DBR1_YEAST
ID DBR1_YEAST Reviewed; 405 AA.
AC P24309; D6VX48;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Lariat debranching enzyme;
DE EC=3.1.-.-;
GN Name=DBR1; Synonyms=PRP26; OrderedLocusNames=YKL149C; ORFNames=YKL604;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1850323; DOI=10.1016/0092-8674(91)90466-c;
RA Chapman K.B., Boeke J.D.;
RT "Isolation and characterization of the gene encoding yeast debranching
RT enzyme.";
RL Cell 65:483-492(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091859; DOI=10.1002/yea.320100005;
RA Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT "DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP loci
RT of chromosome XI of Saccharomyces cerevisiae.";
RL Yeast 10:S35-S40(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-117.
RX PubMed=1518827; DOI=10.1073/pnas.89.17.8011;
RA Schuelke N., Blobel G., Pain D.;
RT "Primary structure, import, and assembly of the yeast homolog of succinate
RT dehydrogenase flavoprotein.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8011-8015(1992).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION.
RX PubMed=14716018; DOI=10.1126/science.1087023;
RA Cheng Z., Menees T.M.;
RT "RNA branching and debranching in the yeast retrovirus-like element Ty1.";
RL Science 303:240-243(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Cleaves the 2'-5' phosphodiester linkage at the branch point
CC of lariat intron pre-mRNAs after splicing and converts them into linear
CC molecules that are subsequently degraded. It thereby facilitates
CC ribonucleotide turnover. It also participates in Ty1 retrovirus-like
CC transposition via an RNA lariat intermediate in cDNA synthesis.
CC {ECO:0000269|PubMed:14716018}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1130 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the lariat debranching enzyme family.
CC {ECO:0000305}.
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DR EMBL; M62813; AAA34560.1; -; Genomic_DNA.
DR EMBL; M94874; AAA35025.1; -; Genomic_DNA.
DR EMBL; M86909; AAA35023.1; -; Genomic_DNA.
DR EMBL; Z26877; CAA81504.1; -; Genomic_DNA.
DR EMBL; Z28149; CAA81990.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09014.1; -; Genomic_DNA.
DR PIR; A38491; A38491.
DR RefSeq; NP_012773.1; NM_001179715.1.
DR AlphaFoldDB; P24309; -.
DR SMR; P24309; -.
DR BioGRID; 33988; 204.
DR DIP; DIP-4858N; -.
DR IntAct; P24309; 2.
DR STRING; 4932.YKL149C; -.
DR iPTMnet; P24309; -.
DR MaxQB; P24309; -.
DR PaxDb; P24309; -.
DR PRIDE; P24309; -.
DR EnsemblFungi; YKL149C_mRNA; YKL149C; YKL149C.
DR GeneID; 853708; -.
DR KEGG; sce:YKL149C; -.
DR SGD; S000001632; DBR1.
DR VEuPathDB; FungiDB:YKL149C; -.
DR eggNOG; KOG2863; Eukaryota.
DR GeneTree; ENSGT00510000047481; -.
DR HOGENOM; CLU_005893_1_0_1; -.
DR InParanoid; P24309; -.
DR OMA; GNHESMR; -.
DR BioCyc; YEAST:G3O-31922-MON; -.
DR PRO; PR:P24309; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P24309; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008419; F:RNA lariat debranching enzyme activity; IDA:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:0006401; P:RNA catabolic process; IDA:SGD.
DR GO; GO:0016074; P:sno(s)RNA metabolic process; IMP:SGD.
DR GO; GO:0032197; P:transposition, RNA-mediated; IMP:SGD.
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 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..405
FT /note="Lariat debranching enzyme"
FT /id="PRO_0000079797"
FT REGION 242..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 405 AA; 47741 MW; 437D5325D1D58257 CRC64;
MTKLRIAVQG CCHGQLNQIY KEVSRIHAKT PIDLLIILGD FQSIRDGQDF KSIAIPPKYQ
RLGDFISYYN NEIEAPVPTI FIGGNHESMR HLMLLPHGGY VAKNIFYMGY SNVIWFKGIR
IGSLSGIWKE WDFNKQRPDW NDLENNNWKA NIRNLYHVRI SDIAPLFMIK HRIDIMLSHD
WPNGVVYHGD TKHLLKLKPF FEQDIKEGKL GSPVTWQLLR DLRPQWWLSA HLHVRFMASI
KHNKRSHEPP NKSTSKTKKN NNEIDLDLSS DEDERSGIMN CQEENEYDSK YGETRFLALD
KCLPRRRWLE ILEIEPDTSH ASWKDENHRM FWDPEFINNL VICQKNKNLL SNKPFNSVNW
IELSQSNREE GRDIDWENYA IPAYTLDIQK DEVRQTKAFI SKFMT
