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 27-MAR-2024, entry version 76.
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; 306901.Q2GNZ6; -.
DR GeneID; 4396518; -.
DR VEuPathDB; FungiDB:CHGG_10308; -.
DR eggNOG; KOG2044; Eukaryota.
DR HOGENOM; CLU_006038_1_1_1; -.
DR InParanoid; Q2GNZ6; -.
DR OMA; CLHYYVH; -.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004534; F:5'-3' RNA exonuclease 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 CDD; cd18673; PIN_XRN1-2-like; 1.
DR Gene3D; 1.25.40.1050; -; 1.
DR Gene3D; 3.40.50.12390; -; 2.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR041412; Xrn1_helical.
DR InterPro; IPR004859; Xrn1_N.
DR InterPro; IPR017151; Xrn2/3/4.
DR InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR12341:SF41; 5'-3' EXORIBONUCLEASE 1; 1.
DR PANTHER; PTHR12341; 5'->3' EXORIBONUCLEASE; 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
//
