ID   F1KTN3_ASCSU            Unreviewed;       555 AA.
AC   F1KTN3;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Lariat debranching enzyme {ECO:0000313|EMBL:ADY41237.1};
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY41237.1};
RN   [1] {ECO:0000313|EMBL:ADY41237.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21685128; DOI=10.1101/gr.121426.111;
RA   Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA   Davis R.E.;
RT   "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT   functional diversification, and novel developmental profiles.";
RL   Genome Res. 21:1462-1477(2011).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the lariat debranching enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006045}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JI165677; ADY41237.1; -; mRNA.
DR   AlphaFoldDB; F1KTN3; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008419; F:RNA lariat debranching enzyme activity; IEA:UniProt.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd00844; MPP_Dbr1_N; 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   PANTHER; PTHR12849:SF0; LARIAT DEBRANCHING ENZYME; 1.
DR   PANTHER; PTHR12849; RNA LARIAT DEBRANCHING ENZYME; 1.
DR   Pfam; PF05011; DBR1; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   SMART; SM01124; DBR1; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          279..423
FT                   /note="Lariat debranching enzyme C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01124"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   555 AA;  63092 MW;  DC99A6F1687C6510 CRC64;
     MFQNSIATNA DHSSTSASNI EDQPAIKRSR ISKKLHIAVA GCSHGEMDKI YASLAEIERT
     SGFNFDLLIS CGDYQAVRNY GDLAHMHVSK KYRNLQTFYR YYCGEVKAPI LTIFIGGNHE
     ASGFLQELPN GGWVAPRIFY MGHANVVRFA GLRIAGLSGI FNKHHYDTGH WERPPFHDYG
     GVVSAYHVRS VDVFRLKQLR PRDSSDDKRI DIMVSHDWPA GITEYGDVDE LLKKKPFFRE
     DIKKNALGNP ATMSLLHDIR PRYWLAAHLH CKFAALISHQ VDGDGAVAPE PTRFLSLDKP
     LPRRHFVQAL EFDVDEDAEM CLSYDPVWLA ILKATDSFTD ATKRTTYMPS QCGSSCGERW
     DYRPTEEEVK VVEKLFEDDF RIPENFRRTA PPYDPSQMIE SELYYRNPQT SEFCAKLGIR
     DLNEMLCAQS REALGVPYFL SEMSDAVKDE QQSAVTVDID RKEFDDGCDF VIDRKRRSSP
     IYLENFVAPK LLDSSSKDEK GPGDKEREGY AASDRVEPAA APDEQKEEVL TERRKVGSGI
     FRRRPIGLPE DEEND
//