ID   A0A0F0I167_ASPPU        Unreviewed;       563 AA.
AC   A0A0F0I167;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Pseudouridine synthase PUS1/ PUS2 like {ECO:0000313|EMBL:KJK61455.1};
GN   ORFNames=P875_00042270 {ECO:0000313|EMBL:KJK61455.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK61455.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK61455.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) 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:KJK61455.1}.
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DR   EMBL; JZEE01000675; KJK61455.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0I167; -.
DR   STRING; 1403190.A0A0F0I167; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:InterPro.
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:UP000033540};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          340..446
FT                   /note="Pseudouridine synthase I TruA alpha/beta"
FT                   /evidence="ECO:0000259|Pfam:PF01416"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        138
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR641708-1"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR641708-2"
SQ   SEQUENCE   563 AA;  63309 MW;  DF73040102F8CD33 CRC64;
     MDNNEGRASG SEEADRKRKK GDLGRAEWSR QTSDKRGRID KENQAKRQKL EKGEEVKAPI
     YATHFSQEDI ENEQRRPKKK VAVLLGYSGT GYKGMQLSAT EKTIEGDLFA AFVAAGAISK
     ANAADPKKSS LVRCARTDKG VHAAGNIVSL KLIVEDEDIV QKINAHLSPQ IRVWGILVAS
     KSFSSYQMCD SRIYEYLMPS YCFLPPHPST FLGKKIIEIA EKEGDLEAHK ARQAEVANYW
     EEADAKYIQP VLDTLDEDIR EIVKNAIYHE KPEDESFETE EQAQATEGGA DAATKPELTE
     AELAHRRKII DAVKAVKAAY NTAKRTYRIP PARVARLQEA LDKYLGTKNF YNYTIQKLYK
     DPSAKRHIKS FKVDPNPIII NGTEWLSLKV HGQSFMMHQI RKMVAMATLI VRCGCDPKRI
     VDSYGPTKIP IPKAPGLGLL LERPIFNGYS KKAEELGKKP INFEEYATEM NEFKQREIYD
     RIFREEEETN AFASFFNHID HFPQEEFLYV TSGGIPAAKP ATQPSAATED AQKGRKSQRE
     ALAEIEEESE DEGNLPNNGE EGG
//