ID D2A3P7_TRICA Unreviewed; 1561 AA.
AC D2A3P7;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=AUGUSTUS-3.0.2_15731 {ECO:0000313|EMBL:EFA05543.2};
GN ORFNames=TcasGA2_TC015731 {ECO:0000313|EMBL:EFA05543.2};
OS Tribolium castaneum (Red flour beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA05543.2, ECO:0000313|Proteomes:UP000007266};
RN [1] {ECO:0000313|EMBL:EFA05543.2, ECO:0000313|Proteomes:UP000007266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA05543.2,
RC ECO:0000313|Proteomes:UP000007266};
RX PubMed=18362917; DOI=10.1038/nature06784;
RG Tribolium Genome Sequencing Consortium;
RA Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT "The genome of the model beetle and pest Tribolium castaneum.";
RL Nature 452:949-955(2008).
RN [2] {ECO:0000313|EMBL:EFA05543.2, ECO:0000313|Proteomes:UP000007266}
RP GENOME REANNOTATION.
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA05543.2,
RC ECO:0000313|Proteomes:UP000007266};
RX PubMed=19820115; DOI=10.1093/nar/gkp807;
RA Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT for Tribolium castaneum.";
RL Nucleic Acids Res. 38:D437-D442(2010).
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};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
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DR EMBL; KQ971348; EFA05543.2; -; Genomic_DNA.
DR STRING; 7070.D2A3P7; -.
DR EnsemblMetazoa; TC015731_001; TC015731_001; TC015731.
DR eggNOG; KOG0926; Eukaryota.
DR HOGENOM; CLU_001832_0_0_1; -.
DR InParanoid; D2A3P7; -.
DR OMA; FERYWAQ; -.
DR Proteomes; UP000007266; Linkage group 6.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR CDD; cd17982; DEXHc_DHX37; 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 InterPro; IPR021777; SANBR_BTB.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF99; ATP-DEPENDENT RNA HELICASE DHX37-RELATED; 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 Pfam; PF11822; SANBR_BTB; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000313|EMBL:EFA05543.2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007266}.
FT DOMAIN 762..928
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 957..1173
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 364..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 574..601
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 373..395
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1561 AA; 177651 MW; 4AFF47596AF1FD16 CRC64;
MKKDFVCNQK LLVEKMGYFA EVTTGQRLED MDISVHCDIG IFEWLMKWVK KESLLEEDWP
QLDPQCVIPI LVSAAFLQME PLQNDCLLYC HQHMNEILRT STNLSCLNDS ILTRLAAMYT
NSEVEAIKDR KDKIQSRIFT KLIQSLAEPE PESMRGHWSS LARVYRCGRC QQLIGPSVAT
RIPCAPPCMQ LQCDGSIISQ HVRDPSWNIN DYILKLYKNL KTWRKVYWRL WGDSHFLYCL
TYPPQYFTLD AQKAPLPVGR YPCCGERAYR FQLLQDYSGC QFREHTISAK DVRDSAVLSL
LENFRGLIEE EPPQLMFPER LTRLVARDPA GDSKKLVCKE NFWWEGFQIV PPRPKLGLLG
QFASRGGEEA VPEEESSEGT DESTSDSDDS DSEGSDGSAE SNPPPMPVKN LKKKRNKRES
RLWQHNLSAR SNQDIQRAFE ENAVREITAM LNRRTVTISE GGAKSGRFSR NVTPIGGVWV
RLESEWKEVH CANNNQQKMR MRLLEINNKM VKKRYNWKSR QVVNTVVDNS ATKKIQLDLQ
VEGHYDQSNE LVLPSKKRKT KIKDEKQKIT KILSKKHRKK LEKIVEKKKK KENRASLLEA
LSKVQATPEE LTKLTSIATV QTKGLKRHYL EEQTGDKKKP KRDLQIISGE IKLNSLSGAK
RRQLLEQTVD TKPNGDPNVV GFESSDSGND SDPEPTKNEP TETEPEPKEP PIKNEPKETK
TKTPTRKVLA PKPAVFVDVI RDEEIQNSRL KLPILAEEQQ IMETINENPV VIIAGETGSG
KTTQVPQFLY EAGYALKKQI AVTEPRRVAA IAMSKRVAQE MNLSSNEVSY LIRFEGNATE
DTKIKFMTDG VLLKEVQNDF LLSQYSVVIL DEAHERSVYT DILIGLLSRI VPLRVKRGDP
LKLIIMSATL RVEDFTKNKR LFKKTPPVIN VDSRQFPVTV HFNKRTNEDY LSESFTKVVK
IHTKLPEGGV LVFVTGQQEV NSLVKKLRAK FPFKVKLNEE AEPTKLKQKK VYAPEVNLDD
YDPDWSSESE EEESERPLYH APPLWVLPLY SMLPTHKQNR VFQAPPPGCR LCVVSTNVAE
TSLTIPNIKY VVDSGRTKVK LYDKITGVSS YVVTWTSKAS ANQRAGRAGR TGPGHCYRLY
SSAVFNDTLH DFCVPEIQQK PVDDLYLQMK CMSIDKVVNF PFPTAPDLLQ LKTAEHRLEI
LGALQNSQVT PLGRAIAKFP VLPRFGKMLA LSHQQDLLPY TICMVAALSV QEVLLDDAKW
AALRRQWAAT GNSLLLGDSM VLLRAVGAAE FANTQNRLEQ FCHANGLRHK AVLEIRKLRL
QLTNEIKANV PEADVVVDPA LAPPTDLQAK LLRQILLAGM GDQIAKKIES EDKKFKYGYQ
ANNMEDPVFL HSGSVLRKNL PEFVIYHEIY ETNKIYMRGV TAIEPEWLPV YVPSLCNLSE
PLAEPEPRLK NGKVYCTVNG TFGSQGWTLP NVEIEYPRTI NYYKWFGRFL LEGLVFKKLE
KYKDVLLSQP AIMVKSWAKL QPRTDAILKA LLSKEAVSKQ RLAEIWTDTP KCGCRSRPME
K
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