ID A0A165U432_9APHY Unreviewed; 1459 AA.
AC A0A165U432;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 03-MAY-2023, entry version 26.
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=DAEQUDRAFT_660280 {ECO:0000313|EMBL:KZT74372.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT74372.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT74372.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT74372.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV429033; KZT74372.1; -; Genomic_DNA.
DR STRING; 1314783.A0A165U432; -.
DR OrthoDB; 945235at2759; -.
DR Proteomes; UP000076727; 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 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 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 SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
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:UP000076727};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_03045}.
FT DOMAIN 884..1221
FT /note="Ribonuclease II/R"
FT /evidence="ECO:0000259|SMART:SM00955"
FT REGION 1..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 896
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
FT BINDING 905
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
FT SITE 904
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
SQ SEQUENCE 1459 AA; 160420 MW; E4D50EA4A7421CDB CRC64;
MTDETAPSTQ QQNVPKKDER KPASTGSGGQ GNGPRKRNPS RTASVSANNA NASAPRPSSR
ASNKSTNKKG PSNAPAGTDS GSESKKGNEP KKNEQRGKSQ GGGNARGNGH RKGQSTAQSR
QGSNKPNTPQ PKQPSNSPAP QTVPDNSDAL SSLQRVIADL KTTSNPSQTP NAQTSNLPAN
APVFQPGASA FPGSQAQLQN EQPPRHRKAA SLGTAGNPAY NSYSPNLGSM MEDVEEGQTN
FPMEEGEINE AAYPAAHQRR SLSQSFTAPR FAALAAQQEG EVPGPTGRPQ LAPGFMFGAR
RRPSQSVNSP MGPPINEEDV GFQFPQQQQQ QNFDLAGEMN QRKNENGPEI SGIMAEQIAL
QNQIEVLQQQ QAALYQQQLA SNQVLSFQTP GLAPGRPNVH RRVHSTVPMG MGMNPFGGPQ
AAMGQFGNIG NLSMGLDGQP SGVPRGHGRR HSVNVLNKSG SPGLGALGFS QSADGFDDGF
TAPGGNGHTR NDSSWRINGG VGGLQNNGGF AADLAQAQAQ LNSLQQFRAA AGGHHQKMAS
FSFPNMLPNM MAANMMGLGL GGMNLLQQQQ QQFQSQLQQQ SNQPQRKSLF APYLPQASLP
PLLAAGKLVV GILRVNKRNR SDAYVATEVL DADIYICGSK DRNRALEGDI VAVELLDVDE
VWGTKKEKEE KKRKKEENSA YDLKGAAGRK NDKKKDDVEV EGQGLMLFED EEVTDDVKPQ
FAGHVVAVVE RMPGQLFSGT LGLLRPSSAA TKEKQEAERR EREGDKGDEP RRQIERPKIV
WFKPTDKRVP LIAIPTEQAP ADFVQNSEAY ANKLFVACIK RHPISSLHPF GTLVEELGPI
GDIEVETSAL LKDCNFPTEE FSENVLKCLP PMPWSIPDHE LEGRKDLRGE RVFTVDPDTA
KDLDDALSVK ANEDGTFDIG VHIADVSYFV KPNSALDRDA RKRATSVYLV QRAVPMLPPA
LSEQLCSLIP GQERLAFSVI FTMTADAKVV KKWFGKTVIR SSAKFFYKDA AVLLEGHTLD
IEDVPEQTAA DYVNDLKVLN DLAHQLRERR YKSGCIRTEP LKLTFKLDEN GLPVDCDQYE
RGDAHHLVEE FMLLANTAVA QQVAVHFTEQ ALLRRHDPPI ERRINAFVER AARMGFKVDV
SSPAALMQSL EAINDPTARK TLELYLRKAS SSAKYFCTGM LDIAKYGHYA LNIPLYTHFT
SPIRRYADIL VHRQLDSILQ GGSEPKFTMD RDAVAKVAQQ CNIKRDSAKL AQEQSTHLYL
CILIHDLTQR YGPVIREAKV VGVLDAAFDV LVPEFGIEKR VHVDQMPIDN HVYDEHTHTL
QIYWSNRDVI TWLAENSDDE HLKNVKQNAE QHALKMEVAS RSVHDEKALF DEDDGEDEIV
LGRDEREKED ETISKQRQLS KRRIAPRFEG LRTTPSGHKI QEIKELQTVP VIVTADLTKS
PPVIKVYSVN PYAEKFEYK
//
