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Database: UniProt
Entry: E3K1T0_PUCGT
LinkDB: E3K1T0_PUCGT
Original site: E3K1T0_PUCGT 
ID   E3K1T0_PUCGT            Unreviewed;       594 AA.
AC   E3K1T0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 2.
DT   24-JAN-2024, entry version 57.
DE   SubName: Full=GTP cyclohydrolase II {ECO:0000313|EMBL:EFP78255.2};
GN   ORFNames=PGTG_04211 {ECO:0000313|EMBL:EFP78255.2};
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:EFP78255.2, 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 GTP cyclohydrolase II family.
CC       {ECO:0000256|ARBA:ARBA00008131}.
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DR   EMBL; DS178269; EFP78255.2; -; Genomic_DNA.
DR   RefSeq; XP_003322674.2; XM_003322626.2.
DR   AlphaFoldDB; E3K1T0; -.
DR   STRING; 418459.E3K1T0; -.
DR   EnsemblFungi; EFP78255; EFP78255; PGTG_04211.
DR   GeneID; 10542047; -.
DR   KEGG; pgr:PGTG_04211; -.
DR   VEuPathDB; FungiDB:PGTG_04211; -.
DR   eggNOG; KOG1284; Eukaryota.
DR   HOGENOM; CLU_029639_1_0_1; -.
DR   InParanoid; E3K1T0; -.
DR   OrthoDB; 46806at2759; -.
DR   Proteomes; UP000008783; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:InterPro.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR   CDD; cd00641; GTP_cyclohydro2; 1.
DR   Gene3D; 3.40.50.10990; GTP cyclohydrolase II; 1.
DR   InterPro; IPR022163; GTP_CH_N.
DR   InterPro; IPR032677; GTP_cyclohydro_II.
DR   InterPro; IPR000926; RibA.
DR   InterPro; IPR036144; RibA-like_sf.
DR   PANTHER; PTHR47259; -; 1.
DR   PANTHER; PTHR47259:SF2; URACIL-REGULATED PROTEIN 1; 1.
DR   Pfam; PF12471; GTP_CH_N; 1.
DR   Pfam; PF00925; GTP_cyclohydro2; 1.
DR   SUPFAM; SSF142695; RibA-like; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008783}.
FT   DOMAIN          145..372
FT                   /note="GTP cyclohydrolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12471"
FT   DOMAIN          405..542
FT                   /note="GTP cyclohydrolase II"
FT                   /evidence="ECO:0000259|Pfam:PF00925"
FT   REGION          45..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   594 AA;  65053 MW;  6F5DF4F8A7551101 CRC64;
     MATQSETTQT TNELLQHLIA EVRCLKESQT SLELKLETLG LSFPSQYPSQ SNIKPHATGG
     SSSSPTEPQR PSSDSRPLPM PLSLSPSTSR SSSKLPKRGS AFEDEGSLRE KAKFVEWMKT
     EGALLGVDNQ SSDMVTKPVT IYPQRLILTT YPGQTGIIPI PLEWGADDPQ KRGPVVASRH
     PQSLKLRNAI GAYSGPYCIY KALATAIGAI DPNHRPDFTN TQPPFAVAPN PSWFDPSRIV
     SMDPWGHLAP QLFKSYFDSG VDIRPTVACT KAHLKLAELD ESVAQGNLLI DGKIVVKSPG
     TWAEKAAQTS VESTGGKWEA LSEEERHLLT SKRAGVEVQV TKAAVEPVWN LPGVAARFGI
     SEAILRRALF EDTGGMYPEL LTRSDLKTYL PPIGGLTVYI FGDPNFVSDP SKELTLRVHD
     ECNGSDVFGS SICTCRPYLL YGIEEAIKCA QRGGSGVIVY FRKEGRALGE VTKYLVYNAR
     KRGGDSAAFY FQRTESVAGV KDMRFQALMP DVLHWLGIKK IDVMCSMSDM KHDAIVQSGI
     PILLRKDIPD HLIPSDSRVE IDAKIAAGYF SASKVVTEED LKNTVGQSWE DVDH
//
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