ID G0SYN8_RHOT2 Unreviewed; 1450 AA.
AC G0SYN8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 03-MAY-2023, entry version 48.
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=RTG_01817 {ECO:0000313|EMBL:EGU12196.1};
OS Rhodosporidium toruloides (strain ATCC 204091 / IIP 30 / MTCC 1151) (Yeast)
OS (Rhodotorula glutinis (strain ATCC 204091)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1001064 {ECO:0000313|EMBL:EGU12196.1, ECO:0000313|Proteomes:UP000006141};
RN [1] {ECO:0000313|EMBL:EGU12196.1, ECO:0000313|Proteomes:UP000006141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204091 / IIP 30 / MTCC 1151
RC {ECO:0000313|Proteomes:UP000006141};
RX PubMed=24526636; DOI=10.1128/genomeA.00046-14;
RA Paul D., Magbanua Z., Arick M.II., French T., Bridges S.M., Burgess S.C.,
RA Lawrence M.L.;
RT "Genome sequence of the oleaginous yeast Rhodotorula glutinis ATCC
RT 204091.";
RL Genome Announc. 2:E0004614-E0004614(2014).
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: 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:EGU12196.1}.
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DR EMBL; AEVR02000009; EGU12196.1; -; Genomic_DNA.
DR HOGENOM; CLU_002333_0_0_1; -.
DR InParanoid; G0SYN8; -.
DR Proteomes; UP000006141; 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; 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:UP000006141};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_03045}.
FT DOMAIN 875..1213
FT /note="Ribonuclease II/R"
FT /evidence="ECO:0000259|SMART:SM00955"
FT REGION 1..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1350..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 887
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
FT BINDING 896
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
FT SITE 895
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
SQ SEQUENCE 1450 AA; 156034 MW; 87BF8763512DD4F0 CRC64;
MSSPTDTTKP ASGSSGTKDD TQSAQQPTRK QAASPNSPAR NRSQHDRKRS TSRGNGGASS
PTNERKPQNQ QGGGGGAGGS HGRRSSRGGG HAGNGGGASG RRSSGGGHGG SSGGQQHHRR
ESQQNDGLAN LQNVISDMPP PPGGPARSSS SQPSSPARQR SQPGGGHRKN PSGTSVPSIS
APPPTLPPAA NTLNPTAGGF QPGMLGPIHD MIDEGLVTPT ASRFDLMTGM PRSPTAPSTL
PDAGTGFGGV AAVNQSAFVF PPPQPATQGL GISNQQQQAL ALQQQQFQLA QLAAGMNPAL
AGAGGGLNEA SELIAEQLAI QQQLENLRLQ QESLMARFGD MQATLTGQAA PPVSAPPPSG
PSGQHRRVSS SSGHQHQPSG AMGSFGLPGG VGAAASQQQL PKGHGRRHSV QTGKTAPGGA
NGSTAAPSGN GGFGTGFQFP PRPQGQQQGT PTQQARFLEE DPFASGNDSP SGGRTMGHHR
RQSGSVSSLG GWSMNMSQSS TNNLAEAQAH LQALGAYRAS SGHARVPSFG MSAIGPGGQG
GPGQLAMAGY GGGIPQPGMG GPNGQNQMRK TLFAPYLPQA SIPPLLAAGK LVIGTLRVNK
RNRSDAYVAT DVLDADIYIC GSKDRNRALE GDIVAVELLD VDEVWGTKKD KEEKKRRKEE
QASYDPKTAR DLRKQDKKKD DVEVEGQGLL LFEDEEVTDE TKPQFAGHVV AVLERAPGQL
FSGMLGVLRP SSAATQQKQD AERREREGVD LRGGHGQSNG SSQPPPKIIW FRPTDKRVPL
IAIPTEQAPA DFVEHSEKYS DRLFVACIKR WPITSLHPFG QLVEELGPIG DIETETNALL
KDCNFTAEDF SDSVNKCLPP TPWSIPDREL QPDVRRDLRD KRVFTIDPET AKDLDDALHI
IQNEDGTFEV GVHIADVSHF VKPNTPLDRE ARKRATTVYL VQRAVPMLPP TLSEELCSLN
AGSDKLTFSV IFTLTPEGQI VSTWFGKTVI NSKVKLAYSD AQHVIDNGTL PEGKIADAEL
REGVETDVKR LAGIAKHLRH RRFDSGALRI DNVKVSFRLD EFGLPVDAHE YARKEANELI
EEFMLMANIA VAGKIASGLP DQSLLRRHEE PIDRRLDAFV QRMRRLGLDI DGSSSHALMD
SIVKITDPGE RLTLQHLSTR SMQRAKYFCT GMLDISKYRH YALNVPLYTH FTSPIRRYAD
VIVHRQLEAV LIAQAAAASA ETPTEAKFSL DAEAVSKIAQ TCNVKKEAAR LAQEQSQHLF
LCVLIDDLTK RYGPVIRYGT VIGVLDQAFD VLVSEFGVEK RVHVDQMPVE STVYDERENS
LQIFWKKGVD VLAWLAESNQ DEHLKRLRAH AHHHSKMMEA DSGKGEAESR LFDDDEEEEE
GEVKQERRVL ETAQHKKSRD RTPLKFQNLN TEHGHCAQTV KTLDVVPVIV SADITKSPPV
LRVVAVSPFA
//
