GenomeNet

Database: UniProt
Entry: F8MEG0_NEUT8
LinkDB: F8MEG0_NEUT8
Original site: F8MEG0_NEUT8 
ID   F8MEG0_NEUT8            Unreviewed;       480 AA.
AC   F8MEG0;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=H/ACA ribonucleoprotein complex subunit CBF5 {ECO:0000256|ARBA:ARBA00019272};
GN   ORFNames=NEUTE1DRAFT_127587 {ECO:0000313|EMBL:EGO60791.1};
OS   Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO60791.1};
RN   [1] {ECO:0000313|EMBL:EGO60791.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO60791.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL891302; EGO60791.1; -; Genomic_DNA.
DR   RefSeq; XP_009847995.1; XM_009849693.1.
DR   AlphaFoldDB; F8MEG0; -.
DR   GeneID; 20825110; -.
DR   KEGG; nte:NEUTE1DRAFT127587; -.
DR   VEuPathDB; FungiDB:NEUTE1DRAFT_127587; -.
DR   HOGENOM; CLU_032087_3_2_1; -.
DR   OrthoDB; 5472308at2759; -.
DR   Proteomes; UP000008065; Unassembled WGS sequence.
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          19..77
FT                   /note="Dyskerin-like"
FT                   /evidence="ECO:0000259|SMART:SM01136"
FT   DOMAIN          270..344
FT                   /note="PUA"
FT                   /evidence="ECO:0000259|SMART:SM00359"
FT   REGION          403..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..459
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   480 AA;  52880 MW;  D17A9CA3AC4658CE CRC64;
     MGAETEHVIK PQATEPAVDT SEWPLLLKNY SNLLVRTGHF TPIPAGSSPS KRDIKSYVSS
     GVINLDKPSN PSSHEVVAWI KRMLRVEKTG HSGTLDPKVT GCLIVCVDRA TRLVKAQQGA
     GKEYVCVIRF HDSVPGGEAA FASALETLTG ALFQRPPLIS AVKRQLRIRS IYESKLIEFD
     NDRHLGVFWV SCEAGTYIRT LCVHLGLLLG VGAHMQELRR VRSGIMSEDN GSMVTLHDVL
     DAQWQFDNGG DETALRKVIQ PLETLLTTYK RIVVKDSAVN AVCYGAKLML PGLLRFEKGI
     ETHEEVVLMT TKGEAIAIGI AQMNGVEMLS CDHGVVAKVK RCIMERDLYP RRWGLGPVAL
     EKKKLKSDGK LDKFGRPNAE TPAKWTEGYK DFSAAAESEA AAAAAPAAEA AKVEIAERPK
     PEEKAEKSEE AEEAGDSKKR KKHDGETAEE KAERKKQKKE KKEKKEKKEK KSKKGGDESD
//
DBGET integrated database retrieval system