ID DHX33_DROME Reviewed; 694 AA. AC Q9VL25; Q8MYY2; DT 14-DEC-2022, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 2. DT 14-DEC-2022, entry version 183. DE RecName: Full=ATP-dependent RNA helicase DHX33; DE EC=3.6.4.13; DE AltName: Full=DEAH box protein 33 homolog {ECO:0000305}; DE AltName: Full=Protein athos {ECO:0000305}; GN Name=ath {ECO:0000312|FlyBase:FBgn0032194}; GN Synonyms=cg4901 {ECO:0000312|EMBL:AAF52873.2}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAF52873.2, ECO:0000312|Proteomes:UP000000803}; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., RA Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP GENOME REANNOTATION. RC STRAIN=Berkeley; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] {ECO:0000312|EMBL:AAM29496.1} RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM29496.1}; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M., RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A., RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S., RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP FUNCTION, DISRUPTION PHENOTYPE, AND RNA-BINDING. RX PubMed=35413237; DOI=10.1016/j.devcel.2022.03.005; RA Martin E.T., Blatt P., Nguyen E., Lahr R., Selvam S., Yoon H.A.M., RA Pocchiari T., Emtenani S., Siekhaus D.E., Berman A., Fuchs G., Rangan P.; RT "A translation control module coordinates germline stem cell RT differentiation with ribosome biogenesis during Drosophila oogenesis."; RL Dev. Cell 57:883-900.e10(2022). CC -!- FUNCTION: Part of a translational control module, also containing CC pths/DDX47 and ais/DDX52, which coordinates germline stem cell CC differentiation with ribosome biogenesis during oogenesis. This module CC allows for coregulation of ribosomal proteins and non1/GTPBP4, a p53 CC repressor, preventing p53 stabilization, cell cycle arrest and loss of CC stem cell differentiation. {ECO:0000269|PubMed:35413237}. 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 -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:35413237}. CC -!- DISRUPTION PHENOTYPE: Mutants show hypotrophy of the nucleolus. CC {ECO:0000269|PubMed:35413237}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014134; AAF52873.2; -; Genomic_DNA. DR EMBL; AY113491; AAM29496.1; -; mRNA. DR EMBL; AE014134; API64983.1; -; Genomic_DNA. DR EMBL; AE014134; API64984.1; -; Genomic_DNA. DR RefSeq; NP_001334733.1; NM_001347805.1. DR RefSeq; NP_001334734.1; NM_001347806.1. DR RefSeq; NP_609356.2; NM_135512.4. DR AlphaFoldDB; Q9VL25; -. DR SMR; Q9VL25; -. DR STRING; 7227.FBpp0079537; -. DR DNASU; 34357; -. DR EnsemblMetazoa; FBtr0079947; FBpp0079537; FBgn0032194. DR EnsemblMetazoa; FBtr0445414; FBpp0401582; FBgn0032194. DR EnsemblMetazoa; FBtr0445415; FBpp0401583; FBgn0032194. DR GeneID; 34357; -. DR KEGG; dme:Dmel_CG4901; -. DR UCSC; CG4901-RA; d. melanogaster. DR AGR; FB:FBgn0032194; -. DR FlyBase; FBgn0032194; CG4901. DR VEuPathDB; VectorBase:FBgn0032194; -. DR eggNOG; KOG0924; Eukaryota. DR GeneTree; ENSGT00940000156747; -. DR HOGENOM; CLU_001832_5_11_1; -. DR OMA; HIHRTTP; -. DR OrthoDB; 354219at2759; -. DR BioGRID-ORCS; 34357; 0 hits in 1 CRISPR screen. DR GenomeRNAi; 34357; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0032194; Expressed in embryonic/larval hemocyte (Drosophila) and 44 other tissues. DR GO; GO:0005730; C:nucleolus; IDA:FlyBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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; ISS:FlyBase. DR GO; GO:0019843; F:rRNA binding; IDA:FlyBase. DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IBA:GO_Central. DR GO; GO:0022414; P:reproductive process; IEA:UniProt. DR GO; GO:0042254; P:ribosome biogenesis; IMP:FlyBase. DR Gene3D; 3.40.50.300; -; 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; IPR007502; Helicase-assoc_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF04408; HA2; 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 1: Evidence at protein level; KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus; KW Reference proteome; RNA-binding. FT CHAIN 1..694 FT /note="ATP-dependent RNA helicase DHX33" FT /id="PRO_0000456957" FT DOMAIN 78..246 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 270..443 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT MOTIF 188..191 FT /note="DEAH box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT BINDING 91..98 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" SQ SEQUENCE 694 AA; 78319 MW; C363A4C0BAD608DE CRC64; MDSKYFATSR NDAVGPSPVK FSFKRKYDAM ANSPILEKKP HVAQIKQTIA PILLTSKRTS IEQQQKSLPV FNCRHRILKE LEANDTVLIM SETGSGKTTQ IPQFLLLAGY AKNGMIGITQ PRRVAAITVA RRVAQELNGT IGDTVGYTVR FEDVTSRATK IRFLTDGVLL RESIKDRLLL KYSVIILDEA HERTVNADLL FGIVKDAQKE RRKQKLANLK VVVTSATMDI DHFGNYFNCK GMYLEGRTYP VRVMHTKEEH EDYIHTVLVT LFHIHRTTPK NHDVLIFLTG QEEIESLAQQ IRQLAKIDTT GTTDLRVFTL YAQLSQGKQL ECFVPTPANV RKVILATNIA ETSITIPGIR CVIDCGFVKE KSFNTVDGLD VLKSVRISKA QAWQRAGRAG RDADGTCYRA YTKAEMDSFA DATQPEILRT NPTSMVLQLL ALDIDCNNFD FLDPPLEDGL RSAYKSLDAL GAIKTGDDSY ITPLGRQMVQ YPLDPKYSKL LLTASSFGCM EEILSLVSVL SSDHVFVSNS EKNEMAALAH AKFQSKHGDH LTLLNVFNGF LKSEKPKMWC HDNYLNLRSL TYARNVRRQL REISEHLHLA LNSSDDIEML KKCILNGFFE NIAVLQRDGF YITASGNIRS KIHPSSVLHG KYKPSYILFT EIVQTEQTFL RQVTEISIEW IKEVVPFVKN IPTR //