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Database: UniProt
Entry: A0A1Q3B0U9_CEPFO
LinkDB: A0A1Q3B0U9_CEPFO
Original site: A0A1Q3B0U9_CEPFO 
ID   A0A1Q3B0U9_CEPFO        Unreviewed;       985 AA.
AC   A0A1Q3B0U9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=CFOL_v3_05126 {ECO:0000313|EMBL:GAV61599.1};
OS   Cephalotus follicularis (Albany pitcher plant).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Oxalidales; Cephalotaceae; Cephalotus.
OX   NCBI_TaxID=3775 {ECO:0000313|EMBL:GAV61599.1, ECO:0000313|Proteomes:UP000187406};
RN   [1] {ECO:0000313|Proteomes:UP000187406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. St1 {ECO:0000313|Proteomes:UP000187406};
RA   Fukushima K., Hasebe M., Fang X.;
RT   "Cephalotus genome sequencing.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:GAV61599.1}.
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DR   EMBL; BDDD01000213; GAV61599.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3B0U9; -.
DR   STRING; 3775.A0A1Q3B0U9; -.
DR   InParanoid; A0A1Q3B0U9; -.
DR   OrthoDB; 391466at2759; -.
DR   Proteomes; UP000187406; 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   GO; GO:0099402; P:plant organ development; IEA:UniProt.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
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; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR   PANTHER; PTHR48056:SF15; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 6.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00369; LRR_TYP; 7.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51450; LRR; 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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:GAV61599.1};
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:UP000187406};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; 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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..985
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012275649"
FT   TRANSMEM        620..644
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          679..962
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         708
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   985 AA;  107953 MW;  75179C26996D0A9D CRC64;
     MLLLLLLLFL SSPLPILSLN QEGLYLQRVK HTLSDPDAAL ASWNDRDDTP CNWAGITCDA
     PTATVTSIDL SNTNIAGPFP SLLCHLQNLT SISLYNDSIN STLPLDISTC RNLQHLDLAQ
     NLLTGTLPHT LADLPDLKYL DLTGNNFSGE IPASFGRFPK LEVISLVYNL LDGTIPAFLG
     NVTSLKMLNL SYNPFFPGRI PPELGNLTNL EILWLTECNL VGPIPDSLGN LKKLTDLDLA
     LNNLEGPIPS SLTELTSVVQ IELYNNTLTG ELPRGFSNLT KLRLLDASMN QLSGTIPDEL
     TRLPLESLNL YENLFEGTLP GSIAESPVLY ELRLFSNRLT GSLPQNLGSN SPLKWLDLST
     NQFTGDIPAS LCEKGELEEL LMLYNSFTGS IPESLSECRS LTRVRLSNNN LSGEVPVGFW
     GLPHIHLLEL SGNSLSGNIA KTIASAANLS MLLISKNKFE GNIVEEIGFL SNLEQFSASE
     NKLSGSLPDS IVNLLQLGIL DLHSNQLSGE LPPGIQSWKK LNELNLANNQ ISGKIPDQIG
     SLSVLNYLDL SGNRLSGSVP VSLQNLKLNQ LNLSNNDLSG DLPPMFVKEM YRSSFLGNLG
     LCGDLAGLCD STSEDKNRGY VWLLRCIFIL AALVFVGGVA WFYFKYRDFN KARAFDKSKW
     TLMSFHKLGF SEYEILDLLD EDNVIGSGAS GKVYKVVLGN GEAVAVKKLW GGVKKDIQTG
     DIEKGQVHDD GFQAEVETLG KIRHKNIVKL WCCCTTRDCK LLVYEYMPNG SLGDLLHSSK
     GGLLDWPTRY KIIVDAAEGL SYLHHDCVPP IVHRDVKANN ILLDGDFGAR VADFGVAKAV
     DSTGKGLKSM SVIAGSRGYI APEYAYTLRV TEKSDTYSFG VVILELVTGK LPVDPEFGEK
     DLVKWVCTTL DQKGVDHVLD PRLDTCFKEE TCMVLNIGLL CTSPLPINRP TMRRVVKMLL
     EIGGDNLSKT VKKDGKLTPC YYDDA
//
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