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Database: UniProt
Entry: U4UQ62_DENPD
LinkDB: U4UQ62_DENPD
Original site: U4UQ62_DENPD 
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
//
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