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Database: UniProt
Entry: A0A1B9GYG0_9TREE
LinkDB: A0A1B9GYG0_9TREE
Original site: A0A1B9GYG0_9TREE 
ID   A0A1B9GYG0_9TREE        Unreviewed;       584 AA.
AC   A0A1B9GYG0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Cyclohydrolase {ECO:0000313|EMBL:OCF35995.1};
GN   ORFNames=I316_02490 {ECO:0000313|EMBL:OCF35995.1};
OS   Kwoniella heveanensis BCC8398.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Kwoniella.
OX   NCBI_TaxID=1296120 {ECO:0000313|EMBL:OCF35995.1, ECO:0000313|Proteomes:UP000092666};
RN   [1] {ECO:0000313|EMBL:OCF35995.1, ECO:0000313|Proteomes:UP000092666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC8398 {ECO:0000313|EMBL:OCF35995.1,
RC   ECO:0000313|Proteomes:UP000092666};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA   Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Cryptococcus heveanensis BCC8398.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000092666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC8398 {ECO:0000313|Proteomes:UP000092666};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family.
CC       {ECO:0000256|ARBA:ARBA00008131}.
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DR   EMBL; KI669497; OCF35995.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B9GYG0; -.
DR   STRING; 1296120.A0A1B9GYG0; -.
DR   Proteomes; UP000092666; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OCF35995.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092666}.
FT   DOMAIN          164..366
FT                   /note="GTP cyclohydrolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12471"
FT   DOMAIN          399..539
FT                   /note="GTP cyclohydrolase II"
FT                   /evidence="ECO:0000259|Pfam:PF00925"
FT   REGION          32..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          4..31
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        32..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..75
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   584 AA;  63447 MW;  A809D6B8F6FB6E0D CRC64;
     MSELQQVLEL LQKLDARQEE LSKRIDNIQC SCSHSASHAH PSPSTYPHLQ TNGSSPPTSP
     TPGVEHIPCP SLPSSPPCTA SGGVEALRQS RGSFSLSAVS QSLSNAFGTS PPASGNGSST
     PYGNLSLDAA QRGAGAPGAL DPPEELKDGA KKEKKESKGL YPSRVVLTTY PSQAGIKPVP
     LNWGAGPTGR ERGPVVCSRI KSNLLIRNSI GAHSGSYSIY RALSIAMGEL RPDWRPDLTN
     THPPFALPPM DGWLGNKIVS FDPWGAMSQE IWKKEYAAGL DVRPTISQTK AHIKIEELDV
     LARKGEFPVD GEIVIKSPEL AAFPGEDRGV EINTYKAAID PVWYLPGVAE RLGIEESVLR
     RALFEDTGGM YPELLTRPDI KIFLPPVGGM TVYIIGDPAK LQDPKTEVTC RPHDSCSGSD
     VFGSDICTCR PYLIFGISEA IKCAQRGGVG VIVYLQREGR ALGEVVKYMV YNRRKRGGDT
     AAEYFNNTEK VAGVKDARHQ VLMPDVLHFL GIKRIDNLIS MSNMKYDAIV GSGIEVINRY
     EIPQELIPAD SQVEIDAKIQ SGYFSKKQVT EELVKLTKGR DWGE
//
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