CBF5_ARATH
ID CBF5_ARATH Reviewed; 565 AA.
AC Q9LD90; Q42348; Q94AA2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=H/ACA ribonucleoprotein complex subunit 4;
DE EC=5.4.99.-;
DE AltName: Full=CBF5 homolog;
DE AltName: Full=Dyskerin;
DE AltName: Full=Nopp-140-associated protein of 57 kDa homolog;
DE Short=AtNAP57;
DE AltName: Full=Nucleolar protein NAP57 homolog;
GN Name=CBF5; Synonyms=NAP57; OrderedLocusNames=At3g57150; ORFNames=F24I3.230;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11833778;
RA Maceluch J., Kmieciak M., Szweykowska-Kulinska Z., Jarmolowski A.;
RT "Cloning and characterization of Arabidopsis thaliana AtNAP57 -- a
RT homologue of yeast pseudouridine synthase Cbf5p.";
RL Acta Biochim. Pol. 48:699-709(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-125.
RC STRAIN=cv. Columbia;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [8]
RP INTERACTION WITH POT1A, AND COMPONENT OF THE TELOMERASE COMPLEX.
RX PubMed=18212040; DOI=10.1128/mcb.01490-07;
RA Kannan K., Nelson A.D., Shippen D.E.;
RT "Dyskerin is a component of the Arabidopsis telomerase RNP required for
RT telomere maintenance.";
RL Mol. Cell. Biol. 28:2332-2341(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515 AND SER-539, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450; SER-515 AND SER-539, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Plays a central role in ribosomal RNA processing. Probable
CC catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA
CC snoRNP) complex, which catalyzes pseudouridylation of rRNA. This
CC involves the isomerization of uridine such that the ribose is
CC subsequently attached to C5, instead of the normal N1. Pseudouridine
CC ('psi') residues may serve to stabilize the conformation of rRNAs (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in RNA = a pseudouridine in RNA;
CC Xref=Rhea:RHEA:48348, Rhea:RHEA-COMP:12068, Rhea:RHEA-COMP:12069,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC -!- SUBUNIT: Component of the small nucleolar ribonucleoprotein particle
CC containing H/ACA-type snoRNAs (H/ACA snoRNPs) (By similarity).
CC Component of the telomerase holoenzyme complex at least composed of
CC TERT, CBF5, POT1a and a telomerase RNA template component TER1.
CC Interacts with POT1a. {ECO:0000250, ECO:0000269|PubMed:18212040}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK83589.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF234984; AAF43210.2; -; mRNA.
DR EMBL; AL138655; CAB72185.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79621.1; -; Genomic_DNA.
DR EMBL; AY049247; AAK83589.1; ALT_FRAME; mRNA.
DR EMBL; BT003810; AAO41863.1; -; mRNA.
DR EMBL; F20038; CAA23387.1; -; mRNA.
DR PIR; T47775; T47775.
DR RefSeq; NP_191274.1; NM_115574.3.
DR AlphaFoldDB; Q9LD90; -.
DR SMR; Q9LD90; -.
DR BioGRID; 10198; 9.
DR IntAct; Q9LD90; 1.
DR STRING; 3702.AT3G57150.1; -.
DR iPTMnet; Q9LD90; -.
DR SwissPalm; Q9LD90; -.
DR PaxDb; Q9LD90; -.
DR PRIDE; Q9LD90; -.
DR ProteomicsDB; 223928; -.
DR EnsemblPlants; AT3G57150.1; AT3G57150.1; AT3G57150.
DR GeneID; 824882; -.
DR Gramene; AT3G57150.1; AT3G57150.1; AT3G57150.
DR KEGG; ath:AT3G57150; -.
DR Araport; AT3G57150; -.
DR TAIR; locus:2080625; AT3G57150.
DR eggNOG; KOG2529; Eukaryota.
DR HOGENOM; CLU_032087_3_2_1; -.
DR InParanoid; Q9LD90; -.
DR OMA; EWTRNVV; -.
DR OrthoDB; 1070373at2759; -.
DR PhylomeDB; Q9LD90; -.
DR BioCyc; ARA:AT3G57150-MON; -.
DR PRO; PR:Q9LD90; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LD90; baseline and differential.
DR Genevisible; Q9LD90; AT.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009982; F:pseudouridine synthase activity; ISS:TAIR.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000495; P:box H/ACA RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0031118; P:rRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0031120; P:snRNA pseudouridine synthesis; IBA:GO_Central.
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; 2.
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 Isomerase; Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..565
FT /note="H/ACA ribonucleoprotein complex subunit 4"
FT /id="PRO_0000121990"
FT DOMAIN 287..362
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 116
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
SQ SEQUENCE 565 AA; 63026 MW; DE731AA935277D54 CRC64;
MAEVDISHSK KKKQDKTEND AADTGDYMIK PQSFTPAIDT SQWPILLKNY DRLNVRTGHY
TPISAGHSPL KRPLQEYIRY GVINLDKPAN PSSHEVVAWI KRILRVEKTG HSGTLDPKVT
GNLIVCIDRA TRLVKSQQGA GKEYVCVARL HSAVPDVAKV ARALESLTGA VFQRPPLISA
VKRQLRIRTI YESKLLEYDA DRHLVVFWVS CEAGTYIRTM CVHLGLLLGV GGHMQELRRV
RSGILGENNN MVTMHDVMDA QFVYDNSRDE SYLRRVIMPL EMILTSYKRL VVKDSAVNAI
CYGAKLMIPG LLRFENDIDV GTEVVLMTTK GEAIAVGIAE MTTSVMATCD HGVVAKIKRV
VMDRDTYPRK WGLGPRASMK KKLIADGKLD KHGKPNEKTP VEWSRNVVLP TGGDAIIAGA
AAAPEEIKAD AENGEAGEAR KRKHDDSSDS PAPVTTKKSK TKEVEGEEAE EKVKSSKKKK
KKDKEEEKEE EAGSEKKEKK KKKDKKEEVI EEVASPKSEK KKKKKSKDTE AAVDAEDESA
AEKSEKKKKK KDKKKKNKDS EDDEE
