ID U520_DROME Reviewed; 2142 AA. AC Q9VUV9; Q5U0X1; Q8T9I9; DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 4. DT 27-MAR-2024, entry version 166. DE RecName: Full=U5 small nuclear ribonucleoprotein 200 kDa helicase {ECO:0000250|UniProtKB:O75643}; DE EC=3.6.4.13 {ECO:0000250|UniProtKB:O75643}; DE AltName: Full=Protein lethal (3) 72Ab; GN Name=Brr2 {ECO:0000312|FlyBase:FBgn0263599}; Synonyms=l(3)72Ab; GN ORFNames=CG5931 {ECO:0000312|FlyBase:FBgn0263599}; 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; 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] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1212-2130. RC STRAIN=Berkeley; TISSUE=Ovary; RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., RA Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, CC an essential step in the assembly of a catalytically active spliceosome CC (By similarity). Plays a role in pre-mRNA splicing (By similarity). CC {ECO:0000250|UniProtKB:O75643}. 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:0000250|UniProtKB:O75643}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75643}. CC -!- DOMAIN: Composed of two similar domains. CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAL39415.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AE014296; AAF49564.4; -; Genomic_DNA. DR EMBL; BT016121; AAV37006.1; -; mRNA. DR EMBL; AY069270; AAL39415.1; ALT_INIT; mRNA. DR RefSeq; NP_648818.3; NM_140561.4. DR AlphaFoldDB; Q9VUV9; -. DR SMR; Q9VUV9; -. DR BioGRID; 65049; 19. DR IntAct; Q9VUV9; 7. DR MINT; Q9VUV9; -. DR STRING; 7227.FBpp0075282; -. DR PaxDb; 7227-FBpp0075282; -. DR DNASU; 39737; -. DR EnsemblMetazoa; FBtr0075527; FBpp0075282; FBgn0263599. DR GeneID; 39737; -. DR KEGG; dme:Dmel_CG5931; -. DR AGR; FB:FBgn0263599; -. DR CTD; 39737; -. DR FlyBase; FBgn0263599; Brr2. DR VEuPathDB; VectorBase:FBgn0263599; -. DR eggNOG; KOG0951; Eukaryota. DR GeneTree; ENSGT00940000154966; -. DR HOGENOM; CLU_000335_2_1_1; -. DR InParanoid; Q9VUV9; -. DR OMA; QTEIQYY; -. DR OrthoDB; 57056at2759; -. DR PhylomeDB; Q9VUV9; -. DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway. DR Reactome; R-DME-72165; mRNA Splicing - Minor Pathway. DR SignaLink; Q9VUV9; -. DR BioGRID-ORCS; 39737; 0 hits in 1 CRISPR screen. DR ChiTaRS; l(3)72Ab; fly. DR GenomeRNAi; 39737; -. DR PRO; PR:Q9VUV9; -. DR Proteomes; UP000000803; Chromosome 3L. DR Bgee; FBgn0263599; Expressed in eye disc (Drosophila) and 25 other cell types or tissues. DR Genevisible; Q9VUV9; DM. DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase. DR GO; GO:0005634; C:nucleus; IDA:FlyBase. DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase. DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; IPI:FlyBase. DR GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; ISS:FlyBase. DR GO; GO:0000278; P:mitotic cell cycle; HMP:FlyBase. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:FlyBase. DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:FlyBase. DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase. DR GO; GO:0000388; P:spliceosome conformational change to release U4 (or U4atac) and U1 (or U11); IBA:GO_Central. DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase. DR CDD; cd18019; DEXHc_Brr2_1; 1. DR CDD; cd18021; DEXHc_Brr2_2; 1. DR CDD; cd18795; SF2_C_Ski2; 2. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2. DR Gene3D; 2.60.40.150; C2 domain; 2. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4. DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2. DR InterPro; IPR041094; Brr2_helicase_PWI. DR InterPro; IPR048863; BRR2_plug. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004179; Sec63-dom. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1. DR PANTHER; PTHR47961:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1. DR Pfam; PF21188; BRR2_plug; 1. DR Pfam; PF00270; DEAD; 2. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF18149; Helicase_PWI; 1. DR Pfam; PF02889; Sec63; 2. DR PIRSF; PIRSF039073; BRR2; 1. DR SMART; SM00487; DEXDc; 2. DR SMART; SM00490; HELICc; 2. DR SMART; SM00973; Sec63; 2. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4. DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2. DR PROSITE; PS51194; HELICASE_CTER; 2. PE 2: Evidence at transcript level; KW ATP-binding; Helicase; Hydrolase; mRNA processing; mRNA splicing; KW Nucleotide-binding; Nucleus; Reference proteome; Repeat; Spliceosome. FT CHAIN 1..2142 FT /note="U5 small nuclear ribonucleoprotein 200 kDa helicase" FT /id="PRO_0000102089" FT DOMAIN 490..673 FT /note="Helicase ATP-binding 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 684..917 FT /note="Helicase C-terminal 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT DOMAIN 981..1286 FT /note="SEC63 1" FT DOMAIN 1337..1511 FT /note="Helicase ATP-binding 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 1544..1752 FT /note="Helicase C-terminal 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT DOMAIN 1811..2128 FT /note="SEC63 2" FT REGION 52..74 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 211..234 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 366..396 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 615..618 FT /note="DEIH box" FT MOTIF 1453..1456 FT /note="DELQ box" FT COMPBIAS 368..392 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 503..510 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT BINDING 1350..1357 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" SQ SEQUENCE 2142 AA; 244510 MW; 10CFE9E84438F2BE CRC64; MADAAARQLQ YEYKANSNLV LQADVRLIER PRRDEATGEV CSLVGKLDGT RMGDRYQRTK PEKTEERKVK RQKRDEAQYD FERMKGATLL SEGIDEMVGI VYRPKTQETR QTYEVLLSFI QEALGDQPRD ILCGAADEIL AVLKNDRLKD RERKKDIDSL LGAVTDERFA LLVNLGKKIT DFGSDAVNAL TAAPNNEEQI DETYGINVQF EESEEESDND MYGEIRDDDA QDEGEEARID HTLHAENLAN EEAANNVKKE RSLHPLDIDA YWLQRCLSKF YKDAMVSQSK AADVLKILKD AADDRDCENQ LVLLLGYDCF DFIKQLKLNR QMVLYCTMLA SAQTDSERQR IREKMRGNSA LAKILRQLDT GKSEDQEEGE ARGSKRGKGD AEDGGAAAAG QVAGVRQLLE LEEMAFTQGS HFMANKRCQL PDGSYRKQRK GYEEVHVPAL KPVPFDANEE LQPVDKLPKY VQPVFEGFKT LNRIQSRLYK AALDSDENML LCAPTGAGKT NVALLTMMRE IGKHINEDGT INAQDFKIIY VAPMKSLVQE MVGNFGRRLA CYNLTVSELT GDHQLTREQI AATQVIVCTP EKWDIITRKG GERTFVSLVR LVIIDEIHLL HDERGPVLEA LVARTIRNIE TTQEEVRLVG LSATLPNYQD VATFLRVKPD KGLFYFDNSY RPVSLEQQYI GVTEKKALKR FQVMNEIVYE KTMEHAGRNQ VLVFVHSRKE TGKTARAVRD MCLEQDTLGS FLKEGSASME VLRTEAEQVK NTELKELLPY GFAIHHAGMT RVDRTLVEDL FADRHIQVLV STATLAWGVN LPAHTVIIKG TQVYNPEKGR WVELSALDVL QMLGRAGRPQ YDTKGEGILI TNHSELQFYL SLLNQQLPIE SQFISKLPDM LNAEIVLGTV QHLQDAVNWL GYTYLYIRML RNPTLYGVSH DAIKADPLLE QHRADLLHTA ACCLERSGLI KYDRKTGHFQ VTDLGRIASH YYLTHETMLT YNQLLKQTLS EIELFRVFSL SSEFRHISVR EEEKLELQKL MERVPIPIKE SIEEHSAKVN VLLQAYISQL KLEGFALMSD MVFITQSAAR LMRAIFEIVL TRGWAQLADK TLTLCKMIDR RMWQSMTPLR QFKKMPDEIA KKLEKKHFPW GRLYDLEPHE LGELIRVPKL GKTIHKFVHQ FPKLELSTHI QPITRGTLRV ELTITPDFQW DEKVHGQSEG FWVLIEDVDS ELILHHEFFL LKQKYSQDEH QLKFFVPVFE PLPPQYFLRI VSDRWIGAET QLPVSFRHLI LPEKNMPPTE LLDLQPLPIS ALRQPKFESF YSQRFPQFNP IQTQVFNAVY NSDENVFVGA PTGSGKMTIA EFAIMRLFTT QSDARCVYLV SEEALADLVF ADWHSKFGSL DIKVVKLTGE TGTDLKLIAK GQLVITTADK WDVLSRRWKQ RKNVQLVNLF IVDELQLVGG EEGPVLEIVC SRMRYISSQI EKQIRIVALS ASLTDARDVA QWLGCNPNAT FNFHPSVRPI PLELHIQGYN VTHNATRIAT MSKPVYNAIL KYSAHKPVIV FVSSRKQARL TAIDVLTYAA SDLQPNRFFH AEEEDIKPFL ERMTDKTLKE TLAQGVAYLH EGLSASDHRL VEQLFDSGAV QVAVISRDLC WGMSISAHLV IIMDTQFYNG KNHSYEDYPI TDVLQMIGRA NRPNEDADAK CVLMCQSSKK DFFKKFINEP LPIESHLDHR MHDHFNAEVV TKTIENKQDA VDYLTWTFLY RRLTQNPNYY NLQGVTHRHL SDHLSELVEN TLSDLEQSKC ISVEDDMDTL PLNLGMIAAY YYINYTTIEL FSLSLNSKTK VRGLLEIISS AAEYEDVVVR HHEEQVLRTL SQRLPNKLTG PNETAPKFND PHIKTNLLLQ AHLSRLQLGP ELQGDTEQIL SKAIRLIQAC VDVLSSNGWL SPAVAAMELA QMVTQAMWSK DSYLKQLPHF SPEIVKRCTE KKIETVFDIM ELEDEDRTRL LQLSDLQMAD VARFCNRYPN IELNYEVVDK DRINSGSTVN VVVQLEREDE VTGPVIAPFF PQKREEGWWV VIGDPKTNSL LSIKRLTLQQ KAKVKLDFVA PSPGKHDYTL YYMSDSYLGC DQEYKFSIEV GDFQSESESE SD //