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DBR1_SCHPO
ID   DBR1_SCHPO              Reviewed;         478 AA.
AC   O13765; P78964;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   25-MAY-2022, entry version 134.
DE   RecName: Full=Lariat debranching enzyme;
DE            EC=3.1.-.-;
GN   Name=dbr1; ORFNames=SPAC17A5.02c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9001235; DOI=10.1128/mcb.17.2.809;
RA   Nam K., Lee G., Trambley J., Devine S.E., Boeke J.D.;
RT   "Severe growth defect in a Schizosaccharomyces pombe mutant defective in
RT   intron lariat degradation.";
RL   Mol. Cell. Biol. 17:809-818(1997).
RN   [2]
RP   SEQUENCE REVISION.
RA   Nam K.;
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lariat debranching enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; U63635; AAC49619.2; -; Genomic_DNA.
DR   EMBL; CU329670; CAB11502.2; -; Genomic_DNA.
DR   PIR; T37817; T37817.
DR   RefSeq; NP_593470.2; NM_001018903.3.
DR   AlphaFoldDB; O13765; -.
DR   SMR; O13765; -.
DR   BioGRID; 278746; 187.
DR   STRING; 4896.SPAC17A5.02c.1; -.
DR   iPTMnet; O13765; -.
DR   MaxQB; O13765; -.
DR   PaxDb; O13765; -.
DR   PRIDE; O13765; -.
DR   EnsemblFungi; SPAC17A5.02c.1; SPAC17A5.02c.1:pep; SPAC17A5.02c.
DR   GeneID; 2542277; -.
DR   KEGG; spo:SPAC17A5.02c; -.
DR   PomBase; SPAC17A5.02c; dbr1.
DR   VEuPathDB; FungiDB:SPAC17A5.02c; -.
DR   eggNOG; KOG2863; Eukaryota.
DR   HOGENOM; CLU_005893_1_0_1; -.
DR   InParanoid; O13765; -.
DR   OMA; ASNYMHE; -.
DR   PhylomeDB; O13765; -.
DR   PRO; PR:O13765; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005681; C:spliceosomal complex; IC:PomBase.
DR   GO; GO:0008419; F:RNA lariat debranching enzyme activity; IGI:PomBase.
DR   GO; GO:0031070; P:intronic snoRNA processing; ISO:PomBase.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IMP:PomBase.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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   3: Inferred from homology;
KW   Hydrolase; mRNA processing; Nucleus; Reference proteome.
FT   CHAIN           1..478
FT                   /note="Lariat debranching enzyme"
FT                   /id="PRO_0000079796"
FT   REGION          250..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..323
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   478 AA;  54565 MW;  01629B8B8A10B9C7 CRC64;
     MSYFARLKPP PAFLKMRVGV QGCCHGILDN LYILAEKRKV DLLIIGGDFQ ALRNVSDYHG
     ISMPPKFKRL GDFFNYYNGR NKAPILTIFV GGNHEASNYL DELPYGGWVA PNIYYMGRSS
     VINVGGLRIA GISGIYSAMD YKKGRYEGLP YNYKMLKSIY HTREFDVLSL KSLQKPIDIF
     LSHDWPRGIE QHGDVAKLLR HKPFFRNEVE RNDLGSPALE ELLVELKPRY WMAAHLHTKF
     TAVVHHNSQE DDGKLSCSSK DVTSSGFSMK GLNEPSQERL PVEKEQNDKS DEEGSNNEQE
     EKQDKKQSTN RDLCRKESCK KEPSLSSSDQ VTKFLALDKC LPRRSYFEVV EIEPVEIPDS
     GAPYMQYDSE WLSVLRAMHP FQSHTIEQDP PLPSLEVVKT LKRKEEIWVD ENLVKKDKLG
     IPRNFCQTAP PHSRDITENM QPSSYINPQT VAFEILIGLK ERTVDSPPPV KNPNEIVL
 
 
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