ID   XRN2_CANGA              Reviewed;        1018 AA.
AC   Q6FKN6;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=5'-3' exoribonuclease 2;
DE            EC=3.1.13.-;
GN   Name=RAT1; OrderedLocusNames=CAGL0L10120g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380958; CAG62182.1; -; Genomic_DNA.
DR   RefSeq; XP_449208.1; XM_449208.1.
DR   AlphaFoldDB; Q6FKN6; -.
DR   SMR; Q6FKN6; -.
DR   STRING; 5478.XP_449208.1; -.
DR   PRIDE; Q6FKN6; -.
DR   EnsemblFungi; CAG62182; CAG62182; CAGL0L10120g.
DR   GeneID; 2891058; -.
DR   KEGG; cgr:CAGL0L10120g; -.
DR   CGD; CAL0135840; CAGL0L10120g.
DR   VEuPathDB; FungiDB:CAGL0L10120g; -.
DR   eggNOG; KOG2044; Eukaryota.
DR   HOGENOM; CLU_006038_1_1_1; -.
DR   InParanoid; Q6FKN6; -.
DR   OMA; CLHYYVH; -.
DR   Proteomes; UP000002428; Chromosome L.
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   Coiled coil; 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..1018
FT                   /note="5'-3' exoribonuclease 2"
FT                   /id="PRO_0000249921"
FT   REGION          402..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          938..1018
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          121..147
FT                   /evidence="ECO:0000255"
FT   COILED          468..541
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        519..545
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        949..986
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        999..1018
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1018 AA;  117656 MW;  ED5034F0A90B5912 CRC64;
     MGVPSFFRWL SRKYPKIISP VLEEPQQLVD GVALPIDYAG PNPNGELDNL YLDMNGIVHP
     CSHPENKPPP ETEDDMLLAV FEYTNRVLNM ARPRKVLVIA VDGVAPRAKM NQQRSRRFRS
     ARDAEIENEA REEIMRQKEQ LGQIIDDSVK NKKTWDSNAI TPGTPFMDKL AIALRYWTAF
     KLATDPGWKN LQVIISDATV PGEGEHKIMN FIRSQRADPE YNPNTTHCIY GLDADLIFLG
     LATHEPHFKI LREDVFAQDN RKRNNVKDTI DMTDEEKDLI RKQDSEKPFL WLHISVLREY
     LSAELWTPKL PFPFDLERAI DDWVFMCFFC GNDFLPHLPC LDVRENSIDI LLDIWKSILP
     RLKTYMTCDG KLNLESVEMV LKELGNREGD IFKTRHIQEI RKKEANERRK QQKQQNVSTG
     QDRHPTKFNE QLQMYDTNGS LAKGSWNLTT SDMVRYKKEL MLANEGDENS IKIIEEVSER
     NNSLMKEIQS EMTPEDYKGN NNNFTAAELL KKKLNARKRE LEKEKENEEQ ERASKQPKIS
     ETPDESDLTE EIEADVIAEV EDETTPDEKD TDSIITEVPE ISNGGITSGV IDTDEAVKLF
     EPGYHDRYYI EKFHIEPNQI PALSKHMVKC YIEGVSWVLM YYYQGCASWT WYYPYHYAPL
     AEDFVDFHDL DIKFELGEPF LPYEQLMSVL PAASGHNLPE VFRPLMSSED SEIIDFYPTE
     FPIDMNGKKM SWQGIALLPF IDETRLLTAT RNQYKFLSED EKRRNTRNDP VLLISNKNVN
     YEKFAKRLYK KGHEDNFQLV FHHFKSSLAG IVSTDTEGFK LHAKLPCPIQ SGALPELSTN
     LFLKMQYKLL PLPSANKSLI LNGFIPSEPM LTQHDFDSIV YKYGTRGFQR NQRNFGMEMK
     QNIVPVGPSG TTQYKPRIGG YRSFFYFGQL NQQMHQHNQV YQQNQAPTHD RYRNDRSDRG
     GRGYGRPDHD RGDYRGDYRG DGYRGGHRGG YRGGSRSRGP SSRGISSRGY SGPSRYNR