ID A0A094DSD8_9PEZI Unreviewed; 556 AA.
AC A0A094DSD8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Sulfatase N-terminal domain-containing protein {ECO:0000259|Pfam:PF00884};
GN ORFNames=V496_01732 {ECO:0000313|EMBL:KFY67158.1};
OS Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY67158.1, ECO:0000313|Proteomes:UP000029302};
RN [1] {ECO:0000313|EMBL:KFY67158.1, ECO:0000313|Proteomes:UP000029302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:PIRSR000972-50}.
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:KFY67158.1}.
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DR EMBL; JPJY01000248; KFY67158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094DSD8; -.
DR STRING; 1420909.A0A094DSD8; -.
DR HOGENOM; CLU_006332_4_0_1; -.
DR OrthoDB; 1365192at2759; -.
DR Proteomes; UP000029302; Unassembled WGS sequence.
DR GO; GO:0004065; F:arylsulfatase activity; IEA:InterPro.
DR GO; GO:0018958; P:phenol-containing compound metabolic process; IEA:InterPro.
DR CDD; cd16147; G6S; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR012083; Arylsulfatase.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR43108; N-ACETYLGLUCOSAMINE-6-SULFATASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43108:SF8; SD21168P; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR PIRSF; PIRSF000972; Arylsulf_plant; 2.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000029302};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..556
FT /note="Sulfatase N-terminal domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001900596"
FT DOMAIN 40..349
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT MOD_RES 84
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000972-50"
SQ SEQUENCE 556 AA; 62274 MW; 6F396A36A0EEF370 CRC64;
MRQSFLFAAL LAAAVVNTTA TPNQQAINAT PLSDPETRRP NVVFILTDDQ DVHLDSLEYM
PLVRRHLIEK GTQFTKHYCT TAICCPSRVT LWTGKAAHNT NVTDVSPPYG KHGLSPTQLK
EFLLDPHTYD YMNSVFQRNK LPPVSHKGEY STDVLTQKAY GLLEEAVKAD KPFFLTLAPI
GPHSNINAQD LLTLPFGGVV FEAPIPAKRH ENLFQDVKVP RTENFNPDSP SGANWIRELG
QLNETNLEYN DHFYRSRLRA LQAVDELVEG VIAKLEEHGI LDNTYIVYSS DNGFHIGQHR
LQPGKTCGYE EDINVPLIIR GPGIAANLTT DVVSTHTDLA PTFFELLGIP LRDDFDGTPI
PLTEEAITEV KSSGTRREHV GVEYWGLAGS EGIYESGLVG PRNNTYKSIR LYGEGYNLYY
STWCSNEHEL YNLNDDPGQL HNLLFEEDGP KPTEKPLLLL GYPVSKVVAR LDTLLFVLKS
CKGQVCVNPW ETLHPEGDVH TLHDALSASF DNFYEIEQTR VSFTSCEPGY IISAEGPQFD
HDGLIFRDGL SWDQWT
//
