NOB1_YEAST
ID NOB1_YEAST Reviewed; 459 AA.
AC Q08444; D6W2B9; O00021;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=20S-pre-rRNA D-site endonuclease NOB1;
DE EC=3.1.-.-;
DE AltName: Full=NIN1-binding protein;
DE AltName: Full=Pre-rRNA-processing endonuclease NOB1;
GN Name=NOB1; OrderedLocusNames=YOR056C; ORFNames=YOR29-07;
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=9133743;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g;
RA Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.;
RT "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the
RT presence of two tRNAs and 24 new open reading frames.";
RL Yeast 13:379-390(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP INTERACTION WITH PNO1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-279;
RP GLN-280 AND MET-281.
RX PubMed=12502737; DOI=10.1101/gad.1025602;
RA Tone Y., Toh-e A.;
RT "Nob1p is required for biogenesis of the 26S proteasome and degraded upon
RT its maturation in Saccharomyces cerevisiae.";
RL Genes Dev. 16:3142-3157(2002).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=12628929; DOI=10.1093/emboj/cdg121;
RA Schaefer T., Strauss D., Petfalski E., Tollervey D., Hurt E.;
RT "The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes.";
RL EMBO J. 22:1370-1380(2003).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12588997; DOI=10.1128/mcb.23.5.1798-1807.2003;
RA Fatica A., Oeffinger M., Dlakic M., Tollervey D.;
RT "Nob1p is required for cleavage of the 3' end of 18S rRNA.";
RL Mol. Cell. Biol. 23:1798-1807(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
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 [9]
RP SUBUNIT.
RX PubMed=15037774; DOI=10.1261/rna.5162204;
RA Vanrobays E., Gelugne J.-P., Caizergues-Ferrer M., Lafontaine D.L.J.;
RT "Dim2p, a KH-domain protein required for small ribosomal subunit
RT synthesis.";
RL RNA 10:645-656(2004).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF ASP-92 AND ASP-110.
RX PubMed=15388878; DOI=10.1261/rna.7123504;
RA Fatica A., Tollervey D., Dlakic M.;
RT "PIN domain of Nob1p is required for D-site cleavage in 20S pre-rRNA.";
RL RNA 10:1698-1701(2004).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for the synthesis of 40S ribosome subunits. Has a
CC role in processing 20S pre-rRNA into the mature 18S rRNA, where it is
CC required for cleavage at the 3' end of the mature 18S rRNA (D-site).
CC Accompanies the 20S pre-rRNA from the nucleus to the cytoplasm. In
CC association with NIN1, may promote the recruitment of the proteasome to
CC the ribosomal subunits stalled in maturation.
CC {ECO:0000269|PubMed:12588997, ECO:0000269|PubMed:15388878}.
CC -!- SUBUNIT: Component of the small ribosomal subunit, ribosomal RNA
CC processing complex (SSU RRP complex). Interacts with PNO1.
CC {ECO:0000269|PubMed:12502737, ECO:0000269|PubMed:15037774}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Endoplasmic
CC reticulum.
CC -!- MISCELLANEOUS: Present with 4490 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NOB1 family. {ECO:0000305}.
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DR EMBL; Z70678; CAA94541.1; -; Genomic_DNA.
DR EMBL; Z74964; CAA99249.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10835.1; -; Genomic_DNA.
DR PIR; S66939; S66939.
DR RefSeq; NP_014699.1; NM_001183475.1.
DR AlphaFoldDB; Q08444; -.
DR BioGRID; 34454; 253.
DR DIP; DIP-6440N; -.
DR IntAct; Q08444; 35.
DR MINT; Q08444; -.
DR STRING; 4932.YOR056C; -.
DR iPTMnet; Q08444; -.
DR MaxQB; Q08444; -.
DR PaxDb; Q08444; -.
DR PRIDE; Q08444; -.
DR EnsemblFungi; YOR056C_mRNA; YOR056C; YOR056C.
DR GeneID; 854221; -.
DR KEGG; sce:YOR056C; -.
DR SGD; S000005582; NOB1.
DR VEuPathDB; FungiDB:YOR056C; -.
DR eggNOG; KOG2463; Eukaryota.
DR GeneTree; ENSGT00390000015857; -.
DR HOGENOM; CLU_024666_2_1_1; -.
DR InParanoid; Q08444; -.
DR OMA; GYELECE; -.
DR BioCyc; YEAST:G3O-33596-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q08444; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08444; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IDA:SGD.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IDA:SGD.
DR GO; GO:0000469; P:cleavage involved in rRNA processing; IEA:InterPro.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IDA:SGD.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0043248; P:proteasome assembly; IMP:SGD.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:MGI.
DR CDD; cd09876; PIN_Nob1-like; 1.
DR Gene3D; 6.20.210.10; -; 1.
DR InterPro; IPR039907; NOB1.
DR InterPro; IPR017117; Nob1_euk.
DR InterPro; IPR036283; NOB1_Zf-like_sf.
DR InterPro; IPR014881; NOB1_Zn-bd.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR033411; Ribonuclease_PIN.
DR PANTHER; PTHR12814; PTHR12814; 1.
DR Pfam; PF08772; NOB1_Zn_bind; 1.
DR Pfam; PF17146; PIN_6; 1.
DR PIRSF; PIRSF037125; D-site_20S_pre-rRNA_nuclease; 1.
DR SMART; SM00670; PINc; 1.
DR SUPFAM; SSF144206; SSF144206; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Hydrolase; Metal-binding; Nuclease;
KW Nucleus; Reference proteome; Ribosome biogenesis; Zinc.
FT CHAIN 1..459
FT /note="20S-pre-rRNA D-site endonuclease NOB1"
FT /id="PRO_0000270554"
FT DOMAIN 10..115
FT /note="PINc"
FT REGION 120..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MUTAGEN 92
FT /note="D->N: No 20S cleavage."
FT /evidence="ECO:0000269|PubMed:15388878"
FT MUTAGEN 110
FT /note="D->N: No change in activity or growth."
FT /evidence="ECO:0000269|PubMed:15388878"
FT MUTAGEN 279
FT /note="L->R: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:12502737"
FT MUTAGEN 280
FT /note="Q->G: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:12502737"
FT MUTAGEN 281
FT /note="M->G: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:12502737"
SQ SEQUENCE 459 AA; 51742 MW; 96DEB818BB490A98 CRC64;
MTENQTAHVR ALILDATPLI TQSYTHYQNY AQSFYTTPTV FQEIKDAQAR KNLEIWQSLG
TLKLVHPSEN SIAKVSTFAK LTGDYSVLSA NDLHILALTY ELEIKLNNGD WRLRKKPGDA
LDASKADVGT DGKQKLTEDN KKEEDSESVP KKKNKRRGGK KQKAKREARE AREAENANLE
LESKAEEHVE EAGSKEQICN DENIKESSDL NEVFEDADDD GDWITPENLT EAIIKDSGED
TTGSLGVEAS EEDRHVALNR PENQVALATG DFAVQNVALQ MNLNLMNFMS GLKIKRIRNY
MLRCHACFKI FPLPKDGKPK HFCASCGGQG TLLRCAVSVD SRTGNVTPHL KSNFQWNNRG
NRYSVASPLS KNSQKRYGKK GHVHSKPQEN VILREDQKEY EKVIKQEEWT RRHNEKILNN
WIGGGSADNY ISPFAITGLK QHNVRIGKGR YVNSSKRRS
