ID A0A4U6UDU7_SETVI Unreviewed; 1074 AA.
AC A0A4U6UDU7;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 03-MAY-2023, entry version 12.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN ORFNames=SEVIR_5G054800v2 {ECO:0000313|EMBL:TKW12734.1};
OS Setaria viridis (Green bristlegrass) (Setaria italica subsp. viridis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4556 {ECO:0000313|EMBL:TKW12734.1, ECO:0000313|Proteomes:UP000298652};
RN [1] {ECO:0000313|EMBL:TKW12734.1, ECO:0000313|Proteomes:UP000298652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. A10 {ECO:0000313|Proteomes:UP000298652};
RA Huang P., Jenkins J., Grimwood J., Barry K., Healey A., Mamidi S.,
RA Sreedasyam A., Shu S., Feldman M., Wu J., Yu Y., Chen C., Johnson J.,
RA Rokhsar D., Baxter I., Schmutz J., Brutnell T., Kellogg E.;
RT "WGS assembly of Setaria viridis.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. Acts as an
CC endogenous post-transcriptional gene silencing (PTGS) suppressor.
CC {ECO:0000256|PIRNR:PIRNR037239}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC subfamily. {ECO:0000256|ARBA:ARBA00006994,
CC ECO:0000256|PIRNR:PIRNR037239}.
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DR EMBL; CM016556; TKW12734.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U6UDU7; -.
DR EnsemblPlants; TKW12734; TKW12734; SEVIR_5G054800v2.
DR Gramene; TKW12734; TKW12734; SEVIR_5G054800v2.
DR OMA; CLHYYVH; -.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000298652; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
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:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
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:SF56; 5'-3' EXORIBONUCLEASE; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 Reference proteome {ECO:0000313|Proteomes:UP000298652};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 263..277
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 137..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 493..521
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 824..838
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1074 AA; 121684 MW; CEE29DBADC2030F6 CRC64;
MGVPAFYRWL AEKYPMVVVD VVEEEAVEIE GVKVPVDTSK PNPNGLEFDN LYLDMNGIIH
PCFHPEDRPS PTTFGEVFQC MFDYIDRLFV MVRPRRLLYM AIDGVAPRAK MNQQRSRRFR
AAKDAADAAA EEERLREEFE REGRKLPPKQ QSQTCDSNVI TPGTEFMAVL SVALQYYIHL
RLNYDPGWKQ IKVILSDANV PGEGEHKIMS YIRGQRNLSG FKPNTRHCLY GLDADLIMLA
LATHEVHFSI LREVVYTPGQ QDKCFLCGQV GHLAANCEGK VKRKAGEFDE KGDAIVPKKP
YQFLNIWTLR EYLEYEFRMP NPPFQIDFER IVDDFIFMCF FVGNDFLPHM PTLEIREGAI
NLLMAVYKKE FPSMGGYLTD SCTPDLDRVE HFIQAVGSYE DKIFQKRARL HQRQAERIKR
EKAQAKRGDD LDPHVRDDLI VPVQRFQGSR LASGAVPAPY EQNGSHKDNK EMNNRARKAA
RVSTSGSSIA AAIVDAENDL EAQERDNKEE LKSMLKDALR EKSDIFNSEN PEEDKVKLGE
PGWRERYYEE KFGARTPEQI EEIRRDVVLK YTEGLCWVMH YYYEGVCSWQ WFYPYHYAPF
ASDLRDLGQL DITFELGTPF KPFDQLMGVF PAASAHALPL QYRRLMMDPN SPIIDFYPTD
FEVDMNGKRY SWQGIAKLPF IDEARLLAEI KKVEHTLTPE EARRNSVMFD MLFVNGSHPL
SPYIYSLNSK FGHLPDKERN EIKEKLDPSA SGGMNGYITL CSGDPCPPIF RSPVDGLEDI
MDNQVICSIY KLPDHHKHIA RPPAGVIIPK KTVEAGDLKP PPVLWHEDSG RRPHDNSNRH
NPPGAISGRQ LGEAAHRLVI NSLNAHGRGQ HNGPSMPYQT IMNGMHHLNV VHPIGNQGMP
PRVEQSAGRP GWNVPRDSVP DGQIPAYASS GSGHYQYDRS GQYEQGNRGR QQNHPYARDG
YHDARGRVPP AYGYQQTGGN MYSSQPVALP PGPGLYGQQP PSAYPGVRGG GYQPPPYGGA
QQWQQQPYSS YAGRGPYGGG PPPTRADSRS QQSQNRYGAL DRSSNRRPPS GYGR
//
