ID A0A0G2FTF7_9PEZI Unreviewed; 828 AA.
AC A0A0G2FTF7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN ORFNames=UCDDA912_g02558 {ECO:0000313|EMBL:KKY37447.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY37447.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY37447.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY37447.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY37447.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY37447.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-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:KKY37447.1}.
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DR EMBL; LCUC01000085; KKY37447.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2FTF7; -.
DR STRING; 1214573.A0A0G2FTF7; -.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000034680; 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; -; 1.
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:UP000034680};
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 413..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 828 AA; 93762 MW; 9018E64C0E7F9BAF CRC64;
MGIPAAFRWL STKYPKIISP VIEDQPVTMD DGSVIPVDHT QPNPNGEEFD NLYLDMNGIV
HPCSHPEDRP PPKDEEEMMV EVFKYTDRVV NMVRPRKLLM IAVDGVAPRA KMNQQRSRRF
RAAQDAKEKE EEKQQLLTLL KRQNGGTHPA ESTEEVVKKA FDSNSITPGT PFMKILAASL
RYWCSYKLNT DPAWANIKVI ISDATVPGEG EHKIMNFVRS QRASPEHDPN TRHVIYGLDA
DLIMLGLATH EPHFRVLRED VFAQDSRAKM CKLCGQKGHD AQNCRGEQKD KDADFDGKDN
AHPLKPFIWL HVSILREYLA VELDVPNLPF RWDIERAIDD WVFMCFFVGN DFLPHLPALE
IRENGIDTLT AIWKDNLPHM GGYLTKDGHC DLERAQLILA GLAKQEDAIF RRRKETEDRR
EAGFKRRKAA EQARAAGRNN SGPQGRNKHQ KVDNMVPGLA PDAAFVPISS LPGPLAKPNS
AITHDMVVNK SSLQNANTAN KSAASVLKSQ IQGLMNKPTE SKEETAKGEE PSSAQETPPS
AARKRKADLL EQDEPGTPST DSPDAVTPST TTENEGPVDT VKLWEDGYAD RYYEQKFHVD
RNDVEFRHQV GRAYVEGLAW VLMYYFQGCP SWDWYYPYHY APFAQDFVDL HKVEIKFEKG
RISRPYEQLM SVLPAASRHA IPEVFHDLMT DEDSEIIDFY PEDFEVDLNG KKMAWQGVAL
LPFIDMPRLL EAMAKKYHLL SEDALARNEP GQDVLIISDA HPGLYDDIIT HFYSKKQGAP
KHQLDPRTSD GLAGEVAKIE DYLPHGALAY PLERKSMPDL DYDRSLSY
//
