ID A0A2N6P1R0_BEABA Unreviewed; 824 AA.
AC A0A2N6P1R0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN Name=RAT1 {ECO:0000313|EMBL:PMB73468.1};
GN ORFNames=BM221_000891 {ECO:0000313|EMBL:PMB73468.1};
OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB73468.1, ECO:0000313|Proteomes:UP000235728};
RN [1] {ECO:0000313|EMBL:PMB73468.1, ECO:0000313|Proteomes:UP000235728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEF-007 {ECO:0000313|EMBL:PMB73468.1,
RC ECO:0000313|Proteomes:UP000235728};
RX PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT "Characterization of T-DNA insertion mutants with decreased virulence in
RT the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL Appl. Microbiol. Biotechnol. 100:8889-8900(2016).
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:PMB73468.1}.
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DR EMBL; MRVG01000001; PMB73468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6P1R0; -.
DR OMA; CLHYYVH; -.
DR Proteomes; UP000235728; 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:UP000235728};
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 112..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 93269 MW; FCEB882953E59CEE CRC64;
MGIPAAFRWL SNKYPKIISP VVEDRPIVMD DGTEIPVDIT RANPNGEELD NLYLDMNGIV
HPCAHPEDKP APKDEEEMML EIFKYTDRVV NMVRPRKILM IAVDGVAPRA KMNQQRSRRF
RSAQEAKEKE NDKQELIKLL KQQNGGSLTA ESTESVTKKA FDNNSITPGT PFMDILASSL
RYWCQYKLNT DPGWAKLKVI ISDATVPGEG EHKIMNFVRS QRASPDYDPN TRHVIYGLDA
DLIMLGLATH EPHFRVLRED VFFQDSKARA CKLCGQKGHD AQNCKGETKE QTEEFDAKDN
ALTLKPFIWL HVSVLREYLA AELAIPELPF RFDLERVIDD WIFMCCFVGN DFLPHLPALE
IREHGIDTLT TIWKRNLPAL GGYITKDGHI DLERAQCILD GLAGQEDMIF KKRREQEDRR
EASAKRRRLQ NNGATGRDNR SDGKGLKSGH EDPSRGLALH PIGSMPIAPL KAITHDMTVN
RTGAADANVA NKSAASVLKE RLKAGRGALS PEANSKDTKD PPSHSVPVKR KLSAVEAFAE
STSNDAQGTN TPGDKAETPA DPVRLWEDGY ADRYYQLKFH RDPGDISFRT HVAHAYVEGL
AWVLQYYFQG CPSWEWYYPY HYAPFAADFK DISQANVTFE KGTVSRPFEQ LMSVLPAASR
DNLPEVFHSL MTDQDSLIID FYPEEFEVDL NGKKMAWQGV ALLPFIEMDR LLAAVQKRYP
LLSDEDRKRN GVGRDVLLLS DSHESIYDEI LTNFYSKKQG STQFRLNPKT SDGLSGYVEK
QEGYVPHGTL HYPLERKSMP DLDYDRSMRY VNDILPGHGN TKVH
//
