ID U4UQ62_DENPD Unreviewed; 859 AA.
AC U4UQ62;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ERL92165.1};
GN ORFNames=D910_09485 {ECO:0000313|EMBL:ERL92165.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL92165.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL92165.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. PKD subfamily. {ECO:0000256|ARBA:ARBA00008582}.
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DR EMBL; KB632313; ERL92165.1; -; Genomic_DNA.
DR AlphaFoldDB; U4UQ62; -.
DR Proteomes; UP000030742; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd20795; C1_PKD_rpt1; 1.
DR CDD; cd20796; C1_PKD_rpt2; 1.
DR CDD; cd01239; PH_PKD; 1.
DR CDD; cd14082; STKc_PKD; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR015727; Protein_Kinase_C_mu-related.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22968; PROTEIN KINASE C, MU; 1.
DR PANTHER; PTHR22968:SF24; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 2.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000030742};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 119..169
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 245..295
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 388..505
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 534..830
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 181..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 859 AA; 97015 MW; 55D837994A3F871C CRC64;
MLQLNLQTSS QLNMDDLGPE VTFMFQFGFI KDAITVPQST LNLKTIKDLA CDFLNSKVPD
HGINKLDDRL LLFKHEYSSS NILQVINSAS DIVDGTLIEI VVTAKVPNVQ HSEVTIVRPH
ALSVHSYKTP TFCDFCGEML FGLVRQGLKC DGCGQNYHKR CVVKVPNNCS FMLYEGNKSE
RRRSANLQVP RSPSGGSNTS LASGNSTQTE DSGLISQHGH NRSPSLGGRS TWLDRDVPCR
VLRIPHTFVI HSYTRPTVCQ HCKKLLKGLF KQGLQCKDCN YNVHKKCLEK VPKDCTGELP
RDSQGQFDYA ESSGSDSQTN LTLAEDDESE KNSCYGQENG STKYIEVIPV HDDDNDYSPS
TSSSSPSANI PLQRIVQSVK HTKRRGSKII KEGWLVHFTN KDRTVRRHFW RLDTKSLVLF
QSDTSTKYYK EIPLSEILTI DTARIKQGDV MHCFEIRTAN VDYFVGQDPL HELQDGNNVN
LPPPDSGIGA YLSKSWETTI RQAMLPVTGN SGKPDEMSSQ SEEQITDMSQ IYQIYPDEVL
GSGQFGIVYG GVHRRTGRSV AIKVIDKLRF PTKQEAQLKN EVAILQNLSH SGVVNLERMF
ETPERIFVVM EKLKGDMLEM ILSHEKGRLT ERVTKFLITQ ILVALKHLHS KNIVHCDLKP
ENVLLNSDAE YPQVKLCDFG FARIIGEKSF RRSVVGTPAY LAVLDIIKGD EPVGEVISRA
FRLRLVQPVD PLSSHKYIMS STAVDETNKG YNRSLDMWSV GVIVYVSLSG TFPFNEDEDI
NDQIQNAAFM YPPNPWKEIS SDAIDLINNL LQVKQRKRYT VDKSLQHVWL QAWCDLRSLE
NQINVRYLTH ESDDARWEK
//