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Database: UniProt
Entry: A0A2H5QN49_CITUN
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ID   A0A2H5QN49_CITUN        Unreviewed;       765 AA.
AC   A0A2H5QN49;
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=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=CUMW_245710 {ECO:0000313|EMBL:GAY66058.1};
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:GAY66058.1, ECO:0000313|Proteomes:UP000236630};
RN   [1] {ECO:0000313|EMBL:GAY66058.1, 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   -!- 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:GAY66058.1}.
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DR   EMBL; BDQV01000536; GAY66058.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H5QN49; -.
DR   STRING; 55188.A0A2H5QN49; -.
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:0042803; F:protein homodimerization activity; IEA:UniProt.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR044815; CCR1-4.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR46146; SERINE/THREONINE-PROTEIN KINASE-LIKE PROTEIN CCR4; 1.
DR   PANTHER; PTHR46146:SF4; SERINE_THREONINE-PROTEIN KINASE-LIKE PROTEIN CCR4; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF13540; RCC1_2; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|SAM:Phobius};
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   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..765
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014174562"
FT   TRANSMEM        364..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          458..747
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          407..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..427
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         486
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   765 AA;  83350 MW;  BF3E548186791DAF CRC64;
     MFNEPNNPFL LTTLLLLFFV SLVPFNSSLS TFSISETGNQ SLVCALIPSS RPGDFSLNCS
     IPQLIPVNPN ASFASIVSGD GFLCTLITFS ASSSSVMHCW RFSADGIIND YKRIYRGPAL
     KQLEAGNSHI CGLVNGTNDL HWWQWHDFNS TSTHNFSNIA VGEDFVCGLL ENGTITCFGS
     RNSPTSVTQK VPSGIFRVVA AGFRHVCAID DDQELRCWGD SVGEVPQGKF TALALGENRS
     CALRNNQKVV CWGQNGFTLP DSLQGIYFVS IEAKRSVFCG VLASNYSLYC WGNENFSSNH
     MVFESVLPGP CTNTCPCLML PGSGNVCGEG QIICQPCFEK TSVTPSPTPQ PPESGSGGGW
     SGRMVALLVV GCLGSLVVVL VSAFFGYKHC KCKGCRVHDS GPLDEAVAQA QSAQPPMPPP
     PPSPPVLEKK LSQLASMGNA GRLEEFSLEI LLEATNNFSE DHKIGSGSFG AVYKATLDDG
     RQVAVKRAEI SSTSSYAIGT KRQEDKDNAF INELESLSRL HHKNLVRLLG FCEDRNERVL
     IYEYLENGTL HDHLHNPQSS SPLKSWPARI KVALDAARGI EYLHEYAVPS IIHRDIKSSN
     VLLDATWTAK VSDFGLSLIG PEDDESHLSL RAAGTVGYMD PEYYRLQQLT EKSDVYSFGV
     VLLEILSGYR AIHRTDNGTP RNVVDFVVPY IVRDEIHRVL DRNVPPPTPF EIEAVAYVGY
     LAADCVTLEG RNRPSMTEIV NSLERALAAC LVSPSISRSA TSSST
//
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