ID A0A1G9CF54_9CLOT Unreviewed; 807 AA.
AC A0A1G9CF54;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain {ECO:0000313|EMBL:SDK50094.1};
GN ORFNames=SAMN04487833_103157 {ECO:0000313|EMBL:SDK50094.1};
OS Sarcina sp. DSM 11001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Sarcina.
OX NCBI_TaxID=1798184 {ECO:0000313|EMBL:SDK50094.1, ECO:0000313|Proteomes:UP000199127};
RN [1] {ECO:0000313|EMBL:SDK50094.1, ECO:0000313|Proteomes:UP000199127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11001 {ECO:0000313|EMBL:SDK50094.1,
RC ECO:0000313|Proteomes:UP000199127};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNFZ01000003; SDK50094.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9CF54; -.
DR STRING; 1798184.SAMN04487833_103157; -.
DR OrthoDB; 9768004at2; -.
DR Proteomes; UP000199127; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:UniProt.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.90.1580.10; paralog of FGE (formylglycine-generating enzyme); 1.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR005532; SUMF_dom.
DR InterPro; IPR042095; SUMF_sf.
DR PANTHER; PTHR39201; EXPORTED PROTEIN-RELATED; 1.
DR PANTHER; PTHR39201:SF1; FLAVODOXIN-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF03781; FGE-sulfatase; 1.
DR Pfam; PF12682; Flavodoxin_4; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000199127};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 651..807
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT REGION 258..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 807 AA; 88550 MW; 687D452A8E80F428 CRC64;
MSRLRTSNIM KRIVDAAMTV LLLCLMAYQV TGEMAHEWTG VSMAVLVIIH QILNRKWYGA
LRKGKYSLYR AVSTVLNILL LVCFALTAFC GMSMSSYAVP FLYGMAPVSF VRRMHLSMSH
WAFVLMGLHL GMHIPAMTAG LRLRTGTRTV LACIFACIGG SGLYLFLRNN MPDYLFFRVP
FAFLDYDKAG WFVFFENILM LLFWVFIGTQ AAQICRNAAQ KAAVKKNPLL PVVFIMAAVI
IGIMLQLALP SGDRAESFGN ADWNPSQAED ASGNAAGSAM QAEGASGNAE GSEMQAEDAS
GNAAGSAMQA EGASGKAEGS AQQAETAQNG ESDKTLNSTQ DKDSTRDSTR DSAKEEVLDN
KDAEKQDLKA VDDGFVLIQS GTFLMGSPET ENWRIDDETQ HEVKVSSFYI DPYETTQAEY
VRLMGENPAT FTGDDLPVEN ISWLEAVQYA NEKSVDKGLT PVYTITDKGV TWDLAAEGYR
LPTEAEWEYA CRAGTVTPFN TESSLSAEEA NFYGHYPYEI EENYFDNSAL EAKPGEYRQT
TLAVGSFEPN TWGLYDMHGN VNEWCWDHYG TYDAADAEDP TGAASGTRHI YRGGGWNDFA
KNMRSAYRAA GQEDMKSFNL GVRLVRNADD SRSGLVTAGE KSLQAETGGK ILIAYFSWSG
NTRGIAGEIQ SQTGADLFEI SPVHPYSTDY NTVLMEAQED QHKQARPELS NHVPNMDDYD
IILLGYPNWW ASIPMPIASF LEEYDFSGKT IIPFCSHGGG RFGQSLTAIA KLAPDSVLGE
GLSVHYSGGS SLSSDVAAWL KENGLTR
//