ID T5AF59_OPHSC Unreviewed; 571 AA.
AC T5AF59;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase {ECO:0000313|EMBL:EQL00377.1};
GN ORFNames=OCS_03910 {ECO:0000313|EMBL:EQL00377.1};
OS Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243) (Yarsagumba
OS caterpillar fungus) (Hirsutella sinensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=911162 {ECO:0000313|EMBL:EQL00377.1, ECO:0000313|Proteomes:UP000019374};
RN [1] {ECO:0000313|EMBL:EQL00377.1, ECO:0000313|Proteomes:UP000019374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Co18 / CGMCC 3.14243 {ECO:0000313|Proteomes:UP000019374};
RC TISSUE=Fruit-body {ECO:0000313|EMBL:EQL00377.1};
RX DOI=10.1007/s11434-013-5929-5;
RA Hu X., Zhang Y., Xiao G., Zheng P., Xia Y., Zhang X., St Leger R.J.,
RA Liu X., Wang C.;
RT "Genome survey uncovers the secrets of sex and lifestyle in caterpillar
RT fungus.";
RL Chin. Sci. Bull. 58:2846-2854(2013).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; KE652834; EQL00377.1; -; Genomic_DNA.
DR AlphaFoldDB; T5AF59; -.
DR eggNOG; ENOG502QSG2; Eukaryota.
DR HOGENOM; CLU_035427_0_0_1; -.
DR Proteomes; UP000019374; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF28; PROTEIN WITH D-ALANINE--D-ALANINE LIGASE C-TERMINAL DOMAIN; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000019374};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..571
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004596806"
FT DOMAIN 40..244
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 323..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 571 AA; 60266 MW; 53128C81FE3597CB CRC64;
MRLCRLAGAA SCLLGLTAAA VTQQVVRVRS PGAVNQTSAG VVLNPLPISR GSGEAIKPGT
ELRVLCAGDS ITLGTLSDTD GGDGNGYRLQ LENDLAGEVD NLPDDIIVQE FVPGTDYSVV
VIEFGTTPVA LNPTIYNYPA AHAKGQNRFL TFDIKFHEEL SESLVQRESD PVLYDLLQTL
AVEAFEVNGM AGGGWGNVDI RVRPDGSPVV IEVNPMPAIF LPERFTFEDV VIRDSLPGEH
RALLNIVLAS YLMQADEAEK DRCKFIGTAY DGVAEKYDAD YMTRSTVKQV ISDLLAEFDF
GGSVLDLACG TGVFGRMLLD KRSQRHDHPS NGASKGASNG ASNGASEGSS NGASNGASNG
ASNGASNGAS NGASNGASNG ASNEASNGAS NGASNGASNG ASNGASHGAS HGASNGASNG
ASNGKTTRLV GLDVSSEMAR LCQEHGYDEG LVGSLQVRFP AISESFDHIV CFQAIHFVSS
YEVSLVLARS FQLALKSVTI GVDEIPDEYN QAIRAKTPPW NLMTSINHVQ EVRDFGVPRG
WRLAYENRSF GWNSPASQVD VYTTVFHYER I
//
