ID A0A3L6PNM0_PANMI Unreviewed; 1052 AA.
AC A0A3L6PNM0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN ORFNames=C2845_PM14G04320 {ECO:0000313|EMBL:RLM61434.1};
OS Panicum miliaceum (Proso millet) (Broomcorn millet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX NCBI_TaxID=4540 {ECO:0000313|EMBL:RLM61434.1, ECO:0000313|Proteomes:UP000275267};
RN [1] {ECO:0000313|Proteomes:UP000275267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT "The genome of broomcorn millet.";
RL Nat. Commun. 10:436-436(2019).
CC -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. Acts as an
CC endogenous post-transcriptional gene silencing (PTGS) suppressor.
CC {ECO:0000256|PIRNR:PIRNR037239}.
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:RLM61434.1}.
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DR EMBL; PQIB02000016; RLM61434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6PNM0; -.
DR STRING; 4540.A0A3L6PNM0; -.
DR Proteomes; UP000275267; Chromosome 14.
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: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 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000275267};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
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 415..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 490..518
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 464..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1052 AA; 119135 MW; C0678252ED83F164 CRC64;
MGVPAFYRWL AEKYPMVVVD VVEEEPVEIE GVCVPVDTSK PNPNGIEFDN LYLDMNGIIH
PCFHPEDRPS PTTFAEVFQC MFDYIDRLFV MVRPRKLMYM AIDGVAPRAK MNQQRSRRFR
AAKDASDAAA EEERLREEFE REGRRLPAKQ QSQTCDSNVI TPGTEFMAVL SVALQYYIHL
RLNYDPGWKQ IKVILSDANV PGEGEHKVMS YIRGQRNLPG FNPNTRHCLY GLDADLIMLA
LATHEVHFSI LREVVYTPGQ QDKCFLCGQV GHLAANCEGK AKRKAGEYDE KGEAIVPKKP
YQFLNIWTLR EYLEYEFRMP NPPFKIDFER IVDDFIFMCF FVGNDFLPHM PTLEIREGAI
NLLMAVYKKE FPAMGGYLTD SCTPDLNRVE HFIQAVGSYE DKIFQKRARL HQRQAERIKR
EKAQAKRGDD LDPHVRDDLI VPVANFRGSR LASGAVPSPY EQNGAHRERN SQPQKAARVS
SSGSSIAAAI VEAENDLEAQ ERDNKEDLKS RLKNAIREKS DVFNSENPEE DKVKLGEPGW
RDRYYEEKFG ARTSDQMEEI RRDVALKYTE GLCWVMHYYY EGVCSWQWFY PYHYAPFASD
LRNLSQLNIT FQLGSPFKPF DQLMGVFPAA SSHALPLQYR QLMTDPNSPI IDFYPTDFEV
DMNGKRFSWQ GIAKLPFIDE DRLLAEIKRV EHTLTPEEAR RNSTMCNMLF VNGSHPLSPY
IYSLNSKFGN MPDKDGNEIK EKLDPSPSGG MNGYIALCAG DPSPPVFRSP VDGLEDIMDN
QVICSVYKLP DPHKHIARPP AGVIIPKKSV EAGDLKPPPV LWHEDSAALK IHAYLVLMKW
SRQNPAGALS GRQLGEAAHR LVVNSLNVRG GGQHNAPSMP YQTIMNGTNY SNGRHHMGNQ
GVPPRMEQPA GHSGWHVPSD NMTNGQAAYG HQHERAGPSR HERDNRGRQH YHPYARDNHH
DSRGRVPPPP GYHQNHGNSH PAAPSAGPGR YGQPSPAYGG GYQPAPYGAQ QWQQRPYGGG
APPTRPNSQQ SQNRYGTLDR GSNKRPSSHG RY
//
