CBF5_KLULA
ID CBF5_KLULA Reviewed; 474 AA.
AC O13473;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=H/ACA ribonucleoprotein complex subunit CBF5 {ECO:0000305};
DE EC=5.4.99.- {ECO:0000250|UniProtKB:P33322};
DE AltName: Full=Centromere-binding factor 5;
DE AltName: Full=H/ACA snoRNP protein CBF5;
DE AltName: Full=Small nucleolar RNP protein CBF5;
GN Name=CBF5; OrderedLocusNames=KLLA0D04796g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC MYA-539 / JBD100;
RX PubMed=9483794;
RX DOI=10.1002/(sici)1097-0061(19980115)14:1<37::aid-yea198>3.0.co;2-2;
RA Winkler A.A., Bobok A., Zonneveld B.J.M., Steensma H.Y., Hooykaas P.J.J.;
RT "The lysine-rich C-terminal repeats of the centromere-binding factor 5
RT (Cbf5) of Kluyveromyces lactis are not essential for function.";
RL Yeast 14:37-48(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein
CC (H/ACA 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 and
CC play a central role in ribosomal RNA processing. The H/ACA snoRNP
CC complex also mediates pseudouridylation of other types of RNAs.
CC Catalyzes pseudouridylation at position 93 in U2 snRNA. Also catalyzes
CC pseudouridylation of mRNAs; H/ACA-type snoRNAs probably guide
CC pseudouridylation of mRNAs. {ECO:0000250|UniProtKB:P33322}.
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;
CC Evidence={ECO:0000250|UniProtKB:P33322};
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:0000250|UniProtKB:P33322};
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:0000250|UniProtKB:P33322};
CC -!- SUBUNIT: Component of the small nucleolar ribonucleoprotein particles
CC containing H/ACA-type snoRNAs (H/ACA snoRNPs).
CC {ECO:0000250|UniProtKB:P33322}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P33322}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC {ECO:0000305}.
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DR EMBL; AF008563; AAC64862.1; -; Genomic_DNA.
DR EMBL; CR382124; CAH00369.1; -; Genomic_DNA.
DR RefSeq; XP_453273.1; XM_453273.1.
DR AlphaFoldDB; O13473; -.
DR SMR; O13473; -.
DR STRING; 28985.XP_453273.1; -.
DR EnsemblFungi; CAH00369; CAH00369; KLLA0_D04796g.
DR GeneID; 2893295; -.
DR KEGG; kla:KLLA0_D04796g; -.
DR eggNOG; KOG2529; Eukaryota.
DR HOGENOM; CLU_032087_3_2_1; -.
DR InParanoid; O13473; -.
DR OMA; GPFKEDE; -.
DR Proteomes; UP000000598; Chromosome D.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; IEA:EnsemblFungi.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000495; P:box H/ACA RNA 3'-end processing; IEA:EnsemblFungi.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IEA:EnsemblFungi.
DR GO; GO:0000454; P:snoRNA guided rRNA pseudouridine synthesis; IEA:EnsemblFungi.
DR GO; GO:0031120; P:snRNA pseudouridine synthesis; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW DNA-binding; Isomerase; Microtubule; Nucleus; Reference proteome; Repeat;
KW Ribonucleoprotein; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..474
FT /note="H/ACA ribonucleoprotein complex subunit CBF5"
FT /id="PRO_0000121980"
FT DOMAIN 265..340
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT REPEAT 431..433
FT /note="1"
FT REPEAT 434..436
FT /note="2"
FT REPEAT 437..439
FT /note="3"
FT REPEAT 440..442
FT /note="4"
FT REPEAT 443..445
FT /note="5"
FT REPEAT 446..448
FT /note="6"
FT REPEAT 449..451
FT /note="7"
FT REPEAT 452..454
FT /note="8"
FT REPEAT 455..457
FT /note="9"
FT REGION 356..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..460
FT /note="9 X 3 AA tandem repeats of K-K-[DE]"
FT COMPBIAS 359..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 94
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P60340"
SQ SEQUENCE 474 AA; 53630 MW; 95306ECE7FEA756C CRC64;
MSDEFVIKPE SVSPSSNTSE WPLLLKDYDK LLVRSGHYTP IPAGASPLKR DLKSYISSGV
INLDKPSNPS SHEVVAWIKR ILRCEKTGHS GTLDPKVTGC LIVCVDRATR LVKSQQGAGK
EYVCIVRLHD ALKDEKELGR GLENLTGALF QRPPLISAVK RQLRVRTIYD SNLIEFDNKR
NLGVFWASCE AGTYMRTLCV HLGMLLGVGG HMQELRRVRS GALSENDNLV TLHDVMDAQW
VYDNTRDESY LRKIIQPLET LLVGYKRIVV KDSAVNAVCY GAKLMIPGLL RYEEGIELYD
EVVLITTKGE AIAVAIAQMS TVDLATCDHG VVAKVKRCIM ERDLYPRRWG LGPIAQKKKQ
MKADGKLDKY GRANENTPET WKKTYVSLEN AEPTTAPASK SEEKPLIKEV EKKEVEQKEE
SKEESKTPEE KKDKKEKKEK KDKKEKKEKK EKKEKKRKAD DDESSEKKKK KSKK
