CBF5_YEAST
ID CBF5_YEAST Reviewed; 483 AA.
AC P33322; D6VYH9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=H/ACA ribonucleoprotein complex subunit CBF5;
DE EC=5.4.99.- {ECO:0000269|PubMed:21131909, ECO:0000269|PubMed:25219674};
DE AltName: Full=Centromere-binding factor 5;
DE AltName: Full=Centromere/microtubule-binding protein CBF5;
DE AltName: Full=H/ACA snoRNP protein CBF5;
DE AltName: Full=Small nucleolar RNP protein CBF5;
DE AltName: Full=p64';
GN Name=CBF5; OrderedLocusNames=YLR175W; ORFNames=L9470.11;
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], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RX PubMed=8336724; DOI=10.1128/mcb.13.8.4884-4893.1993;
RA Jiang W., Middleton K., Yoon H.-J., Fouquet C., Carbon J.;
RT "An essential yeast protein, CBF5p, binds in vitro to centromeres and
RT microtubules.";
RL Mol. Cell. Biol. 13:4884-4893(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 FUNCTION.
RX PubMed=9315678; DOI=10.1128/mcb.17.10.6175;
RA Cadwell C., Yoon H.-J., Zebarjadian Y., Carbon J.;
RT "The yeast nucleolar protein Cbf5p is involved in rRNA biosynthesis and
RT interacts genetically with the RNA polymerase I transcription factor
RT RRN3.";
RL Mol. Cell. Biol. 17:6175-6183(1997).
RN [5]
RP FUNCTION, AND IDENTIFICATION IN H/ACA SNORNP COMPLEXES.
RX PubMed=9472021; DOI=10.1101/gad.12.4.527;
RA Lafontaine D.L., Bousquet-Antonelli C., Henry Y., Caizergues-Ferrer M.,
RA Tollervey D.;
RT "The box H + ACA snoRNAs carry Cbf5p, the putative rRNA pseudouridine
RT synthase.";
RL Genes Dev. 12:527-537(1998).
RN [6]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN H/ACA
RP SNORNP COMPLEX.
RX PubMed=9848653; DOI=10.1017/s1355838298980761;
RA Watkins N.J., Gottschalk A., Neubauer G., Kastner B., Fabrizio P., Mann M.,
RA Luehrmann R.;
RT "Cbf5p, a potential pseudouridine synthase, and Nhp2p, a putative RNA-
RT binding protein, are present together with Gar1p in all H BOX/ACA-motif
RT snoRNPs and constitute a common bipartite structure.";
RL RNA 4:1549-1568(1998).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF ASP-65; LEU-94 AND ASP-95.
RX PubMed=10523634; DOI=10.1128/mcb.19.11.7461;
RA Zebarjadian Y., King T., Fournier M.J., Clarke L., Carbon J.;
RT "Point mutations in yeast CBF5 can abolish in vivo pseudouridylation of
RT rRNA.";
RL Mol. Cell. Biol. 19:7461-7472(1999).
RN [8]
RP INTERACTION WITH SHQ1.
RX PubMed=12228251; DOI=10.1074/jbc.m207669200;
RA Yang P.K., Rotondo G., Porras T., Legrain P., Chanfreau G.;
RT "The Shq1p.Naf1p complex is required for box H/ACA small nucleolar
RT ribonucleoprotein particle biogenesis.";
RL J. Biol. Chem. 277:45235-45242(2002).
RN [9]
RP INTERACTION WITH TGS1.
RX PubMed=11983179; DOI=10.1016/s1097-2765(02)00484-7;
RA Mouaikel J., Verheggen C., Bertrand E., Tazi J., Bordonne R.;
RT "Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs
RT requires a conserved methyltransferase that is localized to the
RT nucleolus.";
RL Mol. Cell 9:891-901(2002).
RN [10]
RP INTERACTION WITH NAF1.
RX PubMed=12515383;
RA Fatica A., Dlakic M., Tollervey D.;
RT "Naf1 p is a box H/ACA snoRNP assembly factor.";
RL RNA 8:1502-1514(2002).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [12]
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 [13]
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 [14]
RP CHARACTERIZATION OF THE H/ACA SNORNP COMPLEX.
RX PubMed=15388873; DOI=10.1261/rna.7770604;
RA Henras A.K., Capeyrou R., Henry Y., Caizergues-Ferrer M.;
RT "Cbf5p, the putative pseudouridine synthase of H/ACA-type snoRNPs, can form
RT a complex with Gar1p and Nop10p in absence of Nhp2p and box H/ACA
RT snoRNAs.";
RL RNA 10:1704-1712(2004).
RN [15]
RP INTERACTION WITH NOP53, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15686447; DOI=10.1042/bj20041297;
RA Sydorskyy Y., Dilworth D.J., Halloran B., Yi E.C., Makhnevych T.,
RA Wozniak R.W., Aitchison J.D.;
RT "Nop53p is a novel nucleolar 60S ribosomal subunit biogenesis protein.";
RL Biochem. J. 388:819-826(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-378, AND IDENTIFICATION BY
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-378, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-378, 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).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND THR-378, 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).
RN [20]
RP FUNCTION, IDENTIFICATION IN THE H/ACA SNORNP COMPLEX, CATALYTIC ACTIVITY,
RP AND MUTAGENESIS OF ASP-95.
RX PubMed=21131909; DOI=10.1038/emboj.2010.316;
RA Wu G., Xiao M., Yang C., Yu Y.T.;
RT "U2 snRNA is inducibly pseudouridylated at novel sites by Pus7p and snR81
RT RNP.";
RL EMBO J. 30:79-89(2011).
RN [21]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-9 AND LYS-267, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [22]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25219674; DOI=10.1016/j.cell.2014.08.028;
RA Schwartz S., Bernstein D.A., Mumbach M.R., Jovanovic M., Herbst R.H.,
RA Leon-Ricardo B.X., Engreitz J.M., Guttman M., Satija R., Lander E.S.,
RA Fink G., Regev A.;
RT "Transcriptome-wide mapping reveals widespread dynamic-regulated
RT pseudouridylation of ncRNA and mRNA.";
RL Cell 159:148-162(2014).
CC -!- FUNCTION: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein
CC (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA
CC (PubMed:10523634, PubMed:9315678, PubMed:9472021, PubMed:9848653). This
CC involves the isomerization of uridine such that the ribose is
CC subsequently attached to C5, instead of the normal N1 (PubMed:10523634,
CC PubMed:9315678, PubMed:9472021, PubMed:9848653). Pseudouridine ('psi')
CC residues may serve to stabilize the conformation of rRNAs and play a
CC central role in ribosomal RNA processing (PubMed:10523634,
CC PubMed:9315678, PubMed:9472021, PubMed:9848653). The H/ACA snoRNP
CC complex also mediates pseudouridylation of other types of RNAs
CC (PubMed:21131909, PubMed:25219674). Catalyzes pseudouridylation at
CC position 93 in U2 snRNA (PubMed:21131909). Also catalyzes
CC pseudouridylation of mRNAs; H/ACA-type snoRNAs probably guide
CC pseudouridylation of mRNAs (PubMed:25219674). It is a centromeric DNA-
CC CBF3-binding factor which is involved in mitotic chromosome segregation
CC (PubMed:8336724). Essential for cell growth (PubMed:8336724).
CC {ECO:0000269|PubMed:10523634, ECO:0000269|PubMed:21131909,
CC ECO:0000269|PubMed:25219674, ECO:0000269|PubMed:8336724,
CC ECO:0000269|PubMed:9315678, ECO:0000269|PubMed:9472021,
CC ECO:0000269|PubMed:9848653}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine in 5S rRNA = pseudouridine in 5S rRNA;
CC Xref=Rhea:RHEA:47036, Rhea:RHEA-COMP:11730, Rhea:RHEA-COMP:11731,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine in snRNA = pseudouridine in snRNA;
CC Xref=Rhea:RHEA:51124, Rhea:RHEA-COMP:12891, Rhea:RHEA-COMP:12892,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000269|PubMed:21131909};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in mRNA = a pseudouridine in mRNA;
CC Xref=Rhea:RHEA:56644, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:14659,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000269|PubMed:25219674};
CC -!- SUBUNIT: Component of the small nucleolar ribonucleoprotein particles
CC containing H/ACA-type snoRNAs (H/ACA snoRNPs) (PubMed:9472021,
CC PubMed:9848653, PubMed:15388873, PubMed:21131909). The protein
CC component of the H/ACA snoRNP contains CBF5, GAR1, NHP2 and NOP10
CC (PubMed:9472021, PubMed:9848653, PubMed:15388873). The complex contains
CC a stable core composed of CBF5 and NOP10, to which GAR1 and NHP2
CC subsequently bind (PubMed:9472021, PubMed:9848653, PubMed:15388873).
CC Also interacts with NAF1 and SHQ1, which may be required for assembly
CC of H/ACA snoRNP complexes. May also associate with the CBF3 110 kDa
CC subunit (CBF2). Interacts with the trimethylguanosine synthase (TGS1)
CC and with NOP53. {ECO:0000269|PubMed:11983179,
CC ECO:0000269|PubMed:12228251, ECO:0000269|PubMed:12515383,
CC ECO:0000269|PubMed:15388873, ECO:0000269|PubMed:15686447,
CC ECO:0000269|PubMed:21131909, ECO:0000269|PubMed:9472021,
CC ECO:0000269|PubMed:9848653}.
CC -!- INTERACTION:
CC P33322; P53919: NAF1; NbExp=6; IntAct=EBI-4105, EBI-28887;
CC P33322; P32495: NHP2; NbExp=11; IntAct=EBI-4105, EBI-12014;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC Chromosome, centromere {ECO:0000269|PubMed:14562095}. Cytoplasm,
CC cytoskeleton {ECO:0000305|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 33600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC {ECO:0000305}.
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DR EMBL; L12351; AAA34473.1; -; Genomic_DNA.
DR EMBL; U17246; AAB67463.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09495.1; -; Genomic_DNA.
DR PIR; S41853; S41853.
DR RefSeq; NP_013276.1; NM_001182062.1.
DR PDB; 3U28; X-ray; 1.90 A; A=3-394.
DR PDB; 3UAI; X-ray; 3.06 A; A=3-394.
DR PDB; 3ZV0; X-ray; 2.80 A; C/D=1-60, C/D=258-386.
DR PDBsum; 3U28; -.
DR PDBsum; 3UAI; -.
DR PDBsum; 3ZV0; -.
DR AlphaFoldDB; P33322; -.
DR SMR; P33322; -.
DR BioGRID; 31446; 334.
DR ComplexPortal; CPX-737; Box H/ACA ribonucleoprotein complex.
DR DIP; DIP-4472N; -.
DR IntAct; P33322; 106.
DR MINT; P33322; -.
DR STRING; 4932.YLR175W; -.
DR iPTMnet; P33322; -.
DR MaxQB; P33322; -.
DR PaxDb; P33322; -.
DR PRIDE; P33322; -.
DR EnsemblFungi; YLR175W_mRNA; YLR175W; YLR175W.
DR GeneID; 850872; -.
DR KEGG; sce:YLR175W; -.
DR SGD; S000004165; CBF5.
DR VEuPathDB; FungiDB:YLR175W; -.
DR eggNOG; KOG2529; Eukaryota.
DR GeneTree; ENSGT00510000047092; -.
DR HOGENOM; CLU_032087_3_2_1; -.
DR InParanoid; P33322; -.
DR OMA; GPFKEDE; -.
DR BioCyc; MetaCyc:YLR175W-MON; -.
DR BioCyc; YEAST:YLR175W-MON; -.
DR Reactome; R-SCE-171319; Telomere Extension By Telomerase.
DR PRO; PR:P33322; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P33322; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; IDA:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; IC:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0009982; F:pseudouridine synthase activity; IDA:UniProtKB.
DR GO; GO:0000495; P:box H/ACA RNA 3'-end processing; IMP:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IMP:SGD.
DR GO; GO:0000154; P:rRNA modification; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR GO; GO:0031118; P:rRNA pseudouridine synthesis; IMP:SGD.
DR GO; GO:0000454; P:snoRNA guided rRNA pseudouridine synthesis; IDA:ComplexPortal.
DR GO; GO:0031120; P:snRNA pseudouridine synthesis; IDA:SGD.
DR DisProt; DP02055; -.
DR Gene3D; 2.30.130.10; -; 1.
DR InterPro; IPR012960; Dyskerin-like.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR002501; PsdUridine_synth_N.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR004802; tRNA_PsdUridine_synth_B_fam.
DR InterPro; IPR032819; TruB_C.
DR InterPro; IPR004521; Uncharacterised_CHP00451.
DR PANTHER; PTHR23127; PTHR23127; 1.
DR Pfam; PF08068; DKCLD; 1.
DR Pfam; PF01472; PUA; 1.
DR Pfam; PF16198; TruB_C_2; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SMART; SM01136; DKCLD; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00425; CBF5; 1.
DR TIGRFAMs; TIGR00451; unchar_dom_2; 1.
DR PROSITE; PS50890; PUA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; DNA-binding; Isomerase;
KW Isopeptide bond; Microtubule; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; Ribosome biogenesis;
KW RNA-binding; rRNA processing; Ubl conjugation.
FT CHAIN 1..483
FT /note="H/ACA ribonucleoprotein complex subunit CBF5"
FT /id="PRO_0000121982"
FT DOMAIN 266..341
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT REPEAT 434..436
FT /note="1"
FT REPEAT 437..439
FT /note="2"
FT REPEAT 440..442
FT /note="3"
FT REPEAT 443..445
FT /note="4"
FT REPEAT 446..448
FT /note="5"
FT REPEAT 449..451
FT /note="6"
FT REPEAT 452..454
FT /note="7"
FT REPEAT 455..457
FT /note="8"
FT REPEAT 458..460
FT /note="9"
FT REPEAT 461..463
FT /note="10"
FT REGION 357..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..463
FT /note="10 X 3 AA tandem repeats of K-K-[DE]"
FT COMPBIAS 360..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 95
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P60340"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 378
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 9
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 267
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 65
FT /note="D->A: Reduced pseudouridylation of rRNA and reduced
FT snoRNA levels."
FT /evidence="ECO:0000269|PubMed:10523634"
FT MUTAGEN 94
FT /note="L->A: Reduced pseudouridylation of rRNA."
FT /evidence="ECO:0000269|PubMed:10523634"
FT MUTAGEN 95
FT /note="D->A: Abolished pseudouridylation of rRNA. Abolishes
FT pseudouridylation at position 93 in U2 snRNA."
FT /evidence="ECO:0000269|PubMed:10523634,
FT ECO:0000269|PubMed:21131909"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:3U28"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:3U28"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3U28"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:3U28"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:3UAI"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:3U28"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:3U28"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 121..131
FT /evidence="ECO:0007829|PDB:3U28"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 165..178
FT /evidence="ECO:0007829|PDB:3U28"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:3U28"
FT HELIX 196..207
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 211..221
FT /evidence="ECO:0007829|PDB:3U28"
FT HELIX 233..246
FT /evidence="ECO:0007829|PDB:3U28"
FT HELIX 250..255
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:3UAI"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:3U28"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:3U28"
FT HELIX 276..282
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:3U28"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 312..320
FT /evidence="ECO:0007829|PDB:3U28"
FT HELIX 322..327
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 329..339
FT /evidence="ECO:0007829|PDB:3U28"
FT HELIX 355..365
FT /evidence="ECO:0007829|PDB:3ZV0"
SQ SEQUENCE 483 AA; 54705 MW; D356B39FDCC32E2D CRC64;
MSKEDFVIKP EAAGASTDTS EWPLLLKNFD KLLVRSGHYT PIPAGSSPLK RDLKSYISSG
VINLDKPSNP SSHEVVAWIK RILRCEKTGH SGTLDPKVTG CLIVCIDRAT RLVKSQQGAG
KEYVCIVRLH DALKDEKDLG RSLENLTGAL FQRPPLISAV KRQLRVRTIY ESNLIEFDNK
RNLGVFWASC EAGTYMRTLC VHLGMLLGVG GHMQELRRVR SGALSENDNM VTLHDVMDAQ
WVYDNTRDES YLRSIIQPLE TLLVGYKRIV VKDSAVNAVC YGAKLMIPGL LRYEEGIELY
DEIVLITTKG EAIAVAIAQM STVDLASCDH GVVASVKRCI MERDLYPRRW GLGPVAQKKK
QMKADGKLDK YGRVNENTPE QWKKEYVPLD NAEQSTSSSQ ETKETEEEPK KAKEDSLIKE
VETEKEEVKE DDSKKEKKEK KDKKEKKEKK EKKDKKEKKE KKEKKRKSED GDSEEKKSKK
SKK
