XRN2_CRYNJ
ID XRN2_CRYNJ Reviewed; 1127 AA.
AC P0CL88; Q55QP9; Q5KFG7;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=5'-3' exoribonuclease 2;
DE EC=3.1.13.-;
GN Name=RAT1; OrderedLocusNames=CNF01810;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
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; AE017346; AAW44210.1; -; Genomic_DNA.
DR RefSeq; XP_571517.1; XM_571517.1.
DR AlphaFoldDB; P0CL88; -.
DR SMR; P0CL88; -.
DR STRING; 5207.AAW44210; -.
DR PaxDb; P0CL88; -.
DR eggNOG; KOG2044; Eukaryota.
DR HOGENOM; CLU_006038_2_1_1; -.
DR InParanoid; P0CL88; -.
DR OMA; CLHYYVH; -.
DR OrthoDB; 685597at2759; -.
DR PHI-base; PHI:3330; -.
DR Proteomes; UP000002149; Chromosome 6.
DR GO; GO:0090730; C:Las1 complex; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0110103; C:RNA polymerase II termination complex; IEA:EnsemblFungi.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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:0000956; P:nuclear-transcribed mRNA catabolic process; IBA:GO_Central.
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; 2.
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; 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..1127
FT /note="5'-3' exoribonuclease 2"
FT /id="PRO_0000249923"
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 532..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1127
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 1082..1103
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1127 AA; 126151 MW; ACD57B4016E0E611 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 STTPEDDEDP 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 GLRAKDPIPI DTKASYGITG
SVLPDPNCVP ASTFDTPIPS ISECPDLNPN DSISVRYYFP RQAHPHRSIL LRGYKPEPAR
LTESDKDWVR RGGQGGRRGH RHNGGGNGNV TGGPGMARGR YESGPPRTNG YQPPPPRSNY
GGSSGYGYGA PAPLPSRPPV SSYGGGAGGY GYSNPYAAAP NPYAGGYGAP APYAAGGYGQ
RPYVPPLPPP NPYSAPPPAY GRPPGGGYGY GAPPPRGGGY NPYPSRR
