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Database: UniProt
Entry: U4UY31_DENPD
LinkDB: U4UY31_DENPD
Original site: U4UY31_DENPD 
ID   U4UY31_DENPD            Unreviewed;       885 AA.
AC   U4UY31;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=D910_12497 {ECO:0000313|EMBL:ERL95230.1};
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:ERL95230.1, ECO:0000313|Proteomes:UP000030742};
RN   [1] {ECO:0000313|EMBL:ERL95230.1, 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001556};
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DR   EMBL; KB632411; ERL95230.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4UY31; -.
DR   STRING; 77166.U4UY31; -.
DR   Proteomes; UP000030742; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   CDD; cd17974; DEXHc_DHX16; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030742}.
FT   DOMAIN          260..424
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          449..622
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          117..144
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        7..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   885 AA;  102506 MW;  A5C565359C9B624E CRC64;
     MSKAKKSRKR YESDSESSID SEEEARRKDL RERDEFAERL KKKDEEKTRN IVHASDRRAY
     EEAAKRLQLQ NAEREKIIPK LRVESRRKYL EKRKEDKLLE LEADIVDDEY LFEEQILTER
     ERKEREHKKE LLKLAQEHEK ARELERVQRY HMPRDLGKDS TSDYIEVDEL EKVPQSEQKK
     WEKDQMASAV FKFGAKDAVK RDEYELLLED QIDFIQALQM PGIKDKMKRE PELSEFEKKK
     LTIAETKKSL PIFPFRDDLI QAVREHQVLI IEGETGSGKT TQIPQYLHEA GFTENEKKIG
     CTQPRRVAAM SVAARVAQEM DVKLGNEVGY AIRFEDCTSE RTVIKYMTDG TLHREFLSEP
     DLQSYSVMII DEAHERTLHT DILFGLVKDI ARFRPDLKLL ISSATLDAQK FSEFFDEAPI
     FRIPGRRFPV DIYYTKAPEA DYVDACVISV LQIHVTQPLG DVLVFLTGQD EIETCQELLQ
     DRLRRLGSKV RELIILPVYA NLPSDMQAKI FEATPRGARK VVLATNIAET SLTIDNIIYV
     IDPGFAKQNY FNSKTGMESL MVVPISKASA NQRAGRAGRV AAGKCFRLYT AWSYKHELEE
     NTVPEIQRIN LGNAVLMLKA LGINDLIHFD FLDPPPHETL VLALEQLYAL GALNHHGELT
     RLGRRMAEFP VDPMMAKMLL AAEKYKCAEE IVSITAMLSV NGAIFYRPKD KIIHADTARK
     NFYHPGGDHL TLLNVYNQWR DTDYSLQWCY ENFIQSMKRA RDVREQLVGL MQRVEIEMVS
     SISETTDIRK AITAGYFYHI ARLSKAGNYK TTVTVHPNSS LFEELPRWVL YHELVFTSKE
     FMRQVIEIES KWLLEVAPHY YKPKELEDST NKKLPKTVGR SERTD
//
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