ID A0A1Q3E8H0_LENED Unreviewed; 1047 AA.
AC A0A1Q3E8H0;
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=Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
DE EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
GN ORFNames=LENED_005241 {ECO:0000313|EMBL:GAW03512.1};
OS Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Lentinula.
OX NCBI_TaxID=5353 {ECO:0000313|EMBL:GAW03512.1, ECO:0000313|Proteomes:UP000188533};
RN [1] {ECO:0000313|EMBL:GAW03512.1, ECO:0000313|Proteomes:UP000188533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW03512.1,
RC ECO:0000313|Proteomes:UP000188533};
RG Lentinula edodes genome sequencing consortium;
RA Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA Konno N.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAW03512.1, ECO:0000313|Proteomes:UP000188533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW03512.1,
RC ECO:0000313|Proteomes:UP000188533};
RA Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA Konno N.;
RT "A genome survey and senescence transcriptome analysis in Lentinula
RT edodes.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.21; Evidence={ECO:0000256|RuleBase:RU361162};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000256|RuleBase:RU361162}.
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:GAW03512.1}.
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DR EMBL; BDGU01000149; GAW03512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3E8H0; -.
DR STRING; 5353.A0A1Q3E8H0; -.
DR Proteomes; UP000188533; 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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13118; POLO_box_1; 1.
DR CDD; cd13117; POLO_box_2; 1.
DR CDD; cd14099; STKc_PLK; 1.
DR Gene3D; 3.30.1120.30; POLO box domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033701; POLO_box_1.
DR InterPro; IPR033695; POLO_box_2.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR036947; POLO_box_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00659; POLO_box; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF82615; Polo-box domain; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50078; POLO_BOX; 2.
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:0000256|RuleBase:RU361162};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU361162};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361162};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1026..1046
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 78..333
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 632..700
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT DOMAIN 734..818
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT REGION 17..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1047 AA; 115952 MW; 640BDC0C2D6C74E6 CRC64;
MSAQIYPIQT YKPSRVPAKR FPLANAANQQ LPPTATTPQK VHAKPKQPTS PPLQRQNTKA
TPPSPPSIIR DNHGYFQFHR VGFLGEGGFA RVYEAEDFRG TRVACKVVTR SSLTTKKTKT
KLYAEIRIHK SLSHPNIVAF QECFEGDDNV YMILELCTSG SLMDMLRRRR RLSEAETRFF
LVQIIGACHY MHIHQVIHRD LKLGNIFLDG KMNIKVGDFG LAALIENPGE RKKTICGTPN
YIAPEVLFDT ANGHSFEVDT WSIGVILYTL VIGRPPFQTK DVKAIYKRIR DNAYEFPTER
PISQASQQLI QSILAPKPQE RPALLDVVHD DFFTKGAFPP HIPTSAHDVV PDFRAITRSA
SEANFRRVRR AALLDPDQIT SIAVPYVSED LAISSAASDA PTRSVTAAIA QQEKEFQKAV
QPGSPISALL SSAKRPLLRS TGPPGAPGNG VTKESPLFRK LQAVSTSNPP NPSPLRQSSA
TGSSRPVAAH TVNRGLEHIA EEDDRNDELG RKRKNQTKEL EAQKARIVAQ MAPVREEERY
EAGAQDRYED PQPERKEIKR SSVREVKENR FPVPSAPIPE LKAQLAGFDA AAHVLTLAFE
SKAVGQVFRD PREDPRIPLP EEKVFIVSWV DYCNKYGMGY ALTDGSVGVH FNDSSSIVLS
ADKHHFDVIS SRRNGTVFVR KSFTVEEYPE ELQTKVYLLK HFERYIMDRL YGEYDYTFED
TEKTKGMIWV QNYLRMKQVI VFKLSHDVLQ FNFYDHSKII LSSSGLVVTH IDKNSVLTRW
LLSDIMHNAL RAASSTSTAN PDTVKFNQKL VDKLKYCKEV LVSIQTAKTS GSDATPTSNI
PGSTVAKTAM LLPKRISSRG RALISLVLVC IFSQVSSYFI INEPDSSSQW SNGASNLISW
TKGLEDGIDA FDVELARLTD DGLIFVARDV PCAKGDTSAL NIYLQDVPAA NDYFLLFLNS
TPGTMYATSS RFTILDSSTS ANASQPSTNP SAATVTVSGS PNPTQLFATT FALANGSPVL
ISDMGYIAVG LGSALFSCLL GAAWTLW
//
