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NGL3_YEAST
ID   NGL3_YEAST              Reviewed;         505 AA.
AC   Q03210; D6W0G6; Q03733;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Probable RNA exonuclease NGL3;
DE            EC=3.1.-.-;
GN   Name=NGL3; OrderedLocusNames=YML118W; ORFNames=YM7056.08, YM8339.01;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- MISCELLANEOUS: Present with 414 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}.
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DR   EMBL; Z49218; CAA89162.1; -; Genomic_DNA.
DR   EMBL; Z49210; CAA89100.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09780.1; -; Genomic_DNA.
DR   PIR; S54066; S54066.
DR   RefSeq; NP_013588.1; NM_001182481.1.
DR   AlphaFoldDB; Q03210; -.
DR   SMR; Q03210; -.
DR   BioGRID; 35086; 28.
DR   IntAct; Q03210; 1.
DR   STRING; 4932.YML118W; -.
DR   iPTMnet; Q03210; -.
DR   MaxQB; Q03210; -.
DR   PaxDb; Q03210; -.
DR   PRIDE; Q03210; -.
DR   EnsemblFungi; YML118W_mRNA; YML118W; YML118W.
DR   GeneID; 854921; -.
DR   KEGG; sce:YML118W; -.
DR   SGD; S000004587; NGL3.
DR   VEuPathDB; FungiDB:YML118W; -.
DR   eggNOG; KOG2338; Eukaryota.
DR   GeneTree; ENSGT00940000176796; -.
DR   HOGENOM; CLU_034867_0_0_1; -.
DR   InParanoid; Q03210; -.
DR   OMA; LFPTSDC; -.
DR   BioCyc; YEAST:G3O-32699-MON; -.
DR   PRO; PR:Q03210; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q03210; protein.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IDA:SGD.
DR   GO; GO:0043633; P:polyadenylation-dependent RNA catabolic process; IDA:SGD.
DR   Gene3D; 3.60.10.10; -; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   SUPFAM; SSF56219; SSF56219; 1.
PE   1: Evidence at protein level;
KW   Exonuclease; Hydrolase; Nuclease; Phosphoprotein; Reference proteome.
FT   CHAIN           1..505
FT                   /note="Probable RNA exonuclease NGL3"
FT                   /id="PRO_0000218580"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         62
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   505 AA;  57742 MW;  2B6D6389A93B7D72 CRC64;
     MDSQVEGKIS PSQKESSSTS GLVSPSEDGP AHQKIHRDQL SVDQIKKIRE ERAQKRQVRR
     NSLISQGKDP DFPTPDLQFI ERPFLPINHD NSKGLTPATI QVTQDSLDVK IMTYNTLAQT
     LIRRDFFPES GPALKWHKRS KVLVHELKKY RPDVVSLQEV DYNELNFWQE NFHKLGFDVI
     FKRHEGKTHG LLVAWNNKKF QLDNDWMLDY DNILAGNVIS ARTRTKNIAL IISLYFKGIT
     DSSSRGIIVA NTHLFWHPFG VFERLRQSYL VLQKIQEIKA CSKYNGWHSL LMGDFNTEPE
     EPPYLAITKR PLILKGPIRA MVECSLAYRY SKKRNGEESD QDDEECDEKS RGEGHSDQPQ
     NPKPESFTAT KEEKALVNQL VALHNSLHVK GVSLYGIGYG KVHPENANGS HGEPGLSNWA
     NTWCGLLDYI FYIEGDHNQD TRQKEPLNAF EGNNNVKIIG YLRMPCAQEM PKHSQPFEGE
     YASDHISLMC QIRLFFGGEK VHSLK
 
 
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