XRN2_CRYNB
ID XRN2_CRYNB Reviewed; 1130 AA.
AC P0CL89; Q55QP9; Q5KFG7;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=5'-3' exoribonuclease 2;
DE EC=3.1.13.-;
GN Name=RAT1; OrderedLocusNames=CNBF2890;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AAEY01000032; EAL19962.1; -; Genomic_DNA.
DR RefSeq; XP_774609.1; XM_769516.1.
DR AlphaFoldDB; P0CL89; -.
DR SMR; P0CL89; -.
DR PRIDE; P0CL89; -.
DR EnsemblFungi; EAL19962; EAL19962; CNBF2890.
DR GeneID; 4936841; -.
DR KEGG; cnb:CNBF2890; -.
DR VEuPathDB; FungiDB:CNBF2890; -.
DR HOGENOM; CLU_006038_2_1_1; -.
DR Proteomes; UP000001435; Chromosome 6.
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:0008270; F:zinc ion binding; IEA:InterPro.
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 InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR12341; PTHR12341; 1.
DR Pfam; PF17846; XRN_M; 1.
DR Pfam; PF03159; XRN_N; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR PIRSF; PIRSF037239; Exonuclease_Xrn2; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Coiled coil; Exonuclease; Hydrolase; Metal-binding; mRNA processing;
KW Nuclease; Nucleus; 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..1130
FT /note="5'-3' exoribonuclease 2"
FT /id="PRO_0000409995"
FT ZN_FING 270..287
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 411..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 121..147
FT /evidence="ECO:0000255"
FT COILED 412..441
FT /evidence="ECO:0000255"
FT COMPBIAS 536..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..663
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1106
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1130 AA; 126478 MW; BD6EED96F2C71263 CRC64;
MGVPALFRWL SKKYPKIVER VKEDTPKKIR GPDGEIVEEP IRYENPNPNG FEVDNLYLDM
NGIVHPCTHP EGRPAPETEE EMMVEIFKYT ERVVNMCRPR KVLMMAIDGV APRAKMNQQR
SRRFRAAQEA ADKEEERREA IKLFEAMGHA VSEETANHKS WDTNAITPGT PFMDLLSISL
KYWVSHKLTT DPGWKDLKII LSDSSVPGEG EHKIMDWIRR QRSYPTWDAN TSHVIYGLDA
DLIMLSLATH EPHFRVLRED VFAQSSKGPH ACKNCGKVGH IAANCKSDKK FKDPNVAEVA
KTEDPKPFIF LDVACLREYL AVELVVPGMP FPFDLELAID DWIFMIFFVG NDFLPHLPSL
EIREGAIDVL LKIWRAELPR MGGYLTNHGK VNLDRAQVIL EGLAKSEDEI FQKRKDDEER
QEHSQKRRRI EEHKRQDEDK AREEDRNTLT LNGTEYVAVD NPAATARGGP LHPSLPSRPA
FDLVPKEDAV KQPEDQDQKA KKAMAGSNSD IVKNRKAIRM ANMSAAQALK AELEGGNDVN
VDDKKAIAQE GKEEDEAVVT VERTEDEEKE QLTKEEARGT LEEQGEKEGV DEEVVPPAIQ
TDEDEGEAPV GDATVAENDE STIPEDDEDP THVPRKRKRG DSDGDEDSNE EDDDDDDDDA
PPNPEADQPI PKKKLKVNAD GTVDYEDDVK LWEPGYRERY YEKKFGVKLS EREFIDKVTK
SYMEGLCWVL EYYYQGVPAW DWFYPYHYAP FAQDFRDVGS MDIKFETSIP FKPFAQLLGV
FPAASRIHLP EPLQTLMIDE DSPILDFYPP DFEIDMNGKK MAWQGVALLP FIDQNRLLTA
LKSKEELLSD DEKRRNSWGD NVMFIANENP LYDLFCDKLY GLRAKDVSKP IPIDTKASYG
ITGSVLPDPN CVPASTFDTP IPSISECPDL NPNDSISVRY YFPRQAHPHR SILLRGYKPE
PARLTESDKD WVRRGGQGGR RGHRHNGGGN GNVTGGPGMA RGRYESGPPR TNGYQPPPPR
SNYGGSSGYG YGAPAPLPSR PPVSSYGGGA GGYGYSNPYA AAPNPYAGGY GAPAPYAAGG
YGQRPYVPPL PPPNPYSAPP PAYGRPPGGG YGYGAPPPRG GGYNPYPSRR
