ID A0A061H661_9BASI Unreviewed; 580 AA.
AC A0A061H661;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=GTP cyclohydrolase II domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PFL1_06269 {ECO:0000313|EMBL:EPQ26061.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ26061.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ26061.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ26061.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family.
CC {ECO:0000256|ARBA:ARBA00008131}.
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DR EMBL; KE361647; EPQ26061.1; -; Genomic_DNA.
DR RefSeq; XP_007882001.1; XM_007883810.1.
DR AlphaFoldDB; A0A061H661; -.
DR GeneID; 19320347; -.
DR KEGG; pfp:PFL1_06269; -.
DR eggNOG; KOG1284; Eukaryota.
DR HOGENOM; CLU_029639_1_0_1; -.
DR OrthoDB; 46806at2759; -.
DR Proteomes; UP000053664; 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:UP000053664}.
FT DOMAIN 156..359
FT /note="GTP cyclohydrolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12471"
FT DOMAIN 395..532
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
FT REGION 37..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 62383 MW; 6C30AE1AED90F5A5 CRC64;
MSQDSAEVLA KILDELTELK IRNAHLEAKV DALHGAATLP SPSSHARRQS STGLSPLVQT
TTASSGSAAA ALALGSSPPP HALGPSVLQS IHGVPQTNSP TPVLTPDLGA KKTLPHQSPP
PPPPPSSSSA ASSATASAGE TTASPAYTTN GYYSSRVILT TYPGQVGIKP LPLAWGASEP
RQRGPVVASR HPNSIKVRNA IGAYGGSYSV YRSLAVAMGQ LNPNHRPDYT NTEPPFDIPP
NPSWFDRSKI VAMDPWGHLA PQLFRSEFDA GIDIRPTASL TKAHIKMPEL DTAQLAGTFP
VDGKVVVKSQ RLAGVPDDVD PGCEVNVSKA AVDPVWYLPG VADRLGVTEG ALRRAIFEDT
GGSYPELLTR HDLKVFLPPI SGLTVYIFGR PEDLRDPAKE VTVRIHDECN GSDVFGSDIC
TCRPYLLFGI EECIKTAQRG GAGAVIYFRK EGRALGEVTK YLVYNARKRG TDTAANYFRR
TEDIAGVKDM RMQALMPDVL HWLGATKIDN WISMSDMKYR AAVDSGITII NRYELPESLI
PADGRVEIDA KIEAGYFSGK KVTEADLKST IGRHWEDVDH
//
