DBR1_DROPS
ID DBR1_DROPS Reviewed; 537 AA.
AC Q29FE1;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Lariat debranching enzyme;
DE EC=3.1.-.-;
GN Name=DBR1; ORFNames=GA20707;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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; CH379067; EAL31314.2; -; Genomic_DNA.
DR AlphaFoldDB; Q29FE1; -.
DR SMR; Q29FE1; -.
DR STRING; 7237.FBpp0277984; -.
DR eggNOG; KOG2863; Eukaryota.
DR HOGENOM; CLU_005893_0_0_1; -.
DR InParanoid; Q29FE1; -.
DR OMA; GIDDPLC; -.
DR Proteomes; UP000001819; Genome assembly.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008419; F:RNA lariat debranching enzyme activity; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Hydrolase; mRNA processing; Nucleus; Reference proteome.
FT CHAIN 1..537
FT /note="Lariat debranching enzyme"
FT /id="PRO_0000250368"
FT REGION 242..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 59528 MW; 4A5B3458C0B6EE02 CRC64;
MKIAIEGCAH GELERIYDTI ACIEKESNTK IDLLLCCGDF QSTRNLEDLQ TMAVPKKYLD
ICTFYKYYSG ECVAPVLTIF IGGNHEASNY LQELPYGGWV APNIYYLGYA GVVNVNGVRI
AGISGIYKGH DFLRGHHEFP PYTESTCRSV YHVRQLEVFR LKQLSGKIDI FLSHDWPTGI
YEYGNKAQLL RKKPYFAADM ESGQLGSRPL EELLKAVQPS YWFAAHLHCK FAALVPHQNA
TKAPTKMGDG SSSSSSSSSS ESDDEESTSR LPPKPVAVTK FLALDKCLPR RAFLQVLDIP
SEAIEGNPTF EYDAEWLVIL QSTNHLISVK ENYYYLPGKK AGAIAERFNF TPTEEELDSL
TTKFQSLKIP ENFQRTVPAF DPQEQSNYKH MVVGQPTAHL NPQSNTFCSV LGVDDPLCLA
LLANGKDLPA VADQCQDQEP IEGSSPPPEP LVTPSKRKLN LFLPAPTVTA DATAAEKDDS
VIDLPEEDED PKTAETAESE AVDNPKVKAV PPPPSSPPSV KKLKRRNQNI YQAEDDD