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Database: UniProt
Entry: A0A1Y4HDW6_9BACT
LinkDB: A0A1Y4HDW6_9BACT
Original site: A0A1Y4HDW6_9BACT 
ID   A0A1Y4HDW6_9BACT        Unreviewed;       513 AA.
AC   A0A1Y4HDW6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Arylsulfatase {ECO:0000313|EMBL:OUP06153.1};
GN   ORFNames=B5F34_14880 {ECO:0000313|EMBL:OUP06153.1};
OS   Mediterranea sp. An20.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Mediterranea.
OX   NCBI_TaxID=1965586 {ECO:0000313|EMBL:OUP06153.1, ECO:0000313|Proteomes:UP000196631};
RN   [1] {ECO:0000313|Proteomes:UP000196631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An20 {ECO:0000313|Proteomes:UP000196631};
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:OUP06153.1}.
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DR   EMBL; NFJV01000033; OUP06153.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4HDW6; -.
DR   OrthoDB; 9762324at2; -.
DR   Proteomes; UP000196631; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; PTHR45953; IDURONATE 2-SULFATASE; 1.
DR   PANTHER; PTHR45953:SF1; IDURONATE 2-SULFATASE; 1.
DR   Pfam; PF00884; Sulfatase; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   PROSITE; PS00523; SULFATASE_1; 1.
DR   PROSITE; PS00149; SULFATASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196631}.
FT   DOMAIN          29..381
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   MOD_RES         77
FT                   /note="3-oxoalanine (Ser)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600917-52"
SQ   SEQUENCE   513 AA;  58271 MW;  A8155F251CFC6DF1 CRC64;
     MKNISIVAPM TVMAAGGLLP AQMQAQQKPH IILIMSDQHR WDAMNCMGNE TVITPHMDAL
     AAEGTLFTNG YSSTPSSTPA RSGLLTGLSP WHHGMLGYGR VGLHYRYEMP QMLRDLGYYT
     FGIGKMHWFP QKALHGFHGT LVDESGRVES PDFISDYRLW FQMQAPGLNP DSTHIGWNDH
     GAADYRLPER LHPTAWTGET ACEMIHNYRN GNGQPLFLKV SFARPHSPYD PPKRFSDLYR
     NREIPAPFVG EWCKDKDYAT LKDASQAPSD AAYGNFGEEY ALNSRRHYYA NVTFIDEEIG
     KIVQALKDEG MYDNALIIYV SDHGDMLGDH YHWRKTYPYE GSTHVPYIVK WPASLGFTPG
     GKVDAPVELR DLLPTFLEVA GGTVPADMDG QSLLCLLDGR KDTWRQYIDL EHATCYSADN
     YWCALTDGKM KYVWRFHTGE EELFDLEADP HELHNVASES AYRQRLQEFR QAMVRHLSER
     GDEYVKDGKL QILKRTILYS PNFPDKNPTD TGI
//
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