ID A0A2G8SSD9_9APHY Unreviewed; 630 AA.
AC A0A2G8SSD9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Sulfatase-modifying factor enzyme domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=GSI_00177 {ECO:0000313|EMBL:PIL36488.1};
OS Ganoderma sinense ZZ0214-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL36488.1, ECO:0000313|Proteomes:UP000230002};
RN [1] {ECO:0000313|EMBL:PIL36488.1, ECO:0000313|Proteomes:UP000230002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL36488.1,
RC ECO:0000313|Proteomes:UP000230002};
RX PubMed=26046933; DOI=10.1038/srep11087;
RA Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA Li X., Schwartz D.C., Wang Y., Chen S.;
RT "Chromosome-level genome map provides insights into diverse defense
RT mechanisms in the medicinal fungus Ganoderma sinense.";
RL Sci. Rep. 5:11087-11087(2015).
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:PIL36488.1}.
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DR EMBL; AYKW01000001; PIL36488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8SSD9; -.
DR STRING; 1077348.A0A2G8SSD9; -.
DR OrthoDB; 1416at2759; -.
DR Proteomes; UP000230002; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1580.10; paralog of FGE (formylglycine-generating enzyme); 1.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR024775; DinB-like.
DR InterPro; IPR005532; SUMF_dom.
DR InterPro; IPR042095; SUMF_sf.
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 SUPFAM; SSF56436; C-type lectin-like; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000230002}.
FT DOMAIN 193..337
FT /note="DinB-like"
FT /evidence="ECO:0000259|Pfam:PF12867"
FT DOMAIN 410..627
FT /note="Sulfatase-modifying factor enzyme"
FT /evidence="ECO:0000259|Pfam:PF03781"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 68778 MW; D55ACF5C76BBFED0 CRC64;
MRSSSPTSSS DSYSPAVSTA PSTPPPGLAA SFCLILHDAS PAFLAALPVS KSSSDRVLLC
RGAGPVKPLL SAAADLLGEK AILDDARWER VCAKDNDSEI TYYTSKESIS SIDEKPAVVL
DAISCDSTPA SHAAMLNLFS EAGLRSVVAF PSPAASLYVL ERPALTFPLL SSTPSSALNP
TANPYTMPSL DEFERGWAIW DLITSNMIPA ELLHSKPIDL RHKPLFYIGH LPTFANILLS
RLIKATPVGP RSYLTTFERG IDPSVDDPDH CHSHSEVPEK DEDWPVIEDV LAYRDEVRGR
VIKRILGELE SGERKLTRRL ARTLMMVHEH DGFHIETLLY MLIQRAGTGM LPPPGFASPP
WAALAAQWDA TPAPSTPTVT LGPCTVTMGH DDQEPDDVLP ALQHDVAAHE FGWDNESPPR
AVEVGAFRVD WRPITNGEFE AFWRGAGKGV VDMPASWVLD EDEDEDGSGV QVRTLYGPVP
MAYARHWPVL TAYDDLAAYA AHKGGRIPTE AELRLFLDTY QVGYEQGANT GFRHWHPLPA
TAGLEDVDGG RGSNGGVWEW TATALDAHPG FEGTGIFPGY SSDFFDGKHQ VVLGASYATI
PRLGDRRTVR NFYQHNYPYP WVGARVAYDV
//
