ID   A0A1Y1UTG6_9TREE        Unreviewed;       615 AA.
AC   A0A1Y1UTG6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   28-JUN-2023, entry version 15.
DE   SubName: Full=GTP cyclohydrolase N terminal-domain-containing protein {ECO:0000313|EMBL:ORX40907.1};
GN   ORFNames=BD324DRAFT_612526 {ECO:0000313|EMBL:ORX40907.1};
OS   Kockovaella imperatae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cuniculitremaceae; Kockovaella.
OX   NCBI_TaxID=4999 {ECO:0000313|EMBL:ORX40907.1, ECO:0000313|Proteomes:UP000193218};
RN   [1] {ECO:0000313|EMBL:ORX40907.1, ECO:0000313|Proteomes:UP000193218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17943 {ECO:0000313|EMBL:ORX40907.1,
RC   ECO:0000313|Proteomes:UP000193218};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Louie K.B., Bewick A.J., Labutti K.,
RA   Haridas S., Kuo A., Salamov A., Ahrendt S.R., Lau R., Bowen B.P.,
RA   Lipzen A., Sullivan W., Andreopoulos W.B., Clum A., Lindquist E., Daum C.,
RA   Northen T.R., Ramamoorthy G., Schmitz R.J., Gryganskyi A., Culley D.,
RA   Magnuson J., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Widespread Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family.
CC       {ECO:0000256|ARBA:ARBA00008131}.
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:ORX40907.1}.
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DR   EMBL; NBSH01000001; ORX40907.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1UTG6; -.
DR   STRING; 4999.A0A1Y1UTG6; -.
DR   InParanoid; A0A1Y1UTG6; -.
DR   OrthoDB; 46806at2759; -.
DR   Proteomes; UP000193218; 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, ECO:0000313|EMBL:ORX40907.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193218}.
FT   DOMAIN          179..394
FT                   /note="GTP cyclohydrolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12471"
FT   DOMAIN          422..567
FT                   /note="GTP cyclohydrolase II"
FT                   /evidence="ECO:0000259|Pfam:PF00925"
FT   REGION          32..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   615 AA;  66257 MW;  67D40F664DA8E4B1 CRC64;
     MSTPELEQIL RLLQNLSKSH EELASKVDAL TARSTTSNGL AAPFSTLTAS RPSTSVTPNR
     SLAGGGIDTS APPSPILTGT DNIPCGPAAS VPGPNSTPGS PTNPADSLSH GLPSPRTGGG
     VDAFRKRASF STSPSTGFAT PRSGAANAAY GIKGMPPPGA TTPPRKDSEG KKEGLYPSRV
     VLTTYPNQAG VNPIPINWGG GPNGQDRGPV ICSRIKSNLP LRNAIGAHAG SYSIFRALSI
     AMGELRPDWR PDLRNTQPPF QLPPMPGWFG DGTGKGEEGN QKNWKIVSFD PFGAMSQEIW
     EKEYAQGLDV RPTIAQTKAH IKIEELDDLA RKGDFPVDGE VVIKSSELAA FPGVDQGVEI
     NTYKAAIDPV WFLPGIAERM GIEESTLRRT LFEDTGGMYP ELLTRPDIKI FLPPVGGMTV
     YIMGDPAKLQ DPNTEITCRP HDSCAGSDVF GSDICTCRPY LIFGLAEAIK CAQRGGVGVV
     VYFQKEGRAL GEVIKYMVYN RRKRGGDTAA EYFNNTERVA GVKDARHQEL MPDVLHWLGI
     KHITNLISMS NMKYDAIINS GITVKNRYEI PEHLIPKDGS VEIDAKIQAG YFSTKKMTGE
     ALMATKGRDW EDLVH
//