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Database: UniProt
Entry: B2AE77_PODAN
LinkDB: B2AE77_PODAN
Original site: B2AE77_PODAN 
ID   B2AE77_PODAN            Unreviewed;       479 AA.
AC   B2AE77;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN   ORFNames=PODANS_4_3110 {ECO:0000313|EMBL:CAP61743.1};
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP61743.1};
RN   [1] {ECO:0000313|EMBL:CAP61743.1, ECO:0000313|Proteomes:UP000001197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC   {ECO:0000313|EMBL:CAP61743.1};
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2] {ECO:0000313|EMBL:CAP61743.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP61743.1};
RA   Genoscope - CEA;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000001197}
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197};
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
RN   [4] {ECO:0000313|EMBL:CDP28091.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA   Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil.
CC       {ECO:0000256|RuleBase:RU362028}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a uridine in RNA = a pseudouridine in RNA;
CC         Xref=Rhea:RHEA:48348, Rhea:RHEA-COMP:12068, Rhea:RHEA-COMP:12069,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC         Evidence={ECO:0000256|RuleBase:RU362028};
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC       {ECO:0000256|RuleBase:RU362028}.
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DR   EMBL; CU633455; CAP61743.1; -; Genomic_DNA.
DR   EMBL; FO904939; CDP28091.1; -; Genomic_DNA.
DR   RefSeq; XP_001903966.1; XM_001903931.1.
DR   AlphaFoldDB; B2AE77; -.
DR   STRING; 515849.B2AE77; -.
DR   GeneID; 6188054; -.
DR   KEGG; pan:PODANSg983; -.
DR   VEuPathDB; FungiDB:PODANS_4_3110; -.
DR   eggNOG; KOG1919; Eukaryota.
DR   HOGENOM; CLU_016902_12_4_1; -.
DR   OrthoDB; 5479603at2759; -.
DR   Proteomes; UP000001197; Chromosome 4.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR   CDD; cd02557; PseudoU_synth_ScRIB2; 1.
DR   Gene3D; 3.30.2350.10; Pseudouridine synthase; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR006224; PsdUridine_synth_RluA-like_CS.
DR   InterPro; IPR006225; PsdUridine_synth_RluC/D.
DR   InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR   NCBIfam; TIGR00005; rluA_subfam; 1.
DR   PANTHER; PTHR21600; MITOCHONDRIAL RNA PSEUDOURIDINE SYNTHASE; 1.
DR   PANTHER; PTHR21600:SF40; PSEUDOURIDYLATE SYNTHASE RPUSD2; 1.
DR   Pfam; PF00849; PseudoU_synth_2; 1.
DR   SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR   PROSITE; PS01129; PSI_RLU; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|RuleBase:RU362028};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          152..330
FT                   /note="Pseudouridine synthase RsuA/RluA-like"
FT                   /evidence="ECO:0000259|Pfam:PF00849"
FT   REGION          281..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        196
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ   SEQUENCE   479 AA;  53285 MW;  53C4839E124C4B69 CRC64;
     MTASILLPGA PSQPLTAVVA ENNKVVESTG AISYTEPSLI SQPEPSASLG PPHPYFFKDG
     LRRVAPYFYT YNTWCKERWR GRKIIEVFES EFRERPVEYY RAAMESGQVA VNGKIVSPDY
     VMVNGDLVSH TTHRHEPPVT QDPVQVIHED DDMIVINKPS GVPVHPAGRY HYNSVVEIMK
     AERGPTFAPR PCNRLDRLTS GIMFIAKTAK AAESLSAQIF RRSVRKEYLA RVVGRFPDGE
     VVCDQPILQI SPKLGLNRVR ANGKSAKTVF KRLAYYPSPI IKPSSSNSPS PDEAETGGPE
     DQFTRETEGY SIVRCLPVTG RTHQIRVHLQ FLGHPVQNDP IYANQKVWGF DLGRNDAEAT
     LNTDEDVLSR LARMGKEQVA DAVAYYDEMV DVYHKKKAER MSGQLCDVCE TPLYTDPGSQ
     ELSLWLHSLR YEDADGSWSY VSPLPAWAMP PEGASGPTQV GGMDDLVEAA GEDMKIEVS
//
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