ID T0K6Z4_COLGC Unreviewed; 902 AA.
AC T0K6Z4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Ergothioneine biosynthesis protein 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CGLO_13076 {ECO:0000313|EMBL:EQB47754.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB47754.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00037882}.
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:EQB47754.1}.
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DR EMBL; AMYD01002835; EQB47754.1; -; Genomic_DNA.
DR AlphaFoldDB; T0K6Z4; -.
DR STRING; 1237896.T0K6Z4; -.
DR eggNOG; ENOG502QS9T; Eukaryota.
DR HOGENOM; CLU_006921_0_1_1; -.
DR OMA; FKHWHPT; -.
DR OrthoDB; 1416at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1580.10; paralog of FGE (formylglycine-generating enzyme); 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR024775; DinB-like.
DR InterPro; IPR019257; MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR017805; SAM_MeTrfase_EasF-type_put.
DR InterPro; IPR005532; SUMF_dom.
DR InterPro; IPR042095; SUMF_sf.
DR NCBIfam; TIGR03439; methyl_EasF; 1.
DR PANTHER; PTHR43397; ERGOTHIONEINE BIOSYNTHESIS PROTEIN 1; 1.
DR PANTHER; PTHR43397:SF1; ERGOTHIONEINE BIOSYNTHESIS PROTEIN 1; 1.
DR Pfam; PF12867; DinB_2; 1.
DR Pfam; PF03781; FGE-sulfatase; 1.
DR Pfam; PF10017; Methyltransf_33; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 58..343
FT /note="Histidine-specific methyltransferase SAM-dependent"
FT /evidence="ECO:0000259|Pfam:PF10017"
FT DOMAIN 377..511
FT /note="DinB-like"
FT /evidence="ECO:0000259|Pfam:PF12867"
FT DOMAIN 803..899
FT /note="Sulfatase-modifying factor enzyme"
FT /evidence="ECO:0000259|Pfam:PF03781"
FT REGION 622..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 902 AA; 101505 MW; 391E96D52E87E891 CRC64;
MGSIAVSQDS LPYAGPKAAK QKAVKSVEKH GVDIIDVRRV AVETNLKDDI LSMWNPTNGP
RRLPTLLLYN ERGLQLFEDI TYLEEYYLTN NEIEVLNRSS REIAQNISPE SMVIELGSGN
LRKIGILLQA FEDAGKKIDY YALDLSREEL ERTLAQLPEF RHVRCHGLLG TYDDGREWLK
KPFNLARPKC IVSLGSSIGN FERYDAAGFL KHFSDVLAPS DKMLIGLDGC GDPAKVYHAY
NDKHGITHDF ILNGLTNANE ILGQEAFKLK DWEVIGEYVY DDEGGRHQAF FSPVRDTYVL
GTLIRQHERI QVEQSLKYSQ RGAENLWSMA GLVETGRWTK GDEHGLHMIS KRKMPFSLLP
DLYASSPCPS LSDWEALWTA WDAVTQSMLP REELLDKPIK LRNACIFYLG HIPGFLDIQL
TKTTKRPATE PAHFQPMFER GIDPDVDNPE KCHSHSEIPD EWPAVEEIIE YQRSVRSRLR
SLYKDGIDKI PRPIAQGIWV GFEHEIMHME TLLYMMIQSD KTLPPPDIER PDFKRLAQKA
HQARVANQWH DVPAQSIKVG MDEPALDAGI NGYFGWDNER PSRRVDVHSF QAKGRPITNE
EYAQYMFDNH IEQVPASWAD VHASESETET NGHTNGFGNG HSNGHTNGHT NGHANGHANG
HTNGHVNGNT NGAKNGVNGV NGHRNVSLPD SFLEGMAVRT VYGLVPLKYA LDWPIFASYD
ELSGCAAWMG GRMPSFEEAR SIYTYVHNLK KMEAERTLGR TVPAVNGHLS NDGVEETPPK
LASLEAEKAR SELFMDLDGA NVGFQHWHPV PVTANGGRLA GQGELGGVWE WTSTPLARHE
GFEPMPLYPQ YTADFFDGKH NIVLGGSWAT HPIIAGRRSF VNWYQRNYPY AWAGARIVRD
IK
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