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Database: UniProt
Entry: M1KJM5_ENCCN
LinkDB: M1KJM5_ENCCN
Original site: M1KJM5_ENCCN 
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
//
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