ID Q0UPQ0_PHANO Unreviewed; 1021 AA.
AC Q0UPQ0;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
GN ORFNames=SNOG_06264 {ECO:0000313|EMBL:EAT86095.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT86095.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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}.
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DR EMBL; CH445333; EAT86095.2; -; Genomic_DNA.
DR RefSeq; XP_001796643.1; XM_001796591.1.
DR AlphaFoldDB; Q0UPQ0; -.
DR STRING; 321614.Q0UPQ0; -.
DR EnsemblFungi; SNOT_06264; SNOT_06264; SNOG_06264.
DR GeneID; 5973522; -.
DR KEGG; pno:SNOG_06264; -.
DR VEuPathDB; FungiDB:JI435_062640; -.
DR eggNOG; KOG2044; Eukaryota.
DR HOGENOM; CLU_006038_1_1_1; -.
DR InParanoid; Q0UPQ0; -.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004534; F:5'-3' RNA exonuclease activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IBA:GO_Central.
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; 3.40.50.12390; -; 2.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR041412; Xrn1_helical.
DR InterPro; IPR004859; Xrn1_N.
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; 2.
DR Pfam; PF03159; XRN_N; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055};
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..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..897
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..934
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1021 AA; 113782 MW; AA504A91611F5E96 CRC64;
MGVPAMFRWL SQKYPKIVST VQEEQPKKVG DEVIPVDRTG PNPNGEEFDN LYLDMNGIVH
PCSHPEDKPA PKTEADMMMA IFEYTDRVVG MVRPRKLLYM AVDGVAPRAK MNQQRSRRFR
AAREAKEKDE ERAEFLKMLN SQKASRGEDI NSLEEVVEKT WDSNAITPGT PFMHLLAESL
QYWCAYKFTT DPSWKDMKVI ISDASVPGEG EHKIMNFVRS QRAIPTHDPN TRHVIYGLDA
DLIMLSLATH EPHFRVLRED VFFDSGKDKA CTRCGRKGHI RNNCEFPDDG KKLTEEEAAE
EWAASEHPPK PYIWLHTNIL REYLAVEMET PKRRFKYDLE RSLDDWVFMC FFVGNDFLPH
LPSLEIRDQG IDLLISIWRD LAAEMDDYVT KDGFPDMRRV QQILGALASR EADIFKKRKE
VSDRQAANRA RREAQQNGRG RGRGDDTYSS GPPQKRVKES TDTYLNSGTI FFDPKDAQSN
DTRRDHAAMR SPMPEAEGTQ ETDSATGVEA PVELGKRKAD ELEDADNGTP GRNTPVVPAS
PAAETPKKED GTPEDTIKLW EDGYEERYYE QKFHVAPDDI AFRNKVARQY AEGLCWVLAY
YMQGCPSWTW YFPHHYAPFA ADFVGLEDMD PRKLFEKGTP FHPYEQLMVL PFIDSKRLLD
AMATKYPELS DDERKRNEFG KETLMFSQEG GLFDDVEKAL YRKGVKKHSI DPAQSRALHG
DIEPHDLFVL DSQLVPPFDV DGDSEFEIVQ DGSMRVYYEM PRLNSKNAHK SVLLPGTKMP
TPALSPGEAE SVRRSNERGG WRGGRGGGRG GGGRGGFNDR RNNDNMRGDY QNGGRGGYNN
GGRGGYNNGG GRGGYNGNQG GYGAPQNFPP PFPNSWPPPP GGANFVPPPP PGWVPPPQQG
GYQGGGGYGG PPGMPPAQRP AWMGNAPPHH GGPPPQQAGN NSSLRNEQYY RPADEILGRN
GGGSGGYGGH RNDNPYNDRQ PRNDRGGARG GRGGGRGGGG GGGGGYGGGG NRQSHNSNDY
R
//
