位置:首页 > 蛋白库 > XRN2_KLULA
XRN2_KLULA
ID   XRN2_KLULA              Reviewed;         992 AA.
AC   Q6CKX0;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=5'-3' exoribonuclease 2;
DE            EC=3.1.13.-;
GN   Name=RAT1; OrderedLocusNames=KLLA0F07469g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. Required for the
CC       processing of nuclear mRNA and rRNA precursors. May promote termination
CC       of transcription by RNA polymerase II (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC       subfamily. {ECO:0000305}.
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; CR382126; CAG98127.1; -; Genomic_DNA.
DR   RefSeq; XP_455419.1; XM_455419.1.
DR   AlphaFoldDB; Q6CKX0; -.
DR   SMR; Q6CKX0; -.
DR   STRING; 28985.XP_455419.1; -.
DR   EnsemblFungi; CAG98127; CAG98127; KLLA0_F07469g.
DR   GeneID; 2895935; -.
DR   KEGG; kla:KLLA0_F07469g; -.
DR   eggNOG; KOG2044; Eukaryota.
DR   HOGENOM; CLU_006038_1_1_1; -.
DR   InParanoid; Q6CKX0; -.
DR   OMA; CLHYYVH; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0090730; C:Las1 complex; IEA:EnsemblFungi.
DR   GO; GO:0110103; C:RNA polymerase II termination complex; IEA:EnsemblFungi.
DR   GO; GO:0004534; F:5'-3' exoribonuclease activity; IEA:EnsemblFungi.
DR   GO; GO:0019843; F:rRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0000448; P:cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:1901408; P:negative regulation of phosphorylation of RNA polymerase II C-terminal domain; IEA:EnsemblFungi.
DR   GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR   GO; GO:0071028; P:nuclear mRNA surveillance; IEA:EnsemblFungi.
DR   GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0034428; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 5'-3'; IEA:EnsemblFungi.
DR   GO; GO:0051984; P:positive regulation of chromosome segregation; IEA:EnsemblFungi.
DR   GO; GO:1904595; P:positive regulation of termination of RNA polymerase II transcription; IEA:EnsemblFungi.
DR   GO; GO:0043144; P:sno(s)RNA processing; IEA:EnsemblFungi.
DR   GO; GO:0030847; P:termination of RNA polymerase II transcription, exosome-dependent; IEA:EnsemblFungi.
DR   GO; GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; IEA:EnsemblFungi.
DR   GO; GO:0106354; P:tRNA surveillance; IEA:EnsemblFungi.
DR   InterPro; IPR027073; 5_3_exoribonuclease.
DR   InterPro; IPR004859; Put_53exo.
DR   InterPro; IPR041412; Xrn1_helical.
DR   InterPro; IPR017151; Xrn2/3/4.
DR   PANTHER; PTHR12341; PTHR12341; 1.
DR   Pfam; PF17846; XRN_M; 2.
DR   Pfam; PF03159; XRN_N; 1.
DR   PIRSF; PIRSF037239; Exonuclease_Xrn2; 1.
PE   3: Inferred from homology;
KW   Exonuclease; Hydrolase; mRNA processing; Nuclease; Nucleus;
KW   Reference proteome; rRNA processing; Transcription;
KW   Transcription regulation; Transcription termination.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..992
FT                   /note="5'-3' exoribonuclease 2"
FT                   /id="PRO_0000249927"
FT   REGION          528..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          916..992
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..545
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..563
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        916..980
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   992 AA;  114291 MW;  CAB1090F1953ED9B CRC64;
     MGVPSFFRWL SRKYPKIISP VLEEYPVIED GVQLPLDYSS ANPNGELDNL YLDMNGIVHP
     CSHPENKPPP ETEDEMLLAV FEYTNRVLNM ARPRKVLMIA VDGVAPRAKM NQQRARRFRS
     ARDAKLQNEA REQVLRERED YGETIDENVK SKKTWDSNAI TPGTPFMDKL ATALRYWTSF
     KLATDPGWKN LQIIISDATV PGEGEHKIMN FIRSQRADTQ YNPNTTHCIY GLDADLIFLG
     LATHEPHFKI LREDVFANNN YKKPKPQDMI NLSEEEKQQL IQQDSEKPFL WLHISVLREY
     LSAELAIPHL SFQFDFERAI DDWVFMCFFC GNDFLPHLPC LDVRENSIDI LVDIWKTVLP
     KTKTYLTCDG TLNLEPVEAL LEQLGDRETD LFKKKYIQEV RKQEAHDRRK KLKSNPNVSQ
     GKVDRNFMIP LENMPVYDVD GNAAEGSLNL SNKDFANMRK EINLANEGDG EAAKALKLKS
     EKNSGVVEFS SEELKNSVQL SKTANYDAAT SLQEKLIAKK MAMRDEENAE ELSLKRKSED
     VDSAEKETSN EPEDDEADYD EDEGSTVPPA VIHTGIVKSG FIDTDESVRL YEPGYHDRYY
     QHKFHVPAKD IPALQKDVIR CYVEGISWVL LYYYQGCASW TWYYPYHYAP FAQDFKNIKN
     LDIHFDLGEP FLPYEQLMSV LPAASGHALP EIFRPLMSDP NSEIIDFYPE EFPVDMNGKK
     MAWQGIALLP FIDETRLLKT VREQYSKLSD SEKARNVRKK DALLISNKNV NYDLFMKNLY
     GENPVNVIEF RHFKSGLSGF VTQAEEGFEL NSKLICPING GGLPDLSTNL FLKLSYTQPV
     VAGRCKSLVL NGYIPPQPML TPQDRDCIIY KYSNRWNPSM MKYNIVPVGP SGITQYQPRV
     GGYRSFFFHK EQTAYAQQPQ QNREYMHSQQ RQPQGSRYQQ SRYNNGNYNN SNNGYSDNNN
     GNTGKYNRHY NNSRGNSNRY SNSNDRRREF RR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024