ID M1KJM5_ENCCN Unreviewed; 357 AA.
AC M1KJM5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=H/ACA ribonucleoprotein complex subunit CBF5 {ECO:0000256|ARBA:ARBA00019272};
GN ORFNames=ECU05_1020 {ECO:0000313|EMBL:AGE95411.1};
OS Encephalitozoon cuniculi (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=6035 {ECO:0000313|EMBL:AGE95411.1};
RN [1] {ECO:0000313|EMBL:AGE95411.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23376943; DOI=10.1128/EC.00307-12;
RA Selman M., Sak B., Kvac M., Farinelli L., Weiss L.M., Corradi N.;
RT "Extremely Reduced Levels of Heterozygosity in the Vertebrate Pathogen
RT Encephalitozoon cuniculi.";
RL Eukaryot. Cell 12:496-502(2013).
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:0000256|ARBA:ARBA00001166};
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:0000256|ARBA:ARBA00001896};
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:0000256|ARBA:ARBA00001832};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC {ECO:0000256|ARBA:ARBA00008999}.
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DR EMBL; KC513607; AGE95411.1; -; Genomic_DNA.
DR AlphaFoldDB; M1KJM5; -.
DR VEuPathDB; MicrosporidiaDB:AEWD_051020; -.
DR VEuPathDB; MicrosporidiaDB:AEWQ_051020; -.
DR VEuPathDB; MicrosporidiaDB:AEWR_051020; -.
DR VEuPathDB; MicrosporidiaDB:ECU05_1020; -.
DR VEuPathDB; MicrosporidiaDB:M970_051020; -.
DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd02572; PseudoU_synth_hDyskerin; 1.
DR CDD; cd21148; PUA_Cbf5; 1.
DR Gene3D; 3.30.2350.10; Pseudouridine synthase; 1.
DR Gene3D; 2.30.130.10; PUA domain; 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 NCBIfam; TIGR00425; CBF5; 1.
DR NCBIfam; TIGR00451; unchar_dom_2; 1.
DR PANTHER; PTHR23127; CENTROMERE/MICROTUBULE BINDING PROTEIN CBF5; 1.
DR PANTHER; PTHR23127:SF0; H_ACA RIBONUCLEOPROTEIN COMPLEX SUBUNIT DKC1; 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; Pseudouridine synthase; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
FT DOMAIN 16..74
FT /note="Dyskerin-like"
FT /evidence="ECO:0000259|SMART:SM01136"
FT DOMAIN 263..337
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
SQ SEQUENCE 357 AA; 40192 MW; 999233492D0D8574 CRC64;
MTKSPEYSGA RTGEDGEGVW DLLLANMDRM VVRTGHYTPL GCGSMPLRRR IEEYIKYGII
NVDKSPNPSS HEVVTWVKEI LKCEKTGHSG TLDPQVSGVL TICIDRATRL TKSQQSLGKE
YVCVIEFLSE PDEEGFHKAS KRLVGSLFQR PPLMCAVKRE LRIRNVYSID ILEFNREKRL
GLFKVSCEAG TYVRTLCTHI GILMGCGARM KELRRTRSGR ISEKDAFTLH DLLDAVYIFN
TTKDETVIRR AILPLESLLV GYPRIMIKDS CVNAICYGAK LSITGVLRFD RDIDVGTEVV
IMTTKGEAVA LGIALVSSPE MSIIDHGLVC RTKRVIMEKD LYPRSWGFKN EYEILSE
//