DBR1_CHICK
ID DBR1_CHICK Reviewed; 536 AA.
AC Q5ZLM2;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Lariat debranching enzyme;
DE EC=3.1.-.-;
GN Name=DBR1; ORFNames=RCJMB04_5i14;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ719712; CAG31371.1; -; mRNA.
DR RefSeq; NP_001026737.1; NM_001031566.1.
DR AlphaFoldDB; Q5ZLM2; -.
DR SMR; Q5ZLM2; -.
DR STRING; 9031.ENSGALP00000001803; -.
DR PaxDb; Q5ZLM2; -.
DR GeneID; 429118; -.
DR KEGG; gga:429118; -.
DR CTD; 51163; -.
DR VEuPathDB; HostDB:geneid_429118; -.
DR eggNOG; KOG2863; Eukaryota.
DR HOGENOM; CLU_005893_0_2_1; -.
DR InParanoid; Q5ZLM2; -.
DR OrthoDB; 1047278at2759; -.
DR PhylomeDB; Q5ZLM2; -.
DR TreeFam; TF313221; -.
DR PRO; PR:Q5ZLM2; -.
DR Proteomes; UP000000539; Unplaced.
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..536
FT /note="Lariat debranching enzyme"
FT /id="PRO_0000250360"
FT REGION 388..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..408
FT /note="Acidic residues"
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..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 60777 MW; 3D1D8CF2EB409FB3 CRC64;
MKVAVAGCCH GALDKMYETL ELLQRRHNVR PDLLLCCGDF QAVRNEADLR CMAVPAKYRH
MQTFYRYYSG EKKAPVLTVF IGGNHEASNH LQELPYGGWV APNIYYLGYA GVVRFRGVRI
GGISGIFKSH DYRKGHFECP PYNQQTIRSA YHVRNIEVFK LKQLKHPMDI FMSHDWPQSI
YHYGNKKQLL KMKSFFRQEV ESNTLGSPAA SELLQHLKPN YWFSAHLHVK FAAFMQHETK
SKEELPKATK FLALDKCLPH RDFLQIIDIE HDPTAGDSLE YDAEWIAVLK ATNSLINVTQ
SSWSVPENNG LHAKWDYSAT EEAIKEVLEE LNHNLKIPCN FTLTTTCYDP SKPQKNMEPV
HTINPQTTEF CAQFGLTDIN DRIQQVKEEG SVRGEYEEEE EEMDSSGSAE EPSEYNTDNS
GLSSINPDEI MLDDEGGDED LSTCSVDPSP DHPPEFSASF SDIRIMPDSM AVSSDDAMDS
TNEELEKSGV NKQVEEKSLN ERPLKRVGGS ENGNSGIKIK RRNQAIYAAE DEDEAK