRGGGGKG RGLESIRKTG KESKAVPAPD
     ANAELQTSIQ KRQNQSNPKA TSEQFNSDED SGSGFPIEPP KGIGRNAGGQ TMKPTTVGAS
     LNMTMDSDRN SRSYMHPGAA GLSRFANSVA VRGGHSQLDC SNRVNSQWSD DSGHEWSQNL
     LDRPMSSYNK KGEKPSGKES KTQDFASKKT RMHYSGPILP PGGNLEEMLK EHERQIQQAV
     RRARGDKTKA QKNGESGQTQ SLLHYGRNGR
//
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