ID G0MPQ3_CAEBE Unreviewed; 850 AA.
AC G0MPQ3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
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 ORFNames=CAEBREN_09077 {ECO:0000313|EMBL:EGT39859.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) 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; GL379805; EGT39859.1; -; Genomic_DNA.
DR AlphaFoldDB; G0MPQ3; -.
DR STRING; 135651.G0MPQ3; -.
DR EnsemblMetazoa; CBN09077.1; CBN09077.1; WBGene00147802.
DR eggNOG; KOG2102; Eukaryota.
DR HOGENOM; CLU_002333_5_2_1; -.
DR InParanoid; G0MPQ3; -.
DR OMA; EVAEHCN; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
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 GO; GO:0042659; P:regulation of cell fate specification; IEA:EnsemblMetazoa.
DR GO; GO:0040034; P:regulation of development, heterochronic; IEA:EnsemblMetazoa.
DR Gene3D; 2.40.50.690; -; 1.
DR Gene3D; 2.40.50.700; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_03045; DIS3L2; 1.
DR InterPro; IPR041505; Dis3_CSD2.
DR InterPro; IPR028591; DIS3L2.
DR InterPro; IPR041093; Dis3l2_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR033771; Rrp44_CSD1.
DR PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR Pfam; PF17877; Dis3l2_C_term; 1.
DR Pfam; PF17849; OB_Dis3; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF17216; Rrp44_CSD1; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
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};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_03045};
KW Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03045}.
FT DOMAIN 334..688
FT /note="Ribonuclease II/R"
FT /evidence="ECO:0000259|SMART:SM00955"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
FT SITE 354
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
SQ SEQUENCE 850 AA; 96829 MW; C697212F7CD34A2D CRC64;
MSEVVESKVD EQEPSNSTLK PTGFTQTATG GQFGAASPIK STPTKQAPYV KKYVHSPNNK
NPPRKIFQDY ISQEETDAGL KDKTMFKAVL RINPKNYQEC FLDHPKGTEY PDVLVLGQDR
NRAMQGDVVI VKMKPKEEWL VNYPEYVKWW GLNKKTERKL GKVDNNTNKP DKRCLQNEID
DNGVTSEEVP ESCLISIGSI VRIDEKKHFR VAAGKLQLMP NSANPNVLFV ATDSRVPRIL
IPKAEIDQEF FTRPKDFEKF LYTAKINEWR ADSIYAEGTL IKLLGMSGEI ETETERIVYE
HQIDHREFSD ECLASLPISS AEDWKIPEKE FEYRRDFRQE IVFTIDPKTA RDLDDALHAK
HIDDCDGKGT PGVEIGVHIA DVTFFLKEDT ELDKWASERG NSTYLSQLVI PMLPRILCEQ
LCSLNPGVDR LAFSTVFKLN YEGELKDVWF GRSIIRSRVK LAYEHAQDFI EHPEKDFTTE
ELPPISDGNT PFEIREKTLM LHRIAQLLRK QRESNGALRI ELPKLKFALD EDKKPQGVSI
YEIKDSNKLV EEFMLLANME VAKKIGSAFP NSALLRNHPP PKEKMIKDVA EQCAKIGFPL
DGKTSGMLST SLRKYQGNTR LDMCIRQVIS SLTIKPMQQA KYFCTADMPP SFFHHYALNV
DHYTHFTSPI RRYPDVIVHR QLAASLGYNE KCDRDPKEIQ NICTRCNDTK QASKEASEES
ATLYFGVFIH SVGKMTCQAV VLGVMDLSFD VLVVEYGVVK RVYVDKMKRE FDKIPEQLTL
HWPADPNAES GNKDAFSTVI QMCCVITVVL SPTKDVDVNA IMLRPTLEQR NILKSTLKDM
LETGSNILES
//
