ID A0A165NPP7_9APHY Unreviewed; 539 AA.
AC A0A165NPP7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Cyclohydrolase {ECO:0008006|Google:ProtNLM};
GN ORFNames=DAEQUDRAFT_729248 {ECO:0000313|EMBL:KZT67222.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT67222.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT67222.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT67222.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family.
CC {ECO:0000256|ARBA:ARBA00008131}.
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DR EMBL; KV429078; KZT67222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165NPP7; -.
DR STRING; 1314783.A0A165NPP7; -.
DR OrthoDB; 46806at2759; -.
DR Proteomes; UP000076727; 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:UP000076727}.
FT DOMAIN 110..317
FT /note="GTP cyclohydrolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12471"
FT DOMAIN 350..490
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
FT REGION 41..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 539 AA; 59260 MW; 2A438C2FFFFD9A20 CRC64;
MSTTQQPVSD AILTQILGQL EALQVSQQAL QAKLDALTNP PVSPVSPPGI GIPISQSHSR
EGSLSGVAPT TISLPSSVSG TQSPSTQALS IDKDKPISDR ERERLLYPGR VLLTTYPDQY
GIKPYPLQWG AADPSVRGPV ICSRFHSTIK QRNAIGAHSG SYSIYRALAI AMGTLMPSHK
PDYSQTEPSV PIPPQPAWSD PTKIVSFDPW GHVIPQVFRR ELDELGLDVR PSIAVTRGHL
KLSEIDETAR KGDITVDGKV LKKSLPLRNP DGSESTADPG VEIAINKAAV EPVWYLPGVA
ERFGISESLL RRALFEDTGG MYPELITRPD IKVFLPPIGG LTAYIFGNPT YLHDETKELT
LRVHDECNGS DVFGSDICTC KPYLIYAIEE CVRCAQRGGV GLVVYFRKEG RALGEVTKYL
VYNLRKRGGD SADKYFKATE LIAGVKDMRF QALMPDILHW FGIKKIDNMV SMSDMKYNAI
VQSGIPILKR YDIPEYLLPP DSRVEIDAKI ASGYFSNAKV VTEADLVKTV GRTWEETEH
//
