DBR1_DROME
ID DBR1_DROME Reviewed; 534 AA.
AC Q9VSD7; A4V1M7;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Lariat debranching enzyme;
DE Short=DmDBR1;
DE EC=3.1.-.-;
GN Name=ldbr; Synonyms=DBR1; ORFNames=CG7942;
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;
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: Cleaves the 2'-5' phosphodiester linkage at the branch point
CC of lariat intron pre-mRNAs after splicing and converts them into linear
CC molecules that are subsequently degraded. It thereby facilitates
CC ribonucleotide turnover. It may also participate in retrovirus
CC replication via an RNA lariat intermediate in cDNA synthesis (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lariat debranching enzyme family.
CC {ECO:0000305}.
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DR EMBL; AE014296; AAS65055.1; -; Genomic_DNA.
DR EMBL; AY119584; AAM50238.1; -; mRNA.
DR RefSeq; NP_996022.1; NM_206300.2.
DR AlphaFoldDB; Q9VSD7; -.
DR SMR; Q9VSD7; -.
DR BioGRID; 64323; 4.
DR IntAct; Q9VSD7; 1.
DR STRING; 7227.FBpp0076410; -.
DR PaxDb; Q9VSD7; -.
DR PRIDE; Q9VSD7; -.
DR DNASU; 38900; -.
DR EnsemblMetazoa; FBtr0076687; FBpp0076410; FBgn0035838.
DR GeneID; 38900; -.
DR KEGG; dme:Dmel_CG7942; -.
DR CTD; 38900; -.
DR FlyBase; FBgn0035838; ldbr.
DR VEuPathDB; VectorBase:FBgn0035838; -.
DR eggNOG; KOG2863; Eukaryota.
DR GeneTree; ENSGT00510000047481; -.
DR HOGENOM; CLU_005893_0_0_1; -.
DR InParanoid; Q9VSD7; -.
DR OMA; GIDDPLC; -.
DR OrthoDB; 1047278at2759; -.
DR PhylomeDB; Q9VSD7; -.
DR BioGRID-ORCS; 38900; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 38900; -.
DR PRO; PR:Q9VSD7; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035838; Expressed in egg chamber and 27 other tissues.
DR Genevisible; Q9VSD7; DM.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008419; F:RNA lariat debranching enzyme activity; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; ISS:FlyBase.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; ISS:UniProtKB.
DR CDD; cd00844; MPP_Dbr1_N; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR007708; DBR1_C.
DR InterPro; IPR041816; Dbr1_N.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR Pfam; PF05011; DBR1; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SMART; SM01124; DBR1; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; mRNA processing; Nucleus; Reference proteome.
FT CHAIN 1..534
FT /note="Lariat debranching enzyme"
FT /id="PRO_0000250367"
FT REGION 242..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 534 AA; 59462 MW; 2C5BD9148F60C49B CRC64;
MKIAVEGCAH GELERIYDTI EGIEKVGGTK IDLLLCCGDF QSTRNLEDLQ TMAVPKKYLD
MCSFYKYYSG ELVAPVLTIF IGGNHEASNY LQELPYGGWV APNIYYLGYA GVVNVNGVRI
AGISGIFKGH DFLRGHHEFP PYTDSTCRSV YHVRQLEVFR LKQISGRVDI FLSHDWPTGI
YEYGNKAQLL RKKPFFAADM ESGKLGSQPL EELLKAVQPA YWFAAHLHCK FAALVPHNHS
QKLGDAESSS SSSSSEDEDE EREKVKKAAP VPPPSKSVPV TKFLALDKCL PRRAFLQVVE
VPSDPIEGTP RLEYDAEWLA ILHSTNHLIS VKENYYYLPG KKAGEFTERS NFTPTEEELE
AVTAKFQKLQ VPENFERTVP AFDPAEQSDY KHMFVDQPKV QLNPQSNTFC ATLGIDDPLC
LVLLANGLDL PAVGATECKD RETKSSKLQA VEEDVAEPLV TPTKRKLNLS LPAPTTAAAD
TTDENVIDLP EEEAEEAIIA TETPHVEEPA SVPASPNVKK LKRRNQNIYQ AQED