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NGL2_YEAST
ID   NGL2_YEAST              Reviewed;         515 AA.
AC   Q03264; D6W0B2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=RNA exonuclease NGL2;
DE            EC=3.1.-.-;
DE   AltName: Full=Carbon catabolite repressor protein 4 homolog;
GN   Name=NGL2; OrderedLocusNames=YMR285C; ORFNames=YM8021.11C;
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   FUNCTION.
RX   PubMed=12358428; DOI=10.1017/s1355838202021027;
RA   Faber A.W., van Dijk M., Raue H.A., Vos J.C.;
RT   "Ngl2p is a Ccr4p-like RNA nuclease essential for the final step in 3'-end
RT   processing of 5.8S rRNA in Saccharomyces cerevisiae.";
RL   RNA 8:1095-1101(2002).
RN   [4]
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).
CC   -!- FUNCTION: Involved in pre-rRNA processing. Required for the final stage
CC       of 3'-end maturation of 5.8S rRNA at site E.
CC       {ECO:0000269|PubMed:12358428}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 3570 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; Z49704; CAA89783.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10186.1; -; Genomic_DNA.
DR   PIR; S54592; S54592.
DR   RefSeq; NP_014012.1; NM_001182792.1.
DR   AlphaFoldDB; Q03264; -.
DR   SMR; Q03264; -.
DR   BioGRID; 35465; 162.
DR   DIP; DIP-894N; -.
DR   IntAct; Q03264; 1.
DR   STRING; 4932.YMR285C; -.
DR   iPTMnet; Q03264; -.
DR   MaxQB; Q03264; -.
DR   PaxDb; Q03264; -.
DR   PRIDE; Q03264; -.
DR   EnsemblFungi; YMR285C_mRNA; YMR285C; YMR285C.
DR   GeneID; 855329; -.
DR   KEGG; sce:YMR285C; -.
DR   SGD; S000004898; NGL2.
DR   VEuPathDB; FungiDB:YMR285C; -.
DR   eggNOG; KOG2338; Eukaryota.
DR   GeneTree; ENSGT00940000176796; -.
DR   HOGENOM; CLU_034867_0_0_1; -.
DR   InParanoid; Q03264; -.
DR   OMA; PEISNWA; -.
DR   BioCyc; YEAST:G3O-32955-MON; -.
DR   PRO; PR:Q03264; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q03264; protein.
DR   GO; GO:0005737; C:cytoplasm; IC:SGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0004521; F:endoribonuclease activity; IMP:SGD.
DR   GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IMP: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   Cytoplasm; Exonuclease; Hydrolase; Nuclease; Nucleus; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..515
FT                   /note="RNA exonuclease NGL2"
FT                   /id="PRO_0000218579"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   515 AA;  59540 MW;  89B30A7D24D6EBC8 CRC64;
     MTQDKEVKVV APDVAPDQEV EINKSVKDAK HQTNDDSLLQ HKKKGKKGKK SKPIVTPEHI
     AKVRAEREVM RKAKRDAMLA QGVDPDCPPE LHFIRRPFLS LHEAEPVTGF RFKLMTYNCL
     AQALIRRKLF PDSGDALKWY RRSKVLLNEF KYYNSDVICL QEIDHIQFQS FWKDEFSKLG
     YDGQYYRNAT KNHGVAIMWR RELFHQVDKM LIDYDKESSE SISTRTTTNN VGLVLALKFS
     EKVLSNLGKK SSKKCGILIG TTHLFWHPFG TYERTRQCYI VLKKMKEFMH RVNVLQNEND
     GDLSHWFPFF CGDFNSQPFD TPYLSMTSKP VHYRNRAKTV IGCSTSYKFS KVRDGEEGAD
     DEEGGNIEKY GKDQPESPVP EKFHANEEQS ELVDKMAQLH NSLDMRAISL YSVGYKNVHP
     ENAGLDNDRG EPEISNWANT WRGLLDYLFY VKKWDPQSNC QEVETLGDFE KENKVKCRGF
     LRMPPGNEMT KHGQPHVGEY ASDHLSMVCD LELQL
 
 
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