ID E3RI22_PYRTT Unreviewed; 883 AA.
AC E3RI22;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=5'-3' exoribonuclease 2 {ECO:0000256|ARBA:ARBA00013845};
DE Flags: Fragment;
GN ORFNames=PTT_07622 {ECO:0000313|EMBL:EFQ94619.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ94619.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ94619.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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. {ECO:0000256|ARBA:ARBA00025537}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC subfamily. {ECO:0000256|ARBA:ARBA00006994}.
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DR EMBL; GL533210; EFQ94619.1; -; Genomic_DNA.
DR RefSeq; XP_003297277.1; XM_003297229.1.
DR AlphaFoldDB; E3RI22; -.
DR STRING; 861557.E3RI22; -.
DR EnsemblFungi; EFQ94619; EFQ94619; PTT_07622.
DR KEGG; pte:PTT_07622; -.
DR eggNOG; KOG2044; Eukaryota.
DR HOGENOM; CLU_006038_1_1_1; -.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004534; F:5'-3' RNA exonuclease activity; IEA:EnsemblFungi.
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:0000956; P:nuclear-transcribed mRNA catabolic process; IEA:EnsemblFungi.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IEA:EnsemblFungi.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0106354; P:tRNA surveillance; IEA:EnsemblFungi.
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 Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW Transcription {ECO:0000256|ARBA:ARBA00022472};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00022472};
KW Transcription termination {ECO:0000256|ARBA:ARBA00022472};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 271..284
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 418..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 883
FT /evidence="ECO:0000313|EMBL:EFQ94619.1"
SQ SEQUENCE 883 AA; 100875 MW; D8D73F24425E2363 CRC64;
MGVPAMFRWL SQKYPKIVST VQEELPKKVG DAVIPVDRTG PNPNGEEFDN LYLDMNGIVH
PCSHPEDKPA PKTEADMMMA IFEYTDRVVG MVRPRKLLYM AVDGVAPRAK MNQQRSRRFR
AAREAKEKDE ERAEFQKILN SQKASRGEDI DTLEEVMEKT WDSNAITPGT PFMHLLAESL
QYWCAYKFTT DPSWKDMKVI ISDASVPGEG EHKIMNFIRS QRAMPTHDPN TSHVIYGLDA
DLIMLSLATH EPHFKVLRED VFYDSGKDKV CTRCGRKGHI RTNCEFPEDE KKLTEEEAAE
EWATSEHQLK PYIWLHTNVL REYLAVEMDT PKRTFKYDLE RSLDDWVFMC FFVGNDFLPH
LPSLEIRDQG IDLLISIWRD LAAEMDDYVT KDGYPDMRRV QQIMSALATR EAGIFKKRKE
VSDRQAANRA RREAQSNAHK RQRTDNDGVS APGFKRAKET TDTYTSAGIV FFDPKDAQSK
EVRDVHKDIM HTRDSQSNKS AAARLKELLK AKADGTSLPE PEQTPDSEPA LESASGTETP
VQLGKRKLDE VDDLDNGTPG RNTPVVPQSP TQAAQPPKKD DSPPEDTIML WEDGYEERYY
EQKFHVAPND IAFRNKVARQ YAEGLCWVLA YYMQGCPSWT WYFPHHYAPF AADFVGLEDM
DPRKLFEKGV PFHPYEQLMG VLPAASNHAI PEPFRVLMED PNSSIVDFYP EDFPIDLNGK
KFAWQGVAVL PFIDEKRLLE AMGTKYPELS DDERKRNEFG KETLMFSQES GLFDDVEKAL
YRKGQQKHKI DPAKSRALHG DIEPHDLFVM DSQLVPPFDA DGTTDFEITQ DRSMRVYYEM
PSVSSSRAHK SVLLEGVKLP KPALQPGEAE SVRRSNERGG FRG
//
