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Database: UniProt
Entry: E6ZSJ4_SPORE
LinkDB: E6ZSJ4_SPORE
Original site: E6ZSJ4_SPORE 
ID   E6ZSJ4_SPORE            Unreviewed;       570 AA.
AC   E6ZSJ4;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Related to PUS1-pseudouridine synthase 1 {ECO:0000313|EMBL:CBQ70201.1};
GN   ORFNames=sr16406 {ECO:0000313|EMBL:CBQ70201.1};
OS   Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX   NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ70201.1, ECO:0000313|Proteomes:UP000008867};
RN   [1] {ECO:0000313|EMBL:CBQ70201.1, ECO:0000313|Proteomes:UP000008867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX   PubMed=21148393; DOI=10.1126/science.1195330;
RA   Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA   Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA   Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA   Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA   Kahmann R.;
RT   "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL   Science 330:1546-1548(2010).
CC   -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC       {ECO:0000256|ARBA:ARBA00009375}.
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DR   EMBL; FQ311440; CBQ70201.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6ZSJ4; -.
DR   SMR; E6ZSJ4; -.
DR   EnsemblFungi; CBQ70201; CBQ70201; sr16406.
DR   VEuPathDB; FungiDB:sr16406; -.
DR   eggNOG; KOG2553; Eukaryota.
DR   HOGENOM; CLU_021971_0_2_1; -.
DR   OrthoDB; 12038at2759; -.
DR   Proteomes; UP000008867; Chromosome 19.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:1990481; P:mRNA pseudouridine synthesis; IEA:EnsemblFungi.
DR   GO; GO:0031120; P:snRNA pseudouridine synthesis; IEA:EnsemblFungi.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:EnsemblFungi.
DR   CDD; cd02568; PseudoU_synth_PUS1_PUS2; 1.
DR   Gene3D; 3.30.70.660; Pseudouridine synthase I, catalytic domain, C-terminal subdomain; 1.
DR   Gene3D; 3.30.70.580; Pseudouridine synthase I, catalytic domain, N-terminal subdomain; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR001406; PsdUridine_synth_TruA.
DR   InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom.
DR   InterPro; IPR020095; PsdUridine_synth_TruA_C.
DR   InterPro; IPR041708; PUS1/PUS2-like.
DR   InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR   NCBIfam; TIGR00071; hisT_truA; 1.
DR   PANTHER; PTHR11142; PSEUDOURIDYLATE SYNTHASE; 1.
DR   PANTHER; PTHR11142:SF4; PSEUDOURIDYLATE SYNTHASE 1 HOMOLOG; 1.
DR   Pfam; PF01416; PseudoU_synth_1; 1.
DR   SUPFAM; SSF55120; Pseudouridine synthase; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          296..400
FT                   /note="Pseudouridine synthase I TruA alpha/beta"
FT                   /evidence="ECO:0000259|Pfam:PF01416"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..570
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        153
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR641708-1"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR641708-2"
SQ   SEQUENCE   570 AA;  63489 MW;  72CE5DA17D3952CD CRC64;
     MTERLEQEVG AAATGADPRS LKREFDSEPA TVDTTAQNSA PAEAEASTPK RARFDDAKKK
     WERRDRRGTG RVPDDTSSSA DPSSSTGGDR LPKRKVAVKF GYCGIGYSGL QINPGVKTIE
     GDIFQAFCTA GAVSADNAVN PNKVGLQRAA RTDRGVHAAG NLLSLKLILQ PDGLQEGETL
     VDRVNALLPE FIRVWGVTRV QNGFSARQSC DSRMYEYLLP TYVFVPPKPG STMHDMLVRM
     RDDELAKTGA TTLGDVVDHA FWTQHGTTHD FSTDMRAKTA FRLPASALAR IRSIFARYLG
     SHNFHNFTVG KEFRDRSCQR FMKQLTISDP TVIGDTEWVS IKFHGQSFML HQIRKMIGLL
     VLVGRTGAGE GLVDECFGPA RVHIPKAPGL GLLLEQPIFD AYNTRIRNNN DKIAKLMRKK
     ASSDQKDSAP ESADRDAGRN STLHDELRES ISYAPHAAAM QQFKQQWIYD RIHSTEQDTY
     EFGKWLNYLD VFQGPDFEFL NPKGVIPPQC IVKVGEFHRD NLRRARESQL GGKEGGGSEQ
     QRQQQQDDDD DDEDHEAYSK KGAELDEYEG
//
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