XRN2_USTMA
ID XRN2_USTMA Reviewed; 1233 AA.
AC Q4P149; A0A0D1DMM4;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=5'-3' exoribonuclease 2;
DE EC=3.1.13.-;
GN Name=RAT1; ORFNames=UMAG_06164;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003161; KIS65784.1; -; Genomic_DNA.
DR RefSeq; XP_011392541.1; XM_011394239.1.
DR AlphaFoldDB; Q4P149; -.
DR SMR; Q4P149; -.
DR STRING; 5270.UM06164P0; -.
DR EnsemblFungi; KIS65784; KIS65784; UMAG_06164.
DR GeneID; 23565847; -.
DR KEGG; uma:UMAG_06164; -.
DR VEuPathDB; FungiDB:UMAG_06164; -.
DR eggNOG; KOG2044; Eukaryota.
DR HOGENOM; CLU_006038_2_1_1; -.
DR InParanoid; Q4P149; -.
DR OMA; CLHYYVH; -.
DR OrthoDB; 685597at2759; -.
DR Proteomes; UP000000561; Chromosome 22.
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 PANTHER; PTHR12341; PTHR12341; 1.
DR Pfam; PF17846; XRN_M; 1.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF037239; Exonuclease_Xrn2; 1.
DR SMART; SM00343; ZnF_C2HC; 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..1233
FT /note="5'-3' exoribonuclease 2"
FT /id="PRO_0000249929"
FT ZN_FING 270..287
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 21..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 117..148
FT /evidence="ECO:0000255"
FT COILED 413..439
FT /evidence="ECO:0000255"
FT COMPBIAS 414..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..639
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..973
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1233 AA; 133649 MW; 16018F19567A15D7 CRC64;
MGVPALFRWL SKKYPRIVSS VQEEDPKTAP GPDGTEITLP LDTSTPNPNG EEFDCLYLDM
NGIVHPCTHP EGKPAPETEE EMMVEVFAYT ERVVNMVRPR RLLMMAIDGV APRAKMNQQR
SRRFRAAKEA REKHEEEQAA LAEWKAKGLG ATDDEKKSKR AWDSNAITPG TPFMDLLAAS
LRYWVAQKIN SDPGWKDIQV IISDASVPGE GEHKIMEHIR RQRSHPEHDP NTKHVIYGLD
ADLIMLSLAT HEPYFKVLRE DVFAADNKPK TCNLCGQPGH FAASCTGAAK KKSGQHDEIA
PTPPEKKPFI FLDVATLREY LEVELNIPQL PFAFDLERAI DDWVFLIFFV GNDFLPHLPS
LEIRDGAIDT LLRIWKKELP AMGGYLTNHG RVELGRAQLI LSGLASEEDE IFRRRKEDED
RRETNRKRRE EMQQRRDKEL DQGNFGNGSM VEVMSKKRRA HETEKPAFNG VSAQEARDQA
NSSNKSYDPR KKAIVLGGDN NQVVSDRNAA RQANMDAAEA LKAELMGDAP KQQEADAERA
LKKVKTEAGA EPTTASVEKQ EHGDDQDSAS AGTKRKADQV QHHANAGDDD VAKIEAATED
GDADADTDAN ADANADAEVD AEAEDDEEED NDEVDGNEDV DPVTTIKKRK VNADGTVDYE
DTVKMWEPGY RERYYKEKFG VDLSDTDFRR SVVKSYIEGL CWVLAYYYQG VPSWQWYYPF
HFSPFAADFE DLESLDIQFQ LGSPFKPFEQ LMGVLPADSR ASIPPAFHPL MTESDSDIID
FYPSEFEIDM NGKKMAWQGV ALLPFIDEKR LLDALKERYP LLSEDEVRRN GFGNNTLFVG
NESRLYDFLC EEIYAKKRTT DDGETPKRVA VNPALSGGIT GFVKPDPVCV PGSTFNSPLT
SQALHDIHND RSISVLYDFP EQKTPHRSVL LKGLKPPKRI LSAAEIDWVK RGSPDNRGRG
RGRGAHHGGA GRDFHRSSNG QQHNNNGYAG GENGSAGYRG SNGGGYGSHN GGGGGGYGAP
VGRSHDYQQY SQSGSGGGGG GYGNYGGYGG YGGSGYGVGG RDGGAYYGGY GGGGGGAYGA
APTYASAGAY DAYAGYGGSG GYGAYGASAY APGAGGNRDN RYAAYTQPSM HVGPAAGRGG
RQAAPANHAG YAGLPSLGAP PAPPAPPTHP AAAYGGYTNG GYGGYGAPAH GYGGAPPARG
GGRGGRGAGS RGAGRGANNA SYAGRGGAYG SFY
