ID   DBR1A_XENLA             Reviewed;         534 AA.
AC   Q6GPB8;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Lariat debranching enzyme A;
DE            EC=3.1.-.-;
GN   Name=dbr1-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cleaves the 2'-5' phosphodiester linkage at the branch point
CC       of excised lariat intron RNA and converts them into linear molecules
CC       that can be subsequently degraded, thereby facilitating ribonucleotide
CC       turnover. Linked to its role in pre-mRNA processing mechanism, may also
CC       participate in retrovirus replication and have an antiviral cell-
CC       intrinsic defense function. {ECO:0000250|UniProtKB:Q9UK59}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lariat debranching enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; BC073223; AAH73223.1; -; mRNA.
DR   RefSeq; NP_001085701.1; NM_001092232.1.
DR   RefSeq; XP_018089813.1; XM_018234324.1.
DR   RefSeq; XP_018089814.1; XM_018234325.1.
DR   AlphaFoldDB; Q6GPB8; -.
DR   SMR; Q6GPB8; -.
DR   DNASU; 444127; -.
DR   GeneID; 444127; -.
DR   KEGG; xla:444127; -.
DR   CTD; 444127; -.
DR   Xenbase; XB-GENE-5852074; dbr1.L.
DR   OMA; GIDDPLC; -.
DR   OrthoDB; 1047278at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 444127; Expressed in egg cell and 19 other tissues.
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   2: Evidence at transcript level;
KW   Hydrolase; mRNA processing; Nucleus; Reference proteome.
FT   CHAIN           1..534
FT                   /note="Lariat debranching enzyme A"
FT                   /id="PRO_0000250362"
FT   REGION          386..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  61088 MW;  576ADE1B6FE55E78 CRC64;
     MKIAVEGCCH GELDKIYETI QFLEKKENTK VDLLLCCGDF QAVRNEGDMK CMAVPMKYRQ
     MQTFYKYYSG EKKAPILTIF IGGNHEASNY LQELPYGGWV APNIYYMGYA GVVKYRGVRI
     GGISGIFKSH DYRKGHFERP PYSKDTVRSA YHVRSIEVFK LKQLKEPMDI FLSHDWPRSI
     YHYGNKKQLL KKKDFFRQEV EDNTLGSPAA SELLLHIQPS YWFSAHLHVK FAAFMQHQNN
     VGEIPKATKF LALDKCLPHR EFLQIVDMEH DPSKPECLEY DLEWLAVLKA TKDLLNITSK
     TWNMPENNGL HARWDFSMSE ETKREVLDDL GHDIKIPCNF SVTTACYDPN NPQYKRMPTH
     IVNPQTTEFC ARLGLVDLNV KVRQHEEEKE DFDMTEDNEA DSIGSAEDPG EYSTDTSILS
     TSVNPDEITL EDDDEQEDEG IAEKLGEPSP EYTPDLSVNF SNIRVLPDSM AVSSDDATDS
     TNDELDRSES SQTEGEGKQS NRPLKRMSNE NGSGGVKIKR RNQAIYQAKD DEDE