DKC1_CHICK
ID DKC1_CHICK Reviewed; 516 AA.
AC Q5ZJH9;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=H/ACA ribonucleoprotein complex subunit DKC1;
DE EC=5.4.99.- {ECO:0000250|UniProtKB:O60832};
DE AltName: Full=Dyskerin;
GN Name=DKC1; ORFNames=RCJMB04_17p9;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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. Each rRNA can
CC contain up to 100 pseudouridine ('psi') residues, which may serve to
CC stabilize the conformation of rRNAs. Required for ribosome biogenesis
CC and telomere maintenance. {ECO:0000250|UniProtKB:O60832}.
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:O60832};
CC -!- SUBUNIT: Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA
CC snoRNP) complex, which contains NHP2/NOLA2, GAR1/NOLA1, NOP10/NOLA3,
CC and DKC1/NOLA4, which is presumed to be the catalytic subunit. The
CC complex contains a stable core formed by binding of one or two NOP10-
CC DKC1 heterodimers to NHP2; GAR1 subsequently binds to this core via
CC DKC1. The complex binds a box H/ACA small nucleolar RNA (snoRNA), which
CC may target the specific site of modification within the RNA substrate.
CC {ECO:0000250|UniProtKB:O60832}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:O60832}. Nucleus, Cajal body
CC {ECO:0000250|UniProtKB:P40615}. Note=Also localized to Cajal bodies
CC (coiled bodies). {ECO:0000250|UniProtKB:P40615}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC {ECO:0000305}.
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DR EMBL; AJ720455; CAG32114.1; -; mRNA.
DR RefSeq; NP_001026286.1; NM_001031115.1.
DR AlphaFoldDB; Q5ZJH9; -.
DR SMR; Q5ZJH9; -.
DR STRING; 9031.ENSGALP00000008091; -.
DR PaxDb; Q5ZJH9; -.
DR PRIDE; Q5ZJH9; -.
DR GeneID; 422196; -.
DR KEGG; gga:422196; -.
DR CTD; 1736; -.
DR VEuPathDB; HostDB:geneid_422196; -.
DR eggNOG; KOG2529; Eukaryota.
DR InParanoid; Q5ZJH9; -.
DR OrthoDB; 1070373at2759; -.
DR PhylomeDB; Q5ZJH9; -.
DR Reactome; R-GGA-417076; Assembly of telomerase and telomere extension.
DR PRO; PR:Q5ZJH9; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; IBA:GO_Central.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005697; C:telomerase holoenzyme complex; ISS:UniProtKB.
DR GO; GO:0009982; F:pseudouridine synthase activity; ISS:UniProtKB.
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:0000455; P:enzyme-directed rRNA pseudouridine synthesis; ISS:UniProtKB.
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 GO; GO:0007004; P:telomere maintenance via telomerase; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Coiled coil; Isomerase; Nucleus; Reference proteome; Ribonucleoprotein;
KW Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..516
FT /note="H/ACA ribonucleoprotein complex subunit DKC1"
FT /id="PRO_0000121986"
FT DOMAIN 294..369
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 463..516
FT /evidence="ECO:0000255"
FT COMPBIAS 434..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P60340"
SQ SEQUENCE 516 AA; 58150 MW; C42EAF2E4866D9DC CRC64;
MADGDGSSVK KRRKKDKRSL PDEDVADIQH TEEFLIKPES RVAQLDTSQW PLLLKNFDKL
NVLTTHYTPL PSGANPLKRE ISDYVRSGFI NLDKPSNPSS HEVVAWIRRI LRVEKTGHSG
TLDPKVTGCL IVCIERATRL VKSQQSAGKE YVGIVRLHNA IESEAQLARA IETLTGALFQ
RPPLIAAVKR QLRVRTIYES KLVEYDPERR LGIFWVSCEA GTYIRTLCVH LGLLLGVGGQ
MQELRRVRSG ILGEMDNMVT MHDVLDAQWQ YDNNKDDSYL RRVILPLEKL LTSHKRLVMK
DSAVNAICYG AKIMLPGVLR YEDGIELKQE IVVITTKGEA ICLAIALMTT AVISTCDHGV
VAKIKRVIME RDTYPRKWGL GPKASQKKMM IQKGLLDKHG KPNECTPDSW KKEYVDYRES
SKKEAAKVPQ AVSEVERAPK RKRESESENE AVSPPPSPAT PPPEELSKKE KKKKKKEKKA
KEAAESGEEQ VEVISESSAK KKKKKKKQKE VEESSE
