NRD1_YEAST
ID NRD1_YEAST Reviewed; 575 AA.
AC P53617; D6W0U2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Protein NRD1;
GN Name=NRD1; OrderedLocusNames=YNL251C; ORFNames=N0868;
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 [GENOMIC DNA].
RX PubMed=8943355; DOI=10.1128/mcb.16.12.6993;
RA Steinmetz E.J., Brow D.A.;
RT "Repression of gene expression by an exogenous sequence element acting in
RT concert with a heterogeneous nuclear ribonucleoprotein-like protein, Nrd1,
RT and the putative helicase Sen1.";
RL Mol. Cell. Biol. 16:6993-7003(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9234673;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<849::aid-yea106>3.0.co;2-n;
RA Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A., Hegemann J.H.;
RT "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the
RT left arm of chromosome XIV from Saccharomyces cerevisiae.";
RL Yeast 13:849-860(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-265, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP IDENTIFICATION BY 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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-265 AND SER-271, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Plays a role in sequence-specific regulation of nuclear pre-
CC mRNA abundance.
CC -!- INTERACTION:
CC P53617; P38996: NAB3; NbExp=7; IntAct=EBI-12228, EBI-11776;
CC P53617; P04050: RPO21; NbExp=2; IntAct=EBI-12228, EBI-15760;
CC P53617; Q12149: RRP6; NbExp=4; IntAct=EBI-12228, EBI-1782;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 19600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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; U28487; AAC49568.1; -; Genomic_DNA.
DR EMBL; X96722; CAA65493.1; -; Genomic_DNA.
DR EMBL; Z71527; CAA96158.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10308.1; -; Genomic_DNA.
DR PIR; S59740; S59740.
DR RefSeq; NP_014148.1; NM_001183089.1.
DR PDB; 2LO6; NMR; -; A=1-153.
DR PDB; 2M88; NMR; -; A=307-491.
DR PDB; 2MOW; NMR; -; A=1-153.
DR PDB; 3CLJ; X-ray; 2.10 A; A=6-151.
DR PDB; 5O1T; NMR; -; A=290-468.
DR PDB; 5O1W; X-ray; 2.30 A; A=301-489.
DR PDB; 5O1X; X-ray; 1.60 A; A=290-468.
DR PDB; 5O1Y; X-ray; 2.45 A; A=290-468.
DR PDB; 5O1Z; X-ray; 3.40 A; A=290-468.
DR PDB; 5O20; X-ray; 3.53 A; A=290-468.
DR PDB; 6GC3; NMR; -; A=1-153.
DR PDB; 6O3W; X-ray; 2.10 A; A/B=6-156.
DR PDB; 6O3X; X-ray; 1.99 A; A/B/C=6-156.
DR PDB; 6O3Y; X-ray; 2.80 A; A/B/C=6-156.
DR PDBsum; 2LO6; -.
DR PDBsum; 2M88; -.
DR PDBsum; 2MOW; -.
DR PDBsum; 3CLJ; -.
DR PDBsum; 5O1T; -.
DR PDBsum; 5O1W; -.
DR PDBsum; 5O1X; -.
DR PDBsum; 5O1Y; -.
DR PDBsum; 5O1Z; -.
DR PDBsum; 5O20; -.
DR PDBsum; 6GC3; -.
DR PDBsum; 6O3W; -.
DR PDBsum; 6O3X; -.
DR PDBsum; 6O3Y; -.
DR AlphaFoldDB; P53617; -.
DR BMRB; P53617; -.
DR SMR; P53617; -.
DR BioGRID; 35588; 302.
DR ComplexPortal; CPX-1316; NRD1 snoRNA termination complex.
DR DIP; DIP-6778N; -.
DR ELM; P53617; -.
DR IntAct; P53617; 35.
DR MINT; P53617; -.
DR STRING; 4932.YNL251C; -.
DR iPTMnet; P53617; -.
DR MaxQB; P53617; -.
DR PaxDb; P53617; -.
DR PRIDE; P53617; -.
DR EnsemblFungi; YNL251C_mRNA; YNL251C; YNL251C.
DR GeneID; 855470; -.
DR KEGG; sce:YNL251C; -.
DR SGD; S000005195; NRD1.
DR VEuPathDB; FungiDB:YNL251C; -.
DR eggNOG; KOG0132; Eukaryota.
DR GeneTree; ENSGT00940000173128; -.
DR HOGENOM; CLU_016577_1_0_1; -.
DR InParanoid; P53617; -.
DR OMA; LIDIWDR; -.
DR BioCyc; YEAST:G3O-33248-MON; -.
DR EvolutionaryTrace; P53617; -.
DR PRO; PR:P53617; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53617; protein.
DR GO; GO:0035649; C:Nrd1 complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0019904; F:protein domain specific binding; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0001068; F:transcription regulatory region RNA binding; IDA:SGD.
DR GO; GO:0071041; P:antisense RNA transcript catabolic process; IDA:SGD.
DR GO; GO:0071034; P:CUT catabolic process; IMP:SGD.
DR GO; GO:0031124; P:mRNA 3'-end processing; IMP:SGD.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IMP:SGD.
DR GO; GO:0031126; P:sno(s)RNA 3'-end processing; IMP:SGD.
DR GO; GO:0034472; P:snRNA 3'-end processing; IMP:SGD.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IBA:GO_Central.
DR GO; GO:0030847; P:termination of RNA polymerase II transcription, exosome-dependent; IDA:SGD.
DR GO; GO:0042780; P:tRNA 3'-end processing; IMP:SGD.
DR CDD; cd12331; RRM_NRD1_SEB1_like; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR034894; Nrd1/Seb1_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF04818; CID; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00582; RPR; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51391; CID; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..575
FT /note="Protein NRD1"
FT /id="PRO_0000081688"
FT DOMAIN 1..153
FT /note="CID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT DOMAIN 339..409
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 225..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:2LO6"
FT HELIX 7..15
FT /evidence="ECO:0007829|PDB:6O3X"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:6O3X"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:6O3X"
FT HELIX 26..38
FT /evidence="ECO:0007829|PDB:6O3X"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:6O3X"
FT HELIX 43..56
FT /evidence="ECO:0007829|PDB:6O3X"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:6O3X"
FT HELIX 62..83
FT /evidence="ECO:0007829|PDB:6O3X"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:6GC3"
FT HELIX 94..115
FT /evidence="ECO:0007829|PDB:6O3X"
FT HELIX 118..134
FT /evidence="ECO:0007829|PDB:6O3X"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:6O3X"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:5O1X"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:5O1W"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:5O1X"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:5O1X"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:5O1X"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:2M88"
FT HELIX 352..359
FT /evidence="ECO:0007829|PDB:5O1X"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:5O1X"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:5O1X"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:5O1X"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:5O1X"
FT HELIX 384..393
FT /evidence="ECO:0007829|PDB:5O1X"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:5O1X"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:5O1X"
FT STRAND 403..406
FT /evidence="ECO:0007829|PDB:5O1X"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:5O1X"
FT TURN 418..421
FT /evidence="ECO:0007829|PDB:5O1X"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:5O1X"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:5O1X"
FT HELIX 432..440
FT /evidence="ECO:0007829|PDB:5O1X"
FT STRAND 442..445
FT /evidence="ECO:0007829|PDB:5O1X"
FT HELIX 450..453
FT /evidence="ECO:0007829|PDB:2M88"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:5O1X"
SQ SEQUENCE 575 AA; 63859 MW; 75082BDB0C42AE37 CRC64;
MQQDDDFQNF VATLESFKDL KSGISGSRIK KLTTYALDHI DIESKIISLI IDYSRLCPDS
HKLGSLYIID SIGRAYLDET RSNSNSSSNK PGTCAHAINT LGEVIQELLS DAIAKSNQDH
KEKIRMLLDI WDRSGLFQKS YLNAIRSKCF AMDISNNTAN TASQQLSLDP KQRSKQILSN
LKKSPPLNLN ISLPTDLTST DPAKQQAALF QVIAALQKHF KTLPSHTSVG TVAPPQAHTI
TEYGSRRERE RERERYNSRR NRSRSPPAPF SQPSTGRKDR YPSVAQDQYS IGAPNTTFGT
NNHHLYPDEL NVSNNPHYRP KPVSYDSTLP PDHIKVYSRT LFIGGVPLNM KEWDLANVLK
PFAEVQSVIL NNSRKHAFVK VYSRHEAENV LQNFNKDGAL PLRTRWGVGF GPRDCCDYQH
GYSIIPMHRL TDADKKWSVS AQWGGTSGQP LVTGIVFEEP DIIVGEGVSS KAISQKMPTD
SGRNGPRSGK PNKSGSISSI SPVPYGNAPL ASPPPQQYVQ PMMQQPYGYA PNQPLPSQGP
AAAAPPVPQQ QFDPTAQLNS LMNMLNQQQQ QQQQS
