ID A0A423XL86_9PEZI Unreviewed; 1044 AA.
AC A0A423XL86;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN ORFNames=VPNG_01221 {ECO:0000313|EMBL:ROW17237.1};
OS Cytospora leucostoma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Cytospora.
OX NCBI_TaxID=1230097 {ECO:0000313|EMBL:ROW17237.1, ECO:0000313|Proteomes:UP000285146};
RN [1] {ECO:0000313|EMBL:ROW17237.1, ECO:0000313|Proteomes:UP000285146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYLt {ECO:0000313|EMBL:ROW17237.1,
RC ECO:0000313|Proteomes:UP000285146};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. May promote
CC termination of transcription by RNA polymerase II.
CC {ECO:0000256|PIRNR:PIRNR037239}.
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,
CC ECO:0000256|PIRNR:PIRNR037239}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROW17237.1}.
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DR EMBL; LKEB01000003; ROW17237.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423XL86; -.
DR STRING; 1230097.A0A423XL86; -.
DR InParanoid; A0A423XL86; -.
DR Proteomes; UP000285146; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004534; F:5'-3' RNA exonuclease activity; IEA:UniProtKB-UniRule.
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-UniRule.
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 Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|PIRNR:PIRNR037239};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037239};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|PIRNR:PIRNR037239};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PIRNR:PIRNR037239};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000285146};
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..285
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 110..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..959
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1044 AA; 115798 MW; A8E5912A1F2325B1 CRC64;
MGIPAAFRWL STKYPKIVSP VVEDQPITMD DGTVIPVDAT RPNPNGEEFD NLYLDMNGIV
HPCSHPEDRP PPKDEEEMMV EVFKYTDRVV NMVRPRKLLM IAVDGVAPRA KMNQQRSRRF
RSAQDAQQKE EDKQQLITLL KKQNGGHHPA ESTEEVVKKA FDSNSITPGT PFMAILAASL
RYWCSYKLNT DPAWANVKVI ISDATVPGEG EHKIMNFVRS QRSSPDHDPN TRHVIYGLDA
DLIMLGLATH EPHFRVLRED VFAQDTRAKM CKLCGQKGHD AQNCRGESKD KDADFDGKDN
AHPLKPFIWL HVSVLREYLA VELDVPDLPF RWDIERAIDD WVFMCFFVGN DFLPHLPALE
IRENGIDTLT AIWKDNLPYM GGFLTKDGHC DLERAQLILA GLAKQEDAIF RRRKETEDRR
EANFKRRKLN EARNEARNGG GRNDATAHGR SKATKVDNMV PGLAPGTEFM PISSLPGPIP
KAITHDMVVN RSALQSANTA NKSAASVLKN KLLGKATEPK EEPAAGEGVA EAQEPPASTA
VKRKAEDIEQ DGTSTPTTDS PVVAAPSAPE DEGPTDTVRL WEEGYTDRYY EQKFHVDPKD
TEFRKKVAHA YVEGLAWVLM YYFQGCPSWE WYYPYHYAPF AQDFVELGTV KVNFEKGRIS
KPYEQLMSVL PAASRHAIPE VFHDLMTNEK SEIIDFYPED FEVDLNGKKM AWQGVALLPF
IDMPRLLTAM DKKYVLMSED ELARNEMGTD VLIISDAHPQ LYEEIITHFY SKKQGAPKYT
LNPRTSDGLG GEIEKIADYL PHGSLTYPLE RKTWPDIDYD RSLSVHYEMP SSAHTHKSML
LRGVKLPTPA LDRNDIEELR SKARRSGRSY GGVPLGRGGY HQNGRNQQFN YGPGRGYHGG
GRGSDRGPPG GGGYGGRDNY SQQHRNGGGY PAPPANWVPP PPGAAGFGNG LPPPPPSGGY
GGYGGYGGGY NQGYGNGGGY GAPPPPAPGQ YYGGGGGGGG GYQGQGYQNQ GYRPQAPPGN
DDRRYNGGHG GYDRGYGNNG GYRR
//
