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Database: UniProt
Entry: L5LVT1_MYODS
LinkDB: L5LVT1_MYODS
Original site: L5LVT1_MYODS 
ID   L5LVT1_MYODS            Unreviewed;       249 AA.
AC   L5LVT1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Steryl-sulfatase {ECO:0000313|EMBL:ELK30206.1};
GN   ORFNames=MDA_GLEAN10014567 {ECO:0000313|EMBL:ELK30206.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK30206.1, ECO:0000313|Proteomes:UP000010556};
RN   [1] {ECO:0000313|Proteomes:UP000010556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SIMILARITY: Belongs to the sulfatase family.
CC       {ECO:0000256|ARBA:ARBA00008779}.
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DR   EMBL; KB107233; ELK30206.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5LVT1; -.
DR   eggNOG; KOG3867; Eukaryota.
DR   Proteomes; UP000010556; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR024607; Sulfatase_CS.
DR   InterPro; IPR000917; Sulfatase_N.
DR   PANTHER; PTHR42693; ARYLSULFATASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR42693:SF9; STERYL-SULFATASE; 1.
DR   Pfam; PF00884; Sulfatase; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 2.
DR   PROSITE; PS00523; SULFATASE_1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..249
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003970707"
FT   DOMAIN          87..179
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   REGION          228..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   249 AA;  27370 MW;  659D17C073CE070E CRC64;
     MRRLLLLLLL LWEAQSRAPS RPNFVLIVAD DLGIGDPGCY GNKTLRTPNI DRLAEEGVKL
     TQHLAASPLC TPSRAAFMTG RYPVRSGQLL NVLEELQLTN KTLVYFTSDQ GAHVEEVTAK
     GERHGGSNGI FKGGKGNNWE GGIRVPGLLR WPGVLPAGLE IAEPTSNMDI FPTVAKLAGS
     QLPEDRIIDG RDLMPLLQGE TQRSDHEFLF HYCNFYLNAV RWHPPNSESQ LPGRLRLPGG
     SALQRSVDG
//
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