ID A0A0B2XHS8_METRA Unreviewed; 493 AA.
AC A0A0B2XHS8;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=GTP cyclohydrolase II {ECO:0008006|Google:ProtNLM};
GN ORFNames=MAA_10967 {ECO:0000313|EMBL:KHO11451.1};
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844 {ECO:0000313|EMBL:KHO11451.1, ECO:0000313|Proteomes:UP000002498};
RN [1] {ECO:0000313|EMBL:KHO11451.1, ECO:0000313|Proteomes:UP000002498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2] {ECO:0000313|EMBL:KHO11451.1, ECO:0000313|Proteomes:UP000002498}
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:KHO11451.1}.
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DR EMBL; ADNJ02000003; KHO11451.1; -; Genomic_DNA.
DR RefSeq; XP_011411214.1; XM_011412912.1.
DR AlphaFoldDB; A0A0B2XHS8; -.
DR GeneID; 23632415; -.
DR KEGG; maj:MAA_10967; -.
DR HOGENOM; CLU_029639_1_0_1; -.
DR OrthoDB; 46806at2759; -.
DR Proteomes; UP000002498; 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}.
FT DOMAIN 82..271
FT /note="GTP cyclohydrolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12471"
FT DOMAIN 312..445
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
FT REGION 33..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 54758 MW; 7EEE0226D5070C4C CRC64;
MNPATPDPAV LDALRQIQHT QTQLLTAVES LTERVGAEES DPDGSSHTKI RSEVRGGGES
TGPNAAASAL PISSPRSPFT SRIILTTYPK QIGIDPLRMD WGNPDPTKRG PVVVSRSPST
IRRRNGLGGS YSIYYALAVA SKELDRDHRP DFTNTEPATR IGPFPQWGDP RKIVAMDPWG
HLTPWTFKNI MEEEHVDLRP TIAITKAHMK LPELEESVKA GRLVPDGKVC LNKLGELAVT
KFAVEPVWYL PGVAERFGID EATLRRSLFE HTGGSYPELI TRGDIKVFLP PIGGLTVYCF
GDPEKMSDQN VRLSLRIHDE CNGSDVFGSD ICTCRPYLIF GIEEAVKEAQ NGGSGVVIYF
RKEGRALGEV TKVLVYNARK RGEDRASDYF MRTENIAGVK DMRFQALMPD ILHWLGIQKI
DRMLSMSNMK HDAIVSQGIP ILERVELPEE LIPADSRVEI DAKITAGYFT AGKRLTAEEL
QSVQGRMWED IDH
//