ID A0A0G2I2J5_9EURO Unreviewed; 612 AA.
AC A0A0G2I2J5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Choline-sulfatase {ECO:0000313|EMBL:KKZ64385.1};
GN ORFNames=EMCG_09642 {ECO:0000313|EMBL:KKZ64385.1};
OS Emmonsia crescens UAMH 3008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=1247875 {ECO:0000313|EMBL:KKZ64385.1, ECO:0000313|Proteomes:UP000034164};
RN [1] {ECO:0000313|Proteomes:UP000034164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 3008 {ECO:0000313|Proteomes:UP000034164};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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:KKZ64385.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCZI01000800; KKZ64385.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2I2J5; -.
DR VEuPathDB; FungiDB:EMCG_09642; -.
DR Proteomes; UP000034164; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd16032; choline-sulfatase; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR017785; Choline-sulfatase.
DR InterPro; IPR025863; Choline_sulf_C_dom.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR NCBIfam; TIGR03417; chol_sulfatase; 1.
DR PANTHER; PTHR45953; IDURONATE 2-SULFATASE; 1.
DR PANTHER; PTHR45953:SF1; IDURONATE 2-SULFATASE; 1.
DR Pfam; PF12411; Choline_sulf_C; 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}.
FT DOMAIN 7..350
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT DOMAIN 544..597
FT /note="Choline sulfatase enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12411"
FT REGION 450..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 68454 MW; FA69B10177CE1F70 CRC64;
MADVKKPNIL YIMADQMAAP LLSLYDKNSP IKTPNLDRLA REGVTFESAY CNSPLCAPSR
FTMVTGQLPS KVGGYDNASD LAADTPTYAH YLRKEGYHTA LAGKMHFAGP DQLHGYEQRL
TSDIYPGDYG WTVNWDEPEI RPDWYHDMSS VMEAGPCVRT NQLDYDDEVI YKATQYLYDH
TRHRNEQPFC LTVSMTHPHD PYAMTKEYWD LYEDVEIPLP KTSALPHNKQ DPHSQRVLKC
IDLFGKEIPE DRIVAARRAY FAACSYVDAQ VGKLMATLKA CDLADNTIVV FTGDHGDMLG
ERGLWYKMVW YEHAARVPMF VHAPGRYRPK RVKENVSTMD LLPTFVAMTG GEMNVDLPID
GVSLMPYILD DNSPEAISGM KTDTVIGEYM AEGTLAPVVM IRRGPWKFVY SPIDPPMLYN
IENDPTELVN LAAGIEMPTR PQLTRNEHLT TTTTTKQQQE IFFPTDPAAP PTPDISPPPG
TLNSSFFCDK ANSAQIPTPP RTPSPNKAPS CTSTSTPQID VQSLLSAFIS EAHSRWDFQA
LQSQVLHSQR RRRLVYSALV KGQLASWDYS PVTDGSAQFI RNHGKGALGD VELLSRYPRA
IQWGGNGGRS GV
//
