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Entry: F2SND0_TRIRC
LinkDB: F2SND0_TRIRC
Original site: F2SND0_TRIRC 
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}.
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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
//
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