ID A0A060SME1_PYCCI Unreviewed; 1499 AA.
AC A0A060SME1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=BN946_scf184858.g10 {ECO:0000313|EMBL:CDO75570.1};
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO75570.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO75570.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO75570.1,
RC ECO:0000313|Proteomes:UP000029665};
RA Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA Pontarotti P., Henrissat B., Record E.;
RT "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT breakdown.";
RL Submitted (JAN-2014) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03045}.
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:CDO75570.1}.
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DR EMBL; CCBP010000280; CDO75570.1; -; Genomic_DNA.
DR STRING; 5643.A0A060SME1; -.
DR HOGENOM; CLU_002333_0_0_1; -.
DR OMA; QIQATHQ; -.
DR OrthoDB; 945235at2759; -.
DR Proteomes; UP000029665; 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; 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}; Nuclease {ECO:0000256|HAMAP-Rule:MF_03045};
KW Reference proteome {ECO:0000313|Proteomes:UP000029665};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_03045}.
FT DOMAIN 898..1254
FT /note="Ribonuclease II/R"
FT /evidence="ECO:0000259|SMART:SM00955"
FT REGION 1..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 910
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
FT BINDING 919
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
SQ SEQUENCE 1499 AA; 163389 MW; DAB745BD1A23B83A CRC64;
MTDEITPQTQ QTAPKKDEKK QQTSASGNGA ASQGGNKQPP KKNTPAGRSA SISGGGAGGA
RPSSRSSNRS SSKKGSTNAQ GAADSGSESA NANARKGNEG GRQRGKSQGG GGNGPRGGSG
HRKASQSTSQ GGRQGASNGG NKPKQSSGSP APAPNNESSD ALSSLQRVIA DLKTTSPPTN
AGNTNPSISA AAGSTLPPNA PIFQPGAVSF PGTNLSEQPP RHRKAASLGA SAFSSSMAYS
PNLGSMIEDA EDGHGHSLVE EGEIQENPYQ TGHPRRSLSQ NFTAPRFAAL AAQQQEQTEL
VGPTGRPQLA PGFMFGARRR PSSNLTMGPP INEEDVGFQF PQQQSQRSYE SADASHRKPE
EYKDIMAEQI AIQTQIEALQ QQQQALYHQQ LASNQVLSSF QSPGFAPGRG AHRRVHSTVP
MSVGLNAFGG SHTTMGQFGN LGSLGMGLDG QPSSVPRGHG RRHSVNVLNK TGGPSLASLG
LSASVDGFDD GFVPPAGLGG SGHSRSDSSW RLNGGAGALQ PNNFASDLAQ AQAQLQSLQQ
FRAAAGGHHQ KMPSFSFPNM LPNMMAANMM GLGLGGINLL QQQQQQFQSQ LQQQSNQPQR
KSLFAPYLPQ ASLPPLLAAG KLVVGILRVN KRNRSDAYVA TEVLDADIYI CGSKDRNRAL
EGDIVAVELL DVDEVWGTKK EKEEKKRKKE ENSAYDLKGA AGRKNDKKKD DVEVEGQGLM
LFEDEEVTDD VKPQYAGHVV AVVERMPGQL FSGTLGLLRP SSAATKEKQE AERREREGDK
GDEPRRPIER PKIVWFKPTD KRVPLIAIPT EQAPPDFVQN SEAYANKLFV ACIKRHPISS
LHPFGTLVEE LGPIGDIEVE TSALLKDCNF PTEDFSDNVL KCLPPTPWTI PERESDVRKD
LRGERVFTID PEDAKDLEDA VSVKANEDGT YDIGVHIADV SYFVKPNTAL DRDARKRATS
VYLVQRAVPM LPPTLSEQVC SLLPGQERLA FSVIFTMTKD AKVVKKWFGK TIIKSAAKLS
YNDAQAVIEG KSLGDVPVIP EHDAAGIAHD IKVLDDIAKQ LRARRYQNGC VKSHSLRLKF
KLDENGMPID CGPYERTEAH KLIEEFMLQT NIAVAQQVAV HFSEQAMLRR QDSPIDRRLV
RERLMTSRPH LDWLQRMFSS TYARERLGYT VDTSSVTALM KSLEAVQDPT ARTILEILLQ
KASPRAKYFC AGMLDIAKYG HYALNIPLYS HFTSPIRRYA DILVHRQLDA ILNGGPEPKF
NMDRDAVAKV AQQCNIKRDS AKLAQEQSAH LFLCVLISDL TQRYGPVIRQ AKVIGVLDAA
FDVFIPEFGI EKRVHVDQMP IDNHVYDEHT HSLQIYWSNR DVITWLAENS DDEHLKKVKQ
NAEQHALKME VASRSVHDEK ALFDEDDDTE EDEIVLGRAN DKVSDESELT SKQRMLSKQK
IPPTFEGLKT LPSGHKIQEI RELMTVPVIV TADLTKSPPV IKVYSVNPYA QEDKAKGSA
//
