ID A0A0R0GK30_SOYBN Unreviewed; 1151 AA.
AC A0A0R0GK30;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=DIS3-like exonuclease 2 {ECO:0000256|HAMAP-Rule:MF_03045};
DE EC=3.1.13.- {ECO:0000256|HAMAP-Rule:MF_03045};
GN Name=100815252 {ECO:0000313|EnsemblPlants:KRH18782};
GN ORFNames=GLYMA_13G082100 {ECO:0000313|EMBL:KRH18782.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH18782.1};
RN [1] {ECO:0000313|EMBL:KRH18782.1, ECO:0000313|EnsemblPlants:KRH18782}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH18782};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH18782.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH18782}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH18782};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH18782.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH18782.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 3'-5'-exoribonuclease that specifically recognizes RNAs
CC polyuridylated at their 3' end and mediates their degradation.
CC Component of an exosome-independent RNA degradation pathway that
CC mediates degradation of cytoplasmic mRNAs that have been deadenylated
CC and subsequently uridylated at their 3'. {ECO:0000256|HAMAP-
CC Rule:MF_03045}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03045};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03045};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03045}.
CC Cytoplasm, P-body {ECO:0000256|HAMAP-Rule:MF_03045}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. DIS3L2 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03045}.
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DR EMBL; CM000846; KRH18782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R0GK30; -.
DR PaxDb; 3847-GLYMA13G02760-2; -.
DR EnsemblPlants; KRH18782; KRH18782; GLYMA_13G082100.
DR Gramene; KRH18782; KRH18782; GLYMA_13G082100.
DR Proteomes; UP000008827; Chromosome 13.
DR ExpressionAtlas; A0A0R0GK30; baseline and differential.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IEA:InterPro.
DR GO; GO:1990074; P:polyuridylation-dependent mRNA catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.50.690; -; 1.
DR Gene3D; 2.40.50.700; -; 1.
DR HAMAP; MF_03045; DIS3L2; 1.
DR InterPro; IPR041505; Dis3_CSD2.
DR InterPro; IPR028591; DIS3L2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR Pfam; PF17849; OB_Dis3; 1.
DR Pfam; PF00773; RNB; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03045};
KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_03045};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03045};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03045};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_03045};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03045}; Nuclease {ECO:0000256|HAMAP-Rule:MF_03045};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_03045}.
FT DOMAIN 522..876
FT /note="Ribonuclease II/R"
FT /evidence="ECO:0000259|SMART:SM00955"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 534
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
FT BINDING 543
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
FT SITE 542
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
SQ SEQUENCE 1151 AA; 128484 MW; 544B03D8C5776590 CRC64;
MRPAVEGSMA ERFDDGEKEK KKKKRRSNRR SKQNPPSSSA SEVNEAQGLS PDSGKIGTPT
HASPSLGNSL NQVNVCSSNE QGLSKASNVA FISIPPMHIN EQVEPGDLRI LPMCGGGIDS
NSFSEPTGCR GSSGINKNKD SVPCGQIGLC GQEKYFSPHW SVEAVEKELE EGDVFKALFH
VNAHNRLEAY CKIDGMPTDV FIGGIPAQNR AVEGDVVAVK FDPLPLWTKM KGPNGSCNNT
ATPEGCNLTE DKEVGGNICK GKAKVDAEYE SAHGRSYPGQ NKEDADQNSL YKSYPFTETT
MVYDDITSRG STNHLDLHGM ANHDSINGHH CAAPNSLKIN SCSGQSNAVE KMCLLVNSFP
SKRPTGRVVA IIERSPRREG IVGHINVKQW VSFRDTSKKD VKKNKNLISE HEYIQLIPTD
PKFPNMMLLV RKLPKCIKKR MKSGDVTIQM DLVAVQIDDW VEESPFPEAH ILRVFGQGGE
VQTQLDAILF QNAICLSEFS PEALSCLPCV PWEIPLKEIQ SRIDLRNLCI FTIDPSTATD
LDDALSIEKL PNGNYRVGVH IADVSYFVLP DTALDNEAKF RSTSVYMLQR KLPMLPALLS
ENIGSLSPGV DRLAVSMLLD INVAGDVVDR WIGRTVIQSC CKLSYEHAQD IIDKAFDFEG
SNFIEDGYPR VYGHFEWPDV IMSLESLYEI SNVLKQKRFT DGALRLENPK VVILFDENGV
PYDSRLSERK ESNFLVEEYM LLANRIAAEV ICRAYPDGAL LRRHPEPNMR KLREFMAFCQ
KHGLELNTSS SGELHWSLEQ IREKLKGDPV LYNILISYAT RPMQLASYFC SGDLKDSENE
WGHYALAVPF YTHFTSPLRR YPDIIVHRTL LATIEAEELY MKHQKALQGS KEVKVQKRCF
TGINFDKSAA ESTEGREALS AAAVKHSVPC AETLADIATY CNGRKLASRN VKDACDKLYI
WFLLKKKEVL LSEARILGLG PRFMSIYIQK LAIERRIYYD EVQGLTVEWL ETTSTLVLSM
STNKCAYRRG CPNKLRPFEE VALLTCPYNL DFTTDNSNPS EVMKVDDSIS AMDREPISRS
DALETLIDPA FFPLTVRLLS TIPVALHAVG GDDGPLDIGV RLYMSSYIGF GKNFTSWSWK
RRVVVLIKDL G
//
