CBF5_CHATD
ID CBF5_CHATD Reviewed; 483 AA.
AC G0SGK0;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 2.
DT 25-MAY-2022, entry version 41.
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=Centromere/microtubule-binding protein CBF5;
DE AltName: Full=H/ACA snoRNP protein CBF5;
DE AltName: Full=Small nucleolar RNP protein CBF5;
GN Name=CBF5; ORFNames=CTHT_0066610;
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=759272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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=EGS17339.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; GL988047; EGS17339.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_006696957.1; XM_006696894.1.
DR AlphaFoldDB; G0SGK0; -.
DR SMR; G0SGK0; -.
DR STRING; 759272.G0SGK0; -.
DR EnsemblFungi; EGS17339; EGS17339; CTHT_0066610.
DR GeneID; 18260699; -.
DR KEGG; cthr:CTHT_0066610; -.
DR eggNOG; KOG2529; Eukaryota.
DR HOGENOM; CLU_014935_0_0_1; -.
DR OrthoDB; 539847at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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 Cell cycle; Cell division; DNA-binding; Isomerase; Microtubule; Mitosis;
KW Nucleus; Reference proteome; Repeat; Ribonucleoprotein;
KW Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..483
FT /note="H/ACA ribonucleoprotein complex subunit CBF5"
FT /id="PRO_5003409223"
FT DOMAIN 279..354
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT REGION 406..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 53313 MW; A5B6036DCF2EA8D9 CRC64;
MSGSAAIMKA PAKSEFIIKP ENTKAEVDTS NWPGLLKNYD KMLIRTSHFT PIPDHGSAPW
SRDIKSYVSS GVINLDKPSN PSSHEVVAWI KRILRVDKTG HSGTLDPKVT GCLIVCIDRA
TRLVKAQQGA GKEYVCCIRF HDTVPGGEPA FAKALETLTG ALFQRPPLIS AVKRQLRIRT
IHKSRLLEFD NERHLGVFWV SCEAGTYIRT LCVHLGLLLG VGAHMQELRR VRSGVMSEDD
GSLVTLHDVL DAQWQYDNNG DEALLRKVIQ PLETLLCTYK RLVVKDTAVN AVCYGAKLMI
PGLLRYDQGI EQGEEVVLMT TKGEAIAIAI AQMGAVELAT CDHGCVAKVK RCIMERDLYP
RRWGMGPVAS EKKKLKASGL LDKYGRPNEK TPASWLQSYK DYNVSSSEAP ALPAPAGADA
AAAPSTPALP APEEKNESEE KSADASDSKK RKKDETAEEK AERKRLKKEK KEKKEKKKSD
KDE
