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Centromere/microtubule-binding protein CBF5 (Centromere-binding factor 5) (H/ACA snoRNP protein CBF5) (Small nucleolar RNP protein CBF5)

 CBF5_KLULA              Reviewed;         474 AA.
O13473;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
20-JUN-2018, entry version 112.
RecName: Full=H/ACA ribonucleoprotein complex subunit CBF5 {ECO:0000305};
EC=5.4.99.- {ECO:0000250|UniProtKB:P33322};
AltName: Full=Centromere-binding factor 5;
AltName: Full=H/ACA snoRNP protein CBF5;
AltName: Full=Small nucleolar RNP protein CBF5;
Name=CBF5; OrderedLocusNames=KLLA0D04796g;
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC
1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
NCBI_TaxID=284590;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC MYA-539 / JBD100;
PubMed=9483794;
DOI=10.1002/(SICI)1097-0061(19980115)14:1<37::AID-YEA198>3.3.CO;2-U;
Winkler A.A., Bobok A., Zonneveld B.J.M., Steensma H.Y.,
Hooykaas P.J.J.;
"The lysine-rich C-terminal repeats of the centromere-binding factor 5
(Cbf5) of Kluyveromyces lactis are not essential for function.";
Yeast 14:37-48(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
WM37;
PubMed=15229592; DOI=10.1038/nature02579;
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
-!- FUNCTION: Catalytic subunit of H/ACA small nucleolar
ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes
pseudouridylation of rRNA. This involves the isomerization of
uridine such that the ribose is subsequently attached to C5,
instead of the normal N1. Pseudouridine ('psi') residues may serve
to stabilize the conformation of rRNAs and play a central role in
ribosomal RNA processing. The H/ACA snoRNP complex also mediates
pseudouridylation of other types of RNAs. Catalyzes
pseudouridylation at position 93 in U2 snRNA. Also catalyzes
pseudouridylation of mRNAs; H/ACA-type snoRNAs probably guide
pseudouridylation of mRNAs. {ECO:0000250|UniProtKB:P33322}.
-!- CATALYTIC ACTIVITY: rRNA uridine = rRNA pseudouridine.
{ECO:0000250|UniProtKB:P33322}.
-!- CATALYTIC ACTIVITY: snRNA uridine = snRNA pseudouridine.
{ECO:0000250|UniProtKB:P33322}.
-!- CATALYTIC ACTIVITY: mRNA uridine = mRNA pseudouridine.
{ECO:0000250|UniProtKB:P33322}.
-!- SUBUNIT: Component of the small nucleolar ribonucleoprotein
particles containing H/ACA-type snoRNAs (H/ACA snoRNPs).
{ECO:0000250|UniProtKB:P33322}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000250|UniProtKB:P33322}.
-!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
{ECO:0000305}.
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EMBL; AF008563; AAC64862.1; -; Genomic_DNA.
EMBL; CR382124; CAH00369.1; -; Genomic_DNA.
RefSeq; XP_453273.1; XM_453273.1.
ProteinModelPortal; O13473; -.
SMR; O13473; -.
STRING; 284590.XP_453273.1; -.
PRIDE; O13473; -.
EnsemblFungi; CAH00369; CAH00369; KLLA0_D04796g.
GeneID; 2893295; -.
KEGG; kla:KLLA0D04796g; -.
eggNOG; KOG2529; Eukaryota.
eggNOG; COG0130; LUCA.
HOGENOM; HOG000231224; -.
InParanoid; O13473; -.
KO; K11131; -.
OMA; IYQRPPL; -.
OrthoDB; EOG092C28F5; -.
Proteomes; UP000000598; Chromosome D.
GO; GO:0031429; C:box H/ACA snoRNP complex; IEA:EnsemblFungi.
GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0009982; F:pseudouridine synthase activity; IEA:EnsemblFungi.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0000495; P:box H/ACA snoRNA 3'-end processing; IEA:EnsemblFungi.
GO; GO:1990481; P:mRNA pseudouridine synthesis; IEA:EnsemblFungi.
GO; GO:0031118; P:rRNA pseudouridine synthesis; IEA:EnsemblFungi.
GO; GO:0031120; P:snRNA pseudouridine synthesis; IEA:EnsemblFungi.
InterPro; IPR012960; Dyskerin-like.
InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
InterPro; IPR002501; PsdUridine_synth_N.
InterPro; IPR002478; PUA.
InterPro; IPR015947; PUA-like_sf.
InterPro; IPR004802; tRNA_PsdUridine_synth_B_fam.
InterPro; IPR032819; TruB_C.
InterPro; IPR004521; Uncharacterised_CHP00451.
PANTHER; PTHR23127; PTHR23127; 1.
Pfam; PF08068; DKCLD; 1.
Pfam; PF01472; PUA; 1.
Pfam; PF16198; TruB_C_2; 1.
Pfam; PF01509; TruB_N; 1.
SMART; SM01136; DKCLD; 1.
SMART; SM00359; PUA; 1.
SUPFAM; SSF55120; SSF55120; 1.
SUPFAM; SSF88697; SSF88697; 1.
TIGRFAMs; TIGR00425; CBF5; 1.
TIGRFAMs; TIGR00451; unchar_dom_2; 1.
PROSITE; PS50890; PUA; 1.
3: Inferred from homology;
Complete proteome; DNA-binding; Isomerase; Microtubule; Nucleus;
Reference proteome; Repeat; Ribonucleoprotein; Ribosome biogenesis;
RNA-binding; rRNA processing.
CHAIN 1 474 H/ACA ribonucleoprotein complex subunit
CBF5.
/FTId=PRO_0000121980.
DOMAIN 265 340 PUA. {ECO:0000255|PROSITE-
ProRule:PRU00161}.
REPEAT 431 433 1.
REPEAT 434 436 2.
REPEAT 437 439 3.
REPEAT 440 442 4.
REPEAT 443 445 5.
REPEAT 446 448 6.
REPEAT 449 451 7.
REPEAT 452 454 8.
REPEAT 455 457 9.
REGION 431 460 9 X 3 AA tandem repeats of K-K-[DE].
ACT_SITE 94 94 Nucleophile.
{ECO:0000250|UniProtKB:P60340}.
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


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