ID E3L261_PUCGT Unreviewed; 551 AA.
AC E3L261;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Pseudouridine synthase I TruA alpha/beta domain-containing protein {ECO:0000259|Pfam:PF01416};
GN ORFNames=PGTG_16662 {ECO:0000313|EMBL:EFP90636.2};
OS Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS (Black stem rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP90636.2, ECO:0000313|Proteomes:UP000008783};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CRL 75-36-700-3;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA Schein J.;
RT "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT 700-3.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRL 75-36-700-3 / race SCCL
RC {ECO:0000313|Proteomes:UP000008783};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC {ECO:0000256|ARBA:ARBA00009375}.
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DR EMBL; DS178335; EFP90636.2; -; Genomic_DNA.
DR RefSeq; XP_003335055.2; XM_003335007.2.
DR AlphaFoldDB; E3L261; -.
DR SMR; E3L261; -.
DR STRING; 418459.E3L261; -.
DR EnsemblFungi; EFP90636; EFP90636; PGTG_16662.
DR GeneID; 10530536; -.
DR KEGG; pgr:PGTG_16662; -.
DR VEuPathDB; FungiDB:PGTG_16662; -.
DR eggNOG; KOG2553; Eukaryota.
DR HOGENOM; CLU_021971_0_2_1; -.
DR InParanoid; E3L261; -.
DR OrthoDB; 12038at2759; -.
DR Proteomes; UP000008783; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IBA:GO_Central.
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:UP000008783};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 252..373
FT /note="Pseudouridine synthase I TruA alpha/beta"
FT /evidence="ECO:0000259|Pfam:PF01416"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..515
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR641708-1"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR641708-2"
SQ SEQUENCE 551 AA; 63252 MW; 6A93C14457CE8B8D CRC64;
MEPTENQQQQ PQPQQQQQQH LKRKPEQEPT TIDGALSRLP KRRVAIMIGY YGRGYQGSQI
NPGTKTIEGT LFNAFVRAGC ITQDNSTHPN KVGLQRAART DANVSACCNL ISLKLILNPP
EIGQDKRMDQ HINRFLPSDM KIWEIIRVQN SFNPRSFCDS RVYEYSLPTW LFLPPKPGSP
LHQRLMKLNQ NRIKKTGEEE EDAEKEEDPE ANWWNDHSNL LEKDFKSIQA ERRGSYRISQ
MMIARIKSVL DQFRGTHNFH NLTVGKAFTE RNAVRIMKDF TVSEPFLVGG SDPTNPKDDD
DHQPLENPPT EWISITFHGQ SFMLHQIRKM IGLLVLVCRT RTPVSIIKQL YGPRKVSIPK
APGIGLILRK LNFHGYNKKI QHINEQTLQR RNKKRKGARN GGDQEDDQLM IWDSIECDRF
EALFERFKLE TLFNRIFLNQ TSQISNEPQD SNPIAGDQKV DPVELDTVKE EESGSKNSKP
TSTKPPKSSR AAHKDDDDDD EIDEKDEDDD VVPVEKLEGE DPFGVWMNYL DVYTGPDLDF
LNPDGILPDD K
//