ID   DBR1B_XENLA             Reviewed;         533 AA.
AC   Q7ZWU9;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Lariat debranching enzyme B;
DE            EC=3.1.-.-;
GN   Name=dbr1-b;
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 (FEB-2003) 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; BC046698; AAH46698.1; -; mRNA.
DR   RefSeq; NP_001080368.1; NM_001086899.1.
DR   AlphaFoldDB; Q7ZWU9; -.
DR   SMR; Q7ZWU9; -.
DR   DNASU; 380060; -.
DR   GeneID; 380060; -.
DR   KEGG; xla:380060; -.
DR   CTD; 380060; -.
DR   Xenbase; XB-GENE-6256598; dbr1.S.
DR   OrthoDB; 1047278at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 380060; 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..533
FT                   /note="Lariat debranching enzyme B"
FT                   /id="PRO_0000250363"
FT   REGION          392..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          468..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..441
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..504
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   533 AA;  60593 MW;  7AFC5F201E9EB43A CRC64;
     MKIAVEGCCH GELDKIYETI QFLEKKENTK VELLLCCGDF QAVRNEGDMK CMAVPVKYRQ
     MQTFYKYYSG EKKAPILTIF IGGNHEASNY LQELPYGGWV APNIYYMGYA GVVKYRGVRI
     GGISGIFKSH DYRKGHFERL PYGKDTVRSA YHVRSIEVFK LKQLKEPMDI FLSHDWPRSI
     YHYGNKKQLL KKKDFFRQEV EDNTLGSPAA SELLLHIQPS YWFSAHLHVK FAAFMQHQTN
     VDGEIPKATK FLALDKCLPR REFLQIVDVE HDSAKSECLE YDLEWLSVLK ATKDLLNITP
     NTWNMPENNG LHSRWDFSAS EETKREVVSD LGHDLKIPCN FSMTTACYDP NNPQYKRVAT
     HIVNPQTTEF CARLGLVDLN AKICQNEEEN FDIAEDNEAD SIGSAEDPGE YSTDTSVLST
     SVNPDEITLE DDDDQEDEGM EDKLGEPSPE YTPDLSINLS KIRVLPDSMA VSSDDATDST
     NDELDRSESS QTEGEGKPSN RPLKRISDEN GSGGVKIKRR NQAIYQAKDD EDE