CBF5_SCHPO
ID CBF5_SCHPO Reviewed; 474 AA.
AC O14007;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
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 homolog;
GN Name=cbf5; ORFNames=SPAC29A4.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; CU329670; CAB10131.1; -; Genomic_DNA.
DR PIR; T38485; T38485.
DR RefSeq; NP_594878.1; NM_001020307.2.
DR AlphaFoldDB; O14007; -.
DR SMR; O14007; -.
DR BioGRID; 278941; 12.
DR STRING; 4896.SPAC29A4.04c.1; -.
DR iPTMnet; O14007; -.
DR MaxQB; O14007; -.
DR PaxDb; O14007; -.
DR PRIDE; O14007; -.
DR EnsemblFungi; SPAC29A4.04c.1; SPAC29A4.04c.1:pep; SPAC29A4.04c.
DR GeneID; 2542481; -.
DR KEGG; spo:SPAC29A4.04c; -.
DR PomBase; SPAC29A4.04c; cbf5.
DR VEuPathDB; FungiDB:SPAC29A4.04c; -.
DR eggNOG; KOG2529; Eukaryota.
DR HOGENOM; CLU_032087_3_2_1; -.
DR InParanoid; O14007; -.
DR OMA; GPFKEDE; -.
DR PhylomeDB; O14007; -.
DR Reactome; R-SPO-171319; Telomere Extension By Telomerase.
DR PRO; PR:O14007; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; ISO:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0034513; F:box H/ACA snoRNA binding; IC:PomBase.
DR GO; GO:0009982; F:pseudouridine synthase activity; ISO:PomBase.
DR GO; GO:0019843; F:rRNA binding; ISO:PomBase.
DR GO; GO:0000495; P:box H/ACA RNA 3'-end processing; ISO:PomBase.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0031118; P:rRNA pseudouridine synthesis; ISO:PomBase.
DR GO; GO:0031120; P:snRNA pseudouridine synthesis; ISO:PomBase.
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 Isomerase; Nucleus; Reference proteome; Repeat; Ribonucleoprotein;
KW Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..474
FT /note="H/ACA ribonucleoprotein complex subunit cbf5"
FT /id="PRO_0000121981"
FT DOMAIN 271..346
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT REPEAT 443..445
FT /note="1"
FT REPEAT 450..452
FT /note="2"
FT REPEAT 454..456
FT /note="3"
FT REPEAT 457..459
FT /note="4"
FT REPEAT 460..462
FT /note="5"
FT REPEAT 463..465
FT /note="6"
FT REPEAT 466..468
FT /note="7"
FT REGION 361..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..468
FT /note="7 X 3 AA approximate tandem repeats of K-K-E"
FT COMPBIAS 363..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 100
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P60340"
SQ SEQUENCE 474 AA; 53110 MW; B8C9896C5FAEEB71 CRC64;
MTDTHPGVDF MIKPEATSAS KIDTAEWPLL LKNFDKLLVR TGHYTPIPCG NNPLKRPIAE
YVSSGVINLD KPANPSSHEV VAWVKKILRV EKTGHSGTLD PKVTGCLIIC NDRATRLVKS
QQSAGKEYVC VLRLHDSVEG ERNVASAIET LTGALFQRPP LISAVKRQLR IRSIYESKLI
EFDNERNLAV FWASCEAGTY MRTLCVHLGL LLGVGGHMQE LRRVRSGCLS ENDDIVTMHD
VLDAQWIYDN TRDESYLRRV IRPLESLLVG YKRIVVKDSA VNAICYGAKL MIPGLLRYEA
GIEVNEEIVL ITTKGEAIAV GIAQMSTVEL STCDHGVVAK VKRCIMERDV YPRRWGLGPQ
SMKKKTLKKE GKLDKYGRPN ENTPADWSKS YIDYSDPNAE VAKPAPVVAP AAPTVEAEVN
GVEDSKKRKS VESSEKDEDE AAKKEEKRRK KEAKKEKKEK KEKKEKKEKK KKSE
