GenomeNet

Database: UniProt
Entry: A0A5N5WME2_9EURO
LinkDB: A0A5N5WME2_9EURO
Original site: A0A5N5WME2_9EURO 
ID   A0A5N5WME2_9EURO        Unreviewed;      1053 AA.
AC   A0A5N5WME2;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE            EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN   ORFNames=BDV29DRAFT_184514 {ECO:0000313|EMBL:KAB8068454.1};
OS   Aspergillus leporis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=41062 {ECO:0000313|EMBL:KAB8068454.1, ECO:0000313|Proteomes:UP000326565};
RN   [1] {ECO:0000313|EMBL:KAB8068454.1, ECO:0000313|Proteomes:UP000326565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 151.66 {ECO:0000313|EMBL:KAB8068454.1,
RC   ECO:0000313|Proteomes:UP000326565};
RG   DOE Joint Genome Institute;
RA   Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA   Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA   Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA   Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA   Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA   Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA   Baker S.E., Andersen M.R.;
RT   "Friends and foes A comparative genomics study of 23 Aspergillus species
RT   from section Flavi.";
RL   Submitted (APR-2019) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ML732392; KAB8068454.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N5WME2; -.
DR   Proteomes; UP000326565; 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:UP000326565};
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          270..284
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          419..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          872..1053
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..446
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        540..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..591
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        947..961
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..989
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        996..1017
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1053 AA;  118786 MW;  C1CF1551F238E3B3 CRC64;
     MGVPALFRWL SNKYPKIISS VIEETPYEVN GEQIPVDTTR PNPNGEEMDN LYLDMNGIVH
     PCTHPEGKPP PANEQEMMLE IFAYTDRVVN MVRPRKLLMI AVDGVAPRAK MNQQRARRFR
     SAQEAKEADE KKEEFRKSFL KKGGSKEDQA IHEEVIQKTW DSNVITPGTP FMDILAASLR
     YWIAYKLNTD PAWEKLKIII SDATVPGEGE HKIMNFVRSQ RAAPEHDPNT RHVIYGLDAD
     LIMLGLATHE PHFRVLREDV FFQESKARTC HLCGQAGHKA EECRGQAKVK NGEFDEKGKG
     SSLKPFIWLN VSILREYLAV ELYVPHQPFP FDLERALDDW VFMCFFVGND FLPHLPSLDI
     RENGIDTLIA IWRDNIPVMG GYLTKDGHVD FQKAQLILQG LAKQEDAIFR RRRQVEERKL
     ANEKRRKEEA QAREERNKKR RRSSPSYETY NESPTSNRTR GGGGGGDAAA PPPGLELITP
     GRGNLSREAR ELTHNMVVNR GAVYKANMAN KSAAAILKSK LMKGSQDDDE PEETNSTPDM
     DETPDTTVEQ TSPSVLGKRK ANEPEGETET PGDDTDSVPK PAKNDEMPPD TVRLWDEGYA
     DRYYEQKFHV DPQDKEFRHK VARAYAEGLA WVLLYYFQGC PSWTWYYPYH YAPFAADFVD
     IGDMELSFDK GIPFKPFEQL MGVLPASSNH AIPEVFHDLM RNPDSEIIDF YPEDFAVDLN
     GKKFAWQGVI LLPFIDEKRL LAAMEKKYPL LSEDERLRNT VGRDVLMLSD GHPLYQDLVS
     NFYSKKQGDP KYKLNMHISE GLAGKVERNE TYIPHSSLVS SLEEYGMPTL EDDRSLMVNY
     EIPKSSHIHK SMLLRGVKFN PPALDNADIQ ATKSKAQHSG RSFGGAPFRN GGGRGGRISY
     ASDRPNDRPN DRPNPFAAHL DPSFMPPGNS GAQMMSSGWV PPVPGSGSYS RGPPPPPRGG
     MSHPHHRNHY ASGQGQQQGH QQTNYGRGDY YGRGQQGHQH QGSYGNQSDQ YNGRPSSYGG
     GQDYRGGGYQ RGGYHQGQGR DYSSRNPGGY GRY
//
DBGET integrated database retrieval system