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Database: UniProt
Entry: A0A163M0D1_DIDRA
LinkDB: A0A163M0D1_DIDRA
Original site: A0A163M0D1_DIDRA 
ID   A0A163M0D1_DIDRA        Unreviewed;       483 AA.
AC   A0A163M0D1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=H/ACA ribonucleoprotein complex subunit CBF5 {ECO:0000256|ARBA:ARBA00019272};
GN   ORFNames=ST47_g576 {ECO:0000313|EMBL:KZM28286.1};
OS   Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS   rabiei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX   NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM28286.1, ECO:0000313|Proteomes:UP000076837};
RN   [1] {ECO:0000313|EMBL:KZM28286.1, ECO:0000313|Proteomes:UP000076837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ArDII {ECO:0000313|EMBL:KZM28286.1,
RC   ECO:0000313|Proteomes:UP000076837};
RX   PubMed=27091329; DOI=10.1038/srep24638;
RA   Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT   "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT   Ascochyta rabiei provides insight into the necrotrophic effector
RT   repertoire.";
RL   Sci. Rep. 6:24638-24638(2016).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZM28286.1}.
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DR   EMBL; JYNV01000025; KZM28286.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A163M0D1; -.
DR   STRING; 5454.A0A163M0D1; -.
DR   Proteomes; UP000076837; 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:UP000076837}.
FT   DOMAIN          23..81
FT                   /note="Dyskerin-like"
FT                   /evidence="ECO:0000259|SMART:SM01136"
FT   DOMAIN          273..347
FT                   /note="PUA"
FT                   /evidence="ECO:0000259|SMART:SM00359"
FT   REGION          367..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..456
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..471
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   483 AA;  53807 MW;  1ACDFA38009C4AA5 CRC64;
     MALVQTNPDA YVIKPEAAAP AIDTSDWPLL LKNYSDLLVR TSHYTPIPQG CAPLARDLKS
     YISSGVINLD KPSNPSSHEV VSWIKRMLRV EKTGHSGTLD PKVTGCLIVC IDRATRLVKS
     QQGAGKEYVC VIRMHDKLPG GEAQFARALE TLTGALFQRP PLISAVKRQL RIRTIHESKL
     YEFDNERQLG VFWVSCEAGT YIRTLCVHLG LLLGVGAHMQ ELRRVRSGAM DETKDLVTLH
     DVLDAQWLHD NNRDESYLRH VISPLESLLT SYKRIVVKDS SVNAICYGAK LMLPGLLRFE
     KGIEIHEEIV LMTTKGEAIA LAYAQMSAVE MTSCDHGVVA KIKRVIMERD LYPRRWGMGP
     VATEKKKMKE AGTLDKFGRP NEKTPAKWNT EYKDFNRTDV ESATLAETTS TAEVLAAPAV
     APTGEAPEAS GASEKTKKRK HDEEETAEEK AERKRKKKEE KAAKKAKKEK RKSKAADSDS
     DSD
//
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