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Database: UniProt
Entry: A0A0A2WIF6_BEABA
LinkDB: A0A0A2WIF6_BEABA
Original site: A0A0A2WIF6_BEABA 
ID   A0A0A2WIF6_BEABA        Unreviewed;       609 AA.
AC   A0A0A2WIF6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=tRNA pseudouridine synthase 1 {ECO:0000313|EMBL:KGQ12904.1};
GN   ORFNames=BBAD15_g1339 {ECO:0000313|EMBL:KGQ12904.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ12904.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ12904.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ12904.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA   Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC       {ECO:0000256|ARBA:ARBA00009375}.
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:KGQ12904.1}.
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DR   EMBL; ANFO01000076; KGQ12904.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2WIF6; -.
DR   STRING; 1245745.A0A0A2WIF6; -.
DR   eggNOG; KOG2553; Eukaryota.
DR   HOGENOM; CLU_021971_1_0_1; -.
DR   Proteomes; UP000030106; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          400..506
FT                   /note="Pseudouridine synthase I TruA alpha/beta"
FT                   /evidence="ECO:0000259|Pfam:PF01416"
FT   REGION          17..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..335
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..609
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        172
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR641708-1"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR641708-2"
SQ   SEQUENCE   609 AA;  68680 MW;  EE434CF657534A60 CRC64;
     MLPIPIASLR TRVNATMATN GESSADIPPA GGRNDSRQDR KQRFGGSRFN SNNQRKKGRG
     GKSSDNKRGE KREGASDWRE YKRRKVDSAG EVIEAKNPFS KDEIAAEERR PKRKVAVMIG
     YSGTGYKGMQ VNGDEPTIER DLFQAFIKAG AISKANADDP RKSSLARCAR TDKGVHAAGN
     VISLKLIIED EDIVDKINAA LPEQIRIWGI QRTNNSFNCY QYCDSRFYEY LLPSYCLLPP
     HPQTFLGQKL VELNKEYGYE DEYHASMADV KNFWAEVEEN DIKPILAKLD PEVRAAVLER
     IHSIDDPEAA KEEAAKEEAA KEEAVQEEPK NDELVAEEAP ATNAEPEAAA ANPVVLTSTK
     PKGRELGPVD FALRDIKAAY INAKRRYRIT PARRERLQEA LDKYTGTRNF HNYTVQKAYG
     DPSAKRTIKS FKVNPTPVLI NNTEWLSLKV HGQSFMMHQI RKMVGLVSLM VRCGTPLERM
     DESYQNHKMA IPKAPGLGLL LEHPVFTNFN RRATDNLGRD EIDFEKYADK MGAFKDKEIY
     QRIFDVEEKE NTFHAFFNQI DQFKANHFLW LTAGGLKVAE IAKEESGKEE DVDKQLGDED
     EEDPDGGQG
//
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