ID A0A1S8BJP4_9PEZI Unreviewed; 1114 AA.
AC A0A1S8BJP4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN ORFNames=BK809_0007809 {ECO:0000313|EMBL:OMP87721.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:OMP87721.1, ECO:0000313|Proteomes:UP000190776};
RN [1] {ECO:0000313|EMBL:OMP87721.1, ECO:0000313|Proteomes:UP000190776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F98.1 {ECO:0000313|EMBL:OMP87721.1,
RC ECO:0000313|Proteomes:UP000190776};
RA Robert-Siegwald G., Vallet J., Abou-Mansour E., Xu J., Rey P., Bertsch C.,
RA Rego C., Larignon P., Fontaine F., Lebrun M.-H.;
RT "Draft genome sequence of Diplodia seriata F98.1, a fungal species involved
RT in grapevine trunk diseases.";
RL Submitted (JAN-2017) 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:OMP87721.1}.
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DR EMBL; MSZU01000076; OMP87721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8BJP4; -.
DR STRING; 420778.A0A1S8BJP4; -.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000190776; 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 InterPro; IPR036875; Znf_CCHC_sf.
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 SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 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:UP000190776};
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 275..289
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 418..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1007
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1114 AA; 122198 MW; 2DBF42108951DBF7 CRC64;
MGVPALFRWL SQKYPKIISP VVEAEPVEYP DGTVEPVDAT KPNPNGEEMD NLYLDMNGIV
HPCSHPEDKD PPENEEEMMI EIFKYTDRVV NMVRPRKLLM IAVDGVAPRA KMNQQRSRRF
RAAQDAKQKD ADAAEFAKML ASQNQKKGES ENDDSAEAKI VKKTWDSNSI TPGTPFMDIL
AQSLRYWCAY KLNTDPAWEK LKVIISDATV PGEGEHKIME FVRSQRRSPY HDPNTRHVIY
GLDADLIMLG LVTHEPHFRV LREDVFANDA KPRTCRRCGQ VGHYADQCRG EIKKKEDDHD
VKQNKVTKKP FIWLHVSILR EYLAAELKVD SQGFPFDLER TLDDWVFMCF FVGNDFLPHL
PSLEIREGGI DTLINIWREN LPIMGGYVTK DGHVDMSRAQ VILQGLAKLE DGIFKRRKET
EDRREAAQKR RKLQEERRHG GRFAQGGDGN QQNNSPTARK GSKKGETAEN FANLPMFSPG
ELQSKEARAL THENFVNRKA IFQGSANVAN ANKSAAAALK EGLLGKKPET VSVAAGQDGS
AEDVPVPDAP AEDATATPPS ALGKRKAELL EDDSSTPGRN TPDAGPPAVK SDEPPEDTVK
MWEDGYMDRY YEQKFHVDPA DIEFRHQVAR DYAEGLAWVL LYYLQGCASW TWYYPHHYAP
FAQDFVDLDK MELKFEKGRP FRPYEQLMGV LPAASNHAIP SVFRPLMEEA DSEIIDFYPE
DFRVDLNGKK MAWQGVAILP FIDEKRLLDA MATKYPLLSP DEAARNEFGK EVLLFSTRHP
LYEEVAQQWY SKKQGEPQHK LNPEVSDGLA GTVTKNDDYL PQSSLVFPLE TKGMPDLEED
QSISVHYEMP KSKNVHKSQL LRGVEFPPPA LTQDEIHGVR NRARHGGGGG GGRDRGFHSH
NENRWQGGPP RHRGGGGGGG GGYNNGGGHH NNNHHHHNQN NNSNPNPNNP IAGFLNPNFD
PQAFMQRGPG AGGGPPGGPA GVPPPPHLAA QMNGWQPPPP PQFGGAFPPM PAGYGGYGGP
PQNGGGGGGG GGGYGYGGRR DDNYRPGGGG GGGGGGGGYG GRQDDSYRPD HGYGGGGGGG
RGGDGYGGGG GGGGGRGGGR RGGGRGGRGA YDRR
//
