ID   DKC1_CAEBR              Reviewed;         445 AA.
AC   Q60YA8; A8XSE8;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Putative H/ACA ribonucleoprotein complex subunit 4;
DE            EC=5.4.99.-;
GN   ORFNames=CBG18316;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Plays a central role in ribosomal RNA processing. Probable
CC       catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA
CC       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 (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a uridine in RNA = a pseudouridine in RNA;
CC         Xref=Rhea:RHEA:48348, Rhea:RHEA-COMP:12068, Rhea:RHEA-COMP:12069,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC   -!- SUBUNIT: Component of the small nucleolar ribonucleoprotein particle
CC       containing H/ACA-type snoRNAs (H/ACA snoRNPs). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC       {ECO:0000305}.
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DR   EMBL; HE600936; CAP35790.1; -; Genomic_DNA.
DR   RefSeq; XP_002642321.1; XM_002642275.1.
DR   AlphaFoldDB; Q60YA8; -.
DR   SMR; Q60YA8; -.
DR   STRING; 6238.CBG18316; -.
DR   EnsemblMetazoa; CBG18316.1; CBG18316.1; WBGene00037760.
DR   GeneID; 8584315; -.
DR   KEGG; cbr:CBG_18316; -.
DR   CTD; 8584315; -.
DR   WormBase; CBG18316; CBP04263; WBGene00037760; -.
DR   eggNOG; KOG2529; Eukaryota.
DR   HOGENOM; CLU_032087_3_2_1; -.
DR   InParanoid; Q60YA8; -.
DR   OMA; GPFKEDE; -.
DR   OrthoDB; 1070373at2759; -.
DR   Proteomes; UP000008549; Chromosome III.
DR   GO; GO:0031429; C:box H/ACA snoRNP complex; IBA:GO_Central.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000495; P:box H/ACA RNA 3'-end processing; IBA:GO_Central.
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: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   3: Inferred from homology;
KW   Coiled coil; Isomerase; Nucleus; Reference proteome; Ribonucleoprotein;
KW   Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..445
FT                   /note="Putative H/ACA ribonucleoprotein complex subunit 4"
FT                   /id="PRO_0000121987"
FT   DOMAIN          284..359
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          407..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        113
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   445 AA;  50226 MW;  554BF5C457942E09 CRC64;
     MGKKDKRSKL EGDELAEAQQ KGSFQLPSSN ETAKLDASQW PLLLKNYDKL NVRTNHYTPH
     VEGVSPLKRD IKNYISSGFF NLDKPSNPSS HEVVSWIKRI LRCEKTGHSG TLDPKVSGCL
     IVCIDRTTRL AKSQQGAGKE YICIFKLHEE VEDERKVKQA LEKLTGALFQ RPPLISAVKR
     QLRIRTVYEN KFIEYDPAQQ MGIFNCICES GTYVRTICVH LGLILGCGGQ MQELRRNRSG
     ICDENENMVT MHDVLDAQYM LDTQKDESYM RHIVRPLEAL LTQHKRVVVK DSCVNAICYG
     AKILIPGILR YDDDIEVGKE IVIMTTKGEA ICIAIAQMST STIASVDHGI VAKSKRVIME
     RDVYGRKWGL GPVASKKKQM VKDGLLDKFG KPNITTPKSW AKEYVQTDKV KKEQEDKEDE
     EEEEAPKKKS KKAAKKEVSS SSDSE