ID F2SND0_TRIRC Unreviewed; 494 AA.
AC F2SND0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=H/ACA ribonucleoprotein complex subunit CBF5 {ECO:0000256|ARBA:ARBA00019272};
GN ORFNames=TERG_04441 {ECO:0000313|EMBL:EGD88191.1};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD88191.1, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; GG700651; EGD88191.1; -; Genomic_DNA.
DR RefSeq; XP_003235386.1; XM_003235338.1.
DR AlphaFoldDB; F2SND0; -.
DR STRING; 559305.F2SND0; -.
DR GeneID; 10379819; -.
DR VEuPathDB; FungiDB:TERG_04441; -.
DR eggNOG; KOG2529; Eukaryota.
DR HOGENOM; CLU_032087_3_2_1; -.
DR InParanoid; F2SND0; -.
DR OMA; CIVRLHD; -.
DR OrthoDB; 5472308at2759; -.
DR Proteomes; UP000008864; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000008864}.
FT DOMAIN 25..83
FT /note="Dyskerin-like"
FT /evidence="ECO:0000259|SMART:SM01136"
FT DOMAIN 275..349
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
FT REGION 401..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 55032 MW; 3AE37A1CA28C1CFA CRC64;
MAATTGKGDV ADYSIKPEAV APPIPTSEWP LLLKNYDKLL VRTSHFTPIP NGCTPLKRDL
KSYISSGVIN LDKPSNPSSH EVVAWMKRML RVEKTGHSGT LDPKVTGCLI VCIDRATRLV
KSQQGAGKEY VCVIRLHDKI PGGEAQFARA LETLSGALFQ RPPLISAVKR QLRIRTIYES
KLYEFDNDRH LGVFWVSCEA GTYIRTLCVH LGLLLGVGAH MQELRRVRSG AMDEKDGMVT
LHDVLDAQWM MDNHRDESYL RKVIRPLESL LTSYKRIVVK DSAVNAVCYG AKLMIPGLLR
FEAGIEIYEE VVLMTTKGEA IAIGIAQMST VELSTCDHGV VAKVKRCIME RDLYPRRWGM
GPVALEKKKL KADGKLDKYG RTNASTPAKW QAEYKDYDAQ AAGTPNAAPA PGATTPAKAA
PAAPAASSPE KEDEEMDDAD KKRKRKDGET AEEREERKRL KKEKKEAKEK KKQEKKEKKE
KRKSKQAEDA SDSD
//