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Database: UniProt
Entry: A0A1Y4D1W3_9BACT
LinkDB: A0A1Y4D1W3_9BACT
Original site: A0A1Y4D1W3_9BACT 
ID   A0A1Y4D1W3_9BACT        Unreviewed;       512 AA.
AC   A0A1Y4D1W3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Arylsulfatase {ECO:0000313|EMBL:OUO53036.1};
GN   ORFNames=B5F77_06915 {ECO:0000313|EMBL:OUO53036.1};
OS   Parabacteroides sp. An277.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=1965619 {ECO:0000313|EMBL:OUO53036.1, ECO:0000313|Proteomes:UP000196154};
RN   [1] {ECO:0000313|Proteomes:UP000196154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An277 {ECO:0000313|Proteomes:UP000196154};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC       FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC       residue in eukaryotes, is critical for catalytic activity.
CC       {ECO:0000256|PIRSR:PIRSR600917-52}.
CC   -!- SIMILARITY: Belongs to the sulfatase family.
CC       {ECO:0000256|ARBA:ARBA00008779}.
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:OUO53036.1}.
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DR   EMBL; NFJB01000013; OUO53036.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4D1W3; -.
DR   OrthoDB; 9765065at2; -.
DR   Proteomes; UP000196154; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd16145; ARS_like; 1.
DR   Gene3D; 3.30.1120.10; -; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR024607; Sulfatase_CS.
DR   InterPro; IPR000917; Sulfatase_N.
DR   PANTHER; PTHR43751:SF3; N-ACETYLGALACTOSAMINE 6-SULFATASE (GALNS); 1.
DR   PANTHER; PTHR43751; SULFATASE; 1.
DR   Pfam; PF00884; Sulfatase; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00523; SULFATASE_1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196154}.
FT   DOMAIN          35..402
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   MOD_RES         83
FT                   /note="3-oxoalanine (Ser)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600917-52"
SQ   SEQUENCE   512 AA;  57591 MW;  3EAC01EF16197C32 CRC64;
     MDTKLLVTTT GLLLAGASCA PKQPEAEKAA EVAKPNIIFI LCDDLGYGDL ACYGQPYIKT
     PNLDRLAAEG MLFTQAYAGS PVSAPSRASL MTGQHSGHGK VRGNREYWAD SGEVRYGKNK
     DYAVVGQMPY DTAHVIIPEI MKANGYTTGM FGKWAGGYEG SESTPDKRGI DEYYGYICQF
     QAHLYYPNFL NRYSKSMGDT AVVRIPMEQN MQHAMYGDDY RNRTQYSADL IHQEAMKWLD
     KQDGKQPFYG FFTYTLPHAE LVQPEDSIVK YYMAKFKADL SYPGSEGSRY NPVMHTHAQF
     AAMITRLDKY VGDIMQALDK KGLAEHTILM FSSDNGPHEE GGADPEFFGR DGKLRGLKRQ
     CYEGGIRVPF IVRWPGKVKA GTVSDHICAF YDIMPTFCDL IGEKDYVKKY SNPRLATDYF
     DGISFAPTLL GESGQQEHEF LYWEFEETDQ IGVRMGDWKM VVVKGEPRLY NLAEDLHEDH
     DIAAQHPDIV AQMKSVITTQ HVESPDFKVT LP
//
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