DKC1_CAEEL
ID DKC1_CAEEL Reviewed; 445 AA.
AC O17919;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Putative H/ACA ribonucleoprotein complex subunit 4;
DE EC=5.4.99.-;
GN ORFNames=K01G5.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; Z92803; CAB07244.1; -; Genomic_DNA.
DR PIR; T23199; T23199.
DR RefSeq; NP_499370.1; NM_066969.4.
DR AlphaFoldDB; O17919; -.
DR SMR; O17919; -.
DR BioGRID; 41691; 33.
DR DIP; DIP-25862N; -.
DR IntAct; O17919; 1.
DR STRING; 6239.K01G5.5; -.
DR iPTMnet; O17919; -.
DR EPD; O17919; -.
DR PaxDb; O17919; -.
DR PeptideAtlas; O17919; -.
DR EnsemblMetazoa; K01G5.5.1; K01G5.5.1; WBGene00010478.
DR GeneID; 176504; -.
DR KEGG; cel:CELE_K01G5.5; -.
DR UCSC; K01G5.5.1; c. elegans.
DR CTD; 176504; -.
DR WormBase; K01G5.5; CE16195; WBGene00010478; -.
DR eggNOG; KOG2529; Eukaryota.
DR GeneTree; ENSGT00510000047092; -.
DR HOGENOM; CLU_032087_3_2_1; -.
DR InParanoid; O17919; -.
DR OMA; GPFKEDE; -.
DR OrthoDB; 1070373at2759; -.
DR PhylomeDB; O17919; -.
DR Reactome; R-CEL-171319; Telomere Extension By Telomerase.
DR PRO; PR:O17919; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00010478; Expressed in germ line (C elegans) and 4 other tissues.
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 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_0000121988"
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 386..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 COMPBIAS 405..445
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; 50211 MW; 12F445A78E4A6B88 CRC64;
MGKKDKRSKL EGDDLAEAQQ KGSFQLPSSN ETAKLDASQW PLLLKNYDKL NVRTNHYTPH
VEGVSPLKRD IKNYISSGFF NLDKPSNPSS HEVVSWIKRI LRCEKTGHSG TLDPKVSGCL
IVCIDRTTRL AKSQQGAGKE YICIFKLHEE VEDDRKVKQA LEKLTGALFQ RPPLISAVKR
QLRIRTVYEN KFIEYDPAQQ MGIFNCICES GTYVRTICVH LGLILGCGGQ MQELRRNRSG
ICDENENMVT MHDVLDAQYL LDTQKDESYM RHIVRPLEAL LTQHKRVVVK DSCINAICYG
AKILIPGILR YDDDIEVGKE IVIMSTKGEA ICIAIAQMNT STIASVDHGV VAKSKRVIME
RDVYGRKWGL GPVASKKKQM VKDGLLDKFG KPNDTTPKSW AKEYVQTSTK KEVKKEETPD
EEEEEAPKKK SKKSKKQESS DSDSD
