DI3L2_SCHPO
ID DI3L2_SCHPO Reviewed; 927 AA.
AC O14040; Q9USE3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=DIS3-like exonuclease 2 {ECO:0000255|HAMAP-Rule:MF_03045};
DE EC=3.1.13.- {ECO:0000255|HAMAP-Rule:MF_03045};
GN Name=dis32; Synonyms=dis3l2; ORFNames=SPAC2C4.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 477-660, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-461.
RX PubMed=23503588; DOI=10.1038/emboj.2013.63;
RA Malecki M., Viegas S.C., Carneiro T., Golik P., Dressaire C.,
RA Ferreira M.G., Arraiano C.M.;
RT "The exoribonuclease Dis3L2 defines a novel eukaryotic RNA degradation
RT pathway.";
RL EMBO J. 32:1842-1854(2013).
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:0000255|HAMAP-
CC Rule:MF_03045, ECO:0000269|PubMed:23503588}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03045};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03045};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23503588}.
CC Cytoplasm, P-body {ECO:0000269|PubMed:23503588}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. DIS3L2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03045}.
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DR EMBL; CU329670; CAB16367.1; -; Genomic_DNA.
DR EMBL; AB027825; BAA87129.1; -; Genomic_DNA.
DR PIR; T38518; T38518.
DR RefSeq; NP_594510.1; NM_001019939.2.
DR PDB; 4RO1; X-ray; 2.80 A; A/B=170-927.
DR PDBsum; 4RO1; -.
DR AlphaFoldDB; O14040; -.
DR SMR; O14040; -.
DR BioGRID; 279097; 21.
DR STRING; 4896.SPAC2C4.07c.1; -.
DR iPTMnet; O14040; -.
DR MaxQB; O14040; -.
DR PaxDb; O14040; -.
DR EnsemblFungi; SPAC2C4.07c.1; SPAC2C4.07c.1:pep; SPAC2C4.07c.
DR GeneID; 2542643; -.
DR KEGG; spo:SPAC2C4.07c; -.
DR PomBase; SPAC2C4.07c; dis32.
DR VEuPathDB; FungiDB:SPAC2C4.07c; -.
DR eggNOG; KOG2102; Eukaryota.
DR HOGENOM; CLU_002333_5_2_1; -.
DR InParanoid; O14040; -.
DR OMA; MADGNRN; -.
DR PhylomeDB; O14040; -.
DR PRO; PR:O14040; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:PomBase.
DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0000291; P:nuclear-transcribed mRNA catabolic process, exonucleolytic; IMP:UniProtKB.
DR GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IGI:PomBase.
DR GO; GO:1990074; P:polyuridylation-dependent mRNA catabolic process; IMP:UniProtKB.
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 Pfam; PF17849; OB_Dis3; 1.
DR Pfam; PF00773; RNB; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; SSF50249; 2.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Exonuclease; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Nuclease; Reference proteome; RNA-binding.
FT CHAIN 1..927
FT /note="DIS3-like exonuclease 2"
FT /id="PRO_0000314756"
FT REGION 1..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03045"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03045"
FT SITE 461
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03045"
FT MUTAGEN 461
FT /note="D->N: Loss of exoribonuclease activity."
FT /evidence="ECO:0000269|PubMed:23503588"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:4RO1"
FT HELIX 360..363
FT /evidence="ECO:0007829|PDB:4RO1"
FT TURN 364..369
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 387..393
FT /evidence="ECO:0007829|PDB:4RO1"
FT HELIX 395..410
FT /evidence="ECO:0007829|PDB:4RO1"
FT TURN 420..424
FT /evidence="ECO:0007829|PDB:4RO1"
FT HELIX 435..439
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 449..453
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 462..468
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 470..481
FT /evidence="ECO:0007829|PDB:4RO1"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:4RO1"
FT HELIX 492..500
FT /evidence="ECO:0007829|PDB:4RO1"
FT HELIX 516..519
FT /evidence="ECO:0007829|PDB:4RO1"
FT TURN 520..523
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 531..541
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 551..557
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 561..564
FT /evidence="ECO:0007829|PDB:4RO1"
FT HELIX 565..573
FT /evidence="ECO:0007829|PDB:4RO1"
FT HELIX 577..580
FT /evidence="ECO:0007829|PDB:4RO1"
FT HELIX 591..612
FT /evidence="ECO:0007829|PDB:4RO1"
FT TURN 613..616
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 625..629
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 635..640
FT /evidence="ECO:0007829|PDB:4RO1"
FT HELIX 645..665
FT /evidence="ECO:0007829|PDB:4RO1"
FT TURN 666..668
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 670..672
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 674..678
FT /evidence="ECO:0007829|PDB:4RO1"
FT TURN 683..686
FT /evidence="ECO:0007829|PDB:4RO1"
FT HELIX 687..695
FT /evidence="ECO:0007829|PDB:4RO1"
FT HELIX 705..715
FT /evidence="ECO:0007829|PDB:4RO1"
FT TURN 716..718
FT /evidence="ECO:0007829|PDB:4RO1"
FT HELIX 721..734
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 739..742
FT /evidence="ECO:0007829|PDB:4RO1"
FT HELIX 743..745
FT /evidence="ECO:0007829|PDB:4RO1"
FT HELIX 749..751
FT /evidence="ECO:0007829|PDB:4RO1"
FT TURN 755..758
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 759..761
FT /evidence="ECO:0007829|PDB:4RO1"
FT TURN 768..770
FT /evidence="ECO:0007829|PDB:4RO1"
FT HELIX 773..783
FT /evidence="ECO:0007829|PDB:4RO1"
FT TURN 784..787
FT /evidence="ECO:0007829|PDB:4RO1"
FT HELIX 794..831
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 843..848
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 853..857
FT /evidence="ECO:0007829|PDB:4RO1"
FT HELIX 859..861
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 862..866
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 909..912
FT /evidence="ECO:0007829|PDB:4RO1"
FT STRAND 917..920
FT /evidence="ECO:0007829|PDB:4RO1"
SQ SEQUENCE 927 AA; 105150 MW; DE144A3F95632BC2 CRC64;
MDLKPNIRRK EKRNLLKGEA ALEKKGSIDR KTKNKAYPST THDPHQNDDS NIPGLGSGLL
ERIKDIVQRP TDTQLKGQDS NHKKASLTET KTEKAKVKPK AKKKNSKEKI SKSSKQDEHK
TDVHKESVSK LSKNLESRNN RDENSAKREK NNSHQVEADT NNATEMVSSN AKKSVYPLYY
DSATVKKGLK SGTLFKGTLR ILENHRSAFA CMEDIPDFYV DGPIARNRAF HNDVVIVEPV
MNNDSPTEKS NFLQNGVEKV KIKDHDDELG GAMEHLERLE IKSVASFKGD SRTRARVVAI
EKRAEISKIV GILRAPGWSL KNVEYVSKKS SYAIFIPKDK RLPFITIHKN DLSDLSGENW
IENILKHHDQ LFSVEITRWS IYSRYPMGVL GEKLGNITDV EAYTNALLLE NGISSSPFSD
EVLNCLPPDD WIISHEEIKK RRDLRNELII TIDPETARDL DDAVSCRALD NGTYEVGVHI
ADVTHFVKPD SALDKEAASR ATTVYLVQKA IPMLPPLLCE RLCSLNPNVE RLAFSVFWKL
DSNGKEIGKR WFGKTVIKTC ARLAYSEAQG VIEGKSWDDA VGKPIGGTHT PKDVETSILT
LCEISRKLRK DRFAKGAVEI NSTELKFQLD EYGMPNKCEV YEQTDANHLI EEFMLLANRS
VAEHISKNFS NNSLLRRHAS PKEKQINEFC HFLKSMNFDF DASSSAAFNA SMVRLRSTFN
EELVELFENM AVRSLNRAEY FCTGDFGEKT DWHHYALSFN HYTHFTSPIR RYPDIIVHRL
LERSLKNTSP GIDKKNCSLV AAHCNEKKEK STTVQEDSQQ LFLSVYIAEY CKKHDKKSMP
VQAFATRISG NSIDVYISEY GISNRVDLSS DDRIKSFIVA PDDSSVKITL FDDSQKTIAL
TDRFQVYLYS DYSRTFFSIR CSLVSLN
