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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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