DBR1_XENTR
ID DBR1_XENTR Reviewed; 534 AA.
AC Q6P886;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Lariat debranching enzyme;
DE EC=3.1.-.-;
GN Name=dbr1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-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; BC061343; AAH61343.1; -; mRNA.
DR RefSeq; NP_988947.1; NM_203616.1.
DR RefSeq; XP_012825690.1; XM_012970236.2.
DR RefSeq; XP_012825691.1; XM_012970237.2.
DR AlphaFoldDB; Q6P886; -.
DR SMR; Q6P886; -.
DR STRING; 8364.ENSXETP00000057335; -.
DR PaxDb; Q6P886; -.
DR Ensembl; ENSXETT00000057335; ENSXETP00000057335; ENSXETG00000027491.
DR GeneID; 394544; -.
DR KEGG; xtr:394544; -.
DR CTD; 51163; -.
DR Xenbase; XB-GENE-5851881; dbr1.
DR eggNOG; KOG2863; Eukaryota.
DR HOGENOM; CLU_005893_0_2_1; -.
DR InParanoid; Q6P886; -.
DR OMA; GIDDPLC; -.
DR OrthoDB; 1047278at2759; -.
DR PhylomeDB; Q6P886; -.
DR TreeFam; TF313221; -.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000027491; Expressed in egg cell and 16 other tissues.
DR ExpressionAtlas; Q6P886; differential.
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: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_0000250364"
FT REGION 388..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..441
FT /note="Acidic 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; 60831 MW; A2DA4252CA151592 CRC64;
MKIAVEGCCH GELDKIYETI QFLEKKENTK VDLLLCCGDF QAVRNEGDMK CMAVPQKYRQ
MQTFYKYYSG EKLAPILTIF IGGNHEASNY LQELPYGGWV APNIYYVGYA GVVKYRGVRI
GGISGIFKSH DYRKGHFERP PYSKDTVRSA YHVRNIEVFR LKQLKEPMDI FMSHDWPRSI
YHYGNKKQLL KKKDFFRQEV ENNTLGSPAA SELLLHIQPS YWFSAHLHVK FAAFMQHQTN
VEGEIPKATK FLALDKCLPH REFLQIVDVE HDPGKPDCLE YDLEWLAVLK ATKDLLNITS
KTWNMPENNG LHSRWDFSAS EKTKREILDD LGHDIKIPCN FCMTTACYDP NNPQYKRVAT
HIVNPQTTEF CARLGLVDLN AKIRQHEEEG DIDITEDNEA DSIGSAEDPG EYSTDTSLLS
TSINPDEIAL EDDDDQEDEG MAEKLGEPSP DYTPDLSINF SNIRVLPDSM AVSSDDATDS
TNDELDRSES SQTEGEGKQS NRPLKRMSNE NGSGGVKIKR RNQAIYQAKD DEDE