CBF5_EMENI
ID CBF5_EMENI Reviewed; 481 AA.
AC O43100; C8V9H8; Q541P5; Q5AS79;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
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;
DE AltName: Full=rRNA pseudouridine synthase;
GN Name=cbf5; Synonyms=swoC; ORFNames=AN8851;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Jiang W., Clifford J., Koltin Y.;
RT "A highly conserved nucleolar protein Cbf5p may be involved in the
RT centromere DNA-binding activity of protein complex CBF3.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14573468; DOI=10.1093/genetics/165.2.543;
RA Lin X., Momany M.;
RT "The Aspergillus nidulans swoC1 mutant shows defects in growth and
RT development.";
RL Genetics 165:543-554(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA60139.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U59148; AAB94296.1; -; mRNA.
DR EMBL; AY057454; AAL23694.1; -; Genomic_DNA.
DR EMBL; AACD01000163; EAA60139.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001303; CBF77883.1; -; Genomic_DNA.
DR RefSeq; XP_682120.1; XM_677028.1.
DR AlphaFoldDB; O43100; -.
DR SMR; O43100; -.
DR STRING; 162425.CADANIAP00006202; -.
DR PRIDE; O43100; -.
DR EnsemblFungi; CBF77883; CBF77883; ANIA_08851.
DR EnsemblFungi; EAA60139; EAA60139; AN8851.2.
DR GeneID; 2868403; -.
DR KEGG; ani:AN8851.2; -.
DR VEuPathDB; FungiDB:AN8851; -.
DR eggNOG; KOG2529; Eukaryota.
DR HOGENOM; CLU_032087_3_2_1; -.
DR InParanoid; O43100; -.
DR OMA; GPFKEDE; -.
DR OrthoDB; 441201at2759; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0004730; F:pseudouridylate synthase activity; ISA:AspGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051211; P:anisotropic cell growth; IMP:AspGD.
DR GO; GO:0000495; P:box H/ACA RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0048315; P:conidium formation; IMP:AspGD.
DR GO; GO:0006897; P:endocytosis; IMP:AspGD.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:AspGD.
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:0000454; P:snoRNA guided rRNA pseudouridine synthesis; IEA:EnsemblFungi.
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; 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 2: Evidence at transcript level;
KW DNA-binding; Isomerase; Microtubule; Nucleus; Reference proteome; Repeat;
KW Ribonucleoprotein; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..481
FT /note="H/ACA ribonucleoprotein complex subunit CBF5"
FT /id="PRO_0000121979"
FT DOMAIN 268..343
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT REGION 387..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 96
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P60340"
SQ SEQUENCE 481 AA; 54204 MW; A671BB6C57CE9590 CRC64;
MAKEVDYTIK PEATASNINT EDWPLLLKNY DKLMVRTGHF TPIPAGSSPL KRDLKSYINS
GVINLDKPSN PSSHEVVAWM KRILRAEKTG HSGTLDPKVT GCLIVCIDRA TRLVKSQQGA
GKEYVCVIRL HDKIPGGEAQ FKRALETLTG ALFQRPPLIS AVKRQLRIRT IHESKLYEFD
NERHLGVFWV SCEAGTYIRT LCVHLGLLLG VGAHMQELRR VRSGAMSENE GMVTLHDVLD
AQWLYDNQRD ESYLRKVIKP LESLLTTYKR IVVKDSAVNA VCYGAKLMIP GLLRFEAGIE
LGEEVVLMTT KGEAIAIGIA QMSTVELSTC DHGVVAKVKR CIMERDLYPR RWGLGPVALE
KKKLKSSGKL DKYGRANEAT PAKWKSEYKD YSAPDGDSSQ QAVDVVAKEE ASPKEEPSLE
ANESKMDIDD AQDDEDKKKR KRHEGETPEE RAERKRKKKE KKEKKERRKS KQEKDDSDDS
D
