ID   S8B1M8_PENO1            Unreviewed;       843 AA.
AC   S8B1M8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EPS32723.1};
GN   ORFNames=PDE_07683 {ECO:0000313|EMBL:EPS32723.1};
OS   Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS32723.1, ECO:0000313|Proteomes:UP000019376};
RN   [1] {ECO:0000313|EMBL:EPS32723.1, ECO:0000313|Proteomes:UP000019376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX   PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA   Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA   Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT   "Genomic and secretomic analyses reveal unique features of the
RT   lignocellulolytic enzyme system of Penicillium decumbens.";
RL   PLoS ONE 8:E55185-E55185(2013).
CC   -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00037882}.
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DR   EMBL; KB644414; EPS32723.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8B1M8; -.
DR   STRING; 933388.S8B1M8; -.
DR   eggNOG; ENOG502QS9T; Eukaryota.
DR   HOGENOM; CLU_006921_0_1_1; -.
DR   OrthoDB; 1416at2759; -.
DR   PhylomeDB; S8B1M8; -.
DR   Proteomes; UP000019376; 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; IPR034660; DinB/YfiT-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.
DR   SUPFAM; SSF109854; DinB/YfiT-like putative metalloenzymes; 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:UP000019376};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          40..332
FT                   /note="Histidine-specific methyltransferase SAM-dependent"
FT                   /evidence="ECO:0000259|Pfam:PF10017"
FT   DOMAIN          371..493
FT                   /note="DinB-like"
FT                   /evidence="ECO:0000259|Pfam:PF12867"
FT   DOMAIN          554..839
FT                   /note="Sulfatase-modifying factor enzyme"
FT                   /evidence="ECO:0000259|Pfam:PF03781"
FT   REGION          687..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..711
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   843 AA;  95178 MW;  7A0B28C7DFF2B647 CRC64;
     MSPTALRNMD EVEIVNIQHE KMDVSLVDIL NKALKPPEGT PRSFPTLLLY DTRGLKIFEK
     ITYVDDYYLT NAEIEILTSQ AKRIVERLPD NAQLVELGSG NLRKIEILLR ECERVEKHVD
     YYALDLSLAE LKRTFSEISP ERFQYVGLHG LHGTYDDALL WLKDPENRTR PTVVLSMGSS
     LGNFNRSAAA NFLRDFSEAL GPSDMLLIGL DACKTPEKVY KAYNDSQGVT REFYENGLVH
     ANAVFGFEAF KPDEWEIVTE YDEENGCHRA FYSPTVDVII NDIQISKGER LLFEEAYKYS
     PDEREELCRN AHLISQTVFA NATDDYHIHL FSPCSVKIPL QPSEYASHPV PTLEDYESLW
     TVWDVVTKTM VPREELLSKP IQLRNALIFY LGHIPTFLDI HLTRALRGKL TEPKSYKEIF
     ERGIDPDVED PEKCHSHSPI PDEWPPVAEI LDYADRVRSR ARSILQDGRA LQDRSLGEAL
     WIGFEHEAMH LETFLYMLLQ SQRVQPPTGV KTPDFAKLAQ DAREAEKPNR WFSIPKQAFT
     IGLDDTDETA LPKASFGWDN EKPQRSVDVD AFEAQARPVT NGEFAKYLQV QHSRAIPASW
     KLAHTDNDFA ITNGVSESSS RATEDFMGNF AVRTVFGPVP LTVAQDWPVI ASYDELASYA
     EWAGCRLPTF EEVRSIYLYA AKLQAEPKKN DSNGHSNGAN GHSTTGHGNG AANGVKRTAD
     GVVKPNPRAD LPVYRSLEGC NVGFQNWHPV PVTPNGDRLA GQGDFGGVWE WTSTPLAPHE
     GFKAMEIYPG YTSDFFDGKH NIIQGGSWAT MPRIAGRTTF VNWYQHNYPY TWAGARLVRD
     LST
//