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Database: UniProt
Entry: A0A1F3N5V2_9BACT
LinkDB: A0A1F3N5V2_9BACT
Original site: A0A1F3N5V2_9BACT 
ID   A0A1F3N5V2_9BACT        Unreviewed;       562 AA.
AC   A0A1F3N5V2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Sulfatase-modifying factor enzyme domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A2Y71_10095 {ECO:0000313|EMBL:OFY60732.1};
OS   Bacteroidetes bacterium RBG_13_42_15.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1797355 {ECO:0000313|EMBL:OFY60732.1, ECO:0000313|Proteomes:UP000178321};
RN   [1] {ECO:0000313|EMBL:OFY60732.1, ECO:0000313|Proteomes:UP000178321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OFY60732.1}.
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DR   EMBL; MEOS01000332; OFY60732.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F3N5V2; -.
DR   Proteomes; UP000178321; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.90.1580.10; paralog of FGE (formylglycine-generating enzyme); 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR002925; Dienelactn_hydro.
DR   InterPro; IPR005532; SUMF_dom.
DR   InterPro; IPR042095; SUMF_sf.
DR   PANTHER; PTHR23150:SF19; FORMYLGLYCINE-GENERATING ENZYME; 1.
DR   PANTHER; PTHR23150; SULFATASE MODIFYING FACTOR 1, 2; 1.
DR   Pfam; PF01738; DLH; 1.
DR   Pfam; PF03781; FGE-sulfatase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
PE   4: Predicted;
FT   DOMAIN          63..260
FT                   /note="Sulfatase-modifying factor enzyme"
FT                   /evidence="ECO:0000259|Pfam:PF03781"
FT   DOMAIN          379..508
FT                   /note="Dienelactone hydrolase"
FT                   /evidence="ECO:0000259|Pfam:PF01738"
SQ   SEQUENCE   562 AA;  63997 MW;  4EF3B425319D2555 CRC64;
     MVKPGFEDIL AMTSTLPGSF ITSFRSLTKD TLYRKLFTQG TIPPGMVYVE GLGIEILSNF
     CNEKHGFFID RYEVPNKQFK EFIDKGGYTN PDFWKHEFKK DGKVISREEA MKFFVDETGR
     TGPSTWIAGQ YPEGQDDFPV SGISWYEAAA YAEYAGKSLP TSAHWYSAAG NDFLNLTFVS
     KLMSISNFNN KGPESVGKYK GVTSFGAYDM AGNVREWCWN ETAVGHIIRG GAWDDASYLF
     YEMSQLPSFD RSAKNGFRCA LYIDKEKIPE RTFEIVDYSE NTDYSKVKPV DDDIFKIYNE
     RFLYDSSALD AITEETIRSY ENYTIEKITF NAAYGNDRVI AYLFLPDNSY PPFQTLIFYP
     GLNALAETNL LKSTETKWLT DYLVKNGRAV MCPVYKGTFD RINDKERAVL SGRQLTDWII
     KWVQDFSRTV DYLETRTDID KNNIGYYGSS WGGLMGGIIP AVEDRLKVNI LIVGGFAGPS
     EMVSTVSRIK IPTLMLNGKY DATFPLESSV LPFYNFLGTP EKDKNLIIYE TDHYVQRNDM
     IKEVLAWCDK YMGPVRPKSN VP
//
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