ID   XRN2_CHAGB              Reviewed;        1039 AA.
AC   Q2GNZ6;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=5'-3' exoribonuclease 2;
DE            EC=3.1.13.-;
GN   Name=RAT1; ORFNames=CHGG_10308;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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}.
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DR   EMBL; CH408035; EAQ83904.1; -; Genomic_DNA.
DR   RefSeq; XP_001228235.1; XM_001228234.1.
DR   AlphaFoldDB; Q2GNZ6; -.
DR   SMR; Q2GNZ6; -.
DR   STRING; 38033.XP_001228235.1; -.
DR   EnsemblFungi; EAQ83904; EAQ83904; CHGG_10308.
DR   GeneID; 4396518; -.
DR   eggNOG; KOG2044; Eukaryota.
DR   HOGENOM; CLU_006038_1_1_1; -.
DR   InParanoid; Q2GNZ6; -.
DR   OMA; CLHYYVH; -.
DR   OrthoDB; 685597at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004534; F:5'-3' exoribonuclease activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR027073; 5_3_exoribonuclease.
DR   InterPro; IPR004859; Put_53exo.
DR   InterPro; IPR041412; Xrn1_helical.
DR   InterPro; IPR017151; Xrn2/3/4.
DR   InterPro; IPR001878; Znf_CCHC.
DR   PANTHER; PTHR12341; PTHR12341; 1.
DR   Pfam; PF17846; XRN_M; 1.
DR   Pfam; PF03159; XRN_N; 1.
DR   PIRSF; PIRSF037239; Exonuclease_Xrn2; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Exonuclease; Hydrolase; Metal-binding; mRNA processing;
KW   Nuclease; Nucleus; Reference proteome; rRNA processing; Transcription;
KW   Transcription regulation; Transcription termination; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..1039
FT                   /note="5'-3' exoribonuclease 2"
FT                   /id="PRO_0000249922"
FT   ZN_FING         270..287
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          414..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          869..907
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          930..1039
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          119..147
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        414..428
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        940..967
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1039 AA;  115014 MW;  864422C4250DC6FD CRC64;
     MGIPAAFRWL STKYPKIISP VVEEKALVME DGTVVPVDAT QPNPNGEEFD NLYLDMNGIV
     HPCSHPEDRP APSDEEEMMV EVFKYTERVV NMVRPRKLLM IAVADGVAPR AKMNQQRSRR
     FRAAQDAKEK EEDKQQLLKM LQKEKGSTAK EEPIETVVKK AFDSNSITPG TPFMDILAAS
     LRYWCAYKLN TDPAWAKMKV IISDATVPGE GEHKIMEFVR SQRNSPEHDP NTRHVIYGLD
     ADLIMLGLAT HEPHFRVLRE DVFFQQGKAR MCKLCGQKGH DERNCRGEAK EKAGEFDEKD
     KAEPLKPFIW LHVSILREYL AIELNIPNLP FRWDLERAID DWVFMCFFVG NDFLPHLPAL
     EIRENGIETL MAIWKDNLPV MGGYVTKDGH VDLDRAQYIL SGLAKQEDSI FRRRKETEDR
     REAGFKRRKL NNQQGNNRGG AHDSPLSGRG GRKGAPEANG PPVGMNLFPV ASIPKPVITH
     DMVVNRANVA NKSAASVLKS QIQSLVAQTQ EKPEGDEPKE ENPEAKTPPS ALGKRKAELI
     EEGTATASDA ASDTETPATT SSEEGPIDTV RLWEEGYADR YYEQKFKVDA KDIAFRHKVA
     RAYVEGLAWV LMYYFQGCPS WEWFYPYHYA PFAADFVDLG KMKISFEKGR ISRPFEQLMS
     VLPAASRHAI PEVFHDLMTQ EDSPILDFYP EDFEIDLNGK KMSWQGIALL PFIEMPRLLD
     AMKTKSHLLS AEDKARNAPG HDVLLISDSH PGLYEDISSH FYSKKQAVPE FKLDPKRSDG
     LSGKVRKIEG YVPHGSLVYP LERNTMPDVD YDRSMSVNYD MPTSSHIHKS MLLRGLKMPT
     PALDRSDVDF VRSKGRGAGR SFGGVPLRNN YNGGGRGDRI NYAGGPPRGG GGGGRGRGGY
     QQDRGYGNGY GGGGGSGGGG GGGGYGNGYG GYQQPAAPGQ QSWQPPPPPG YPGFGVGVPP
     PPPPAHASGG GYNQGYGNQG YGGQNYRNDR YPPGPPPHGG YQGGGYPGGG YQGGGHQGGY
     QGQYHPPHGQ SQDRRHDNS