ID F0RBY5_CELLC Unreviewed; 550 AA.
AC F0RBY5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Iduronate-2-sulfatase {ECO:0000313|EMBL:ADY29619.1};
DE EC=3.1.6.13 {ECO:0000313|EMBL:ADY29619.1};
GN OrderedLocusNames=Celly_1796 {ECO:0000313|EMBL:ADY29619.1};
OS Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 /
OS NCIMB 1423 / VKM B-1433 / Cy l20).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY29619.1, ECO:0000313|Proteomes:UP000007487};
RN [1] {ECO:0000313|EMBL:ADY29619.1, ECO:0000313|Proteomes:UP000007487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 /
RC VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487};
RX PubMed=21677859; DOI=10.4056/sigs.1774329;
RA Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Mavromatis K., Ovchinikova G., Chen A.,
RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Brambilla E.M., Kannan K.P., Rohde M., Spring S., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Ivanova N.;
RT "Complete genome sequence of Cellulophaga lytica type strain (LIM- 21).";
RL Stand. Genomic Sci. 4:221-232(2011).
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; CP002534; ADY29619.1; -; Genomic_DNA.
DR RefSeq; WP_013621364.1; NC_015167.1.
DR AlphaFoldDB; F0RBY5; -.
DR STRING; 867900.Celly_1796; -.
DR KEGG; cly:Celly_1796; -.
DR eggNOG; COG3119; Bacteria.
DR HOGENOM; CLU_006332_9_0_10; -.
DR OrthoDB; 9763552at2; -.
DR Proteomes; UP000007487; Chromosome.
DR GO; GO:0004423; F:iduronate-2-sulfatase activity; IEA:UniProtKB-EC.
DR CDD; cd16030; iduronate-2-sulfatase; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR035874; IDS.
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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADY29619.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007487};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 30..400
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
SQ SEQUENCE 550 AA; 62413 MW; 91D2B9E92C3E1E1F CRC64;
MRYAQLILLL LFISSCQSQK ETKKEIKKKP NILFIAVDDL RPELGTYGSE IAITPNIDAL
ASNGLQFNNA YCQEAICSPS RASLMTGARP ESISVVENFT YFRDANPDIV TLPQQLWANG
YETVHTGKIY HGKYNDPKLS WSRKPVPHSQ MSASKKPKFG FKLPENIKLH KENSAAMVAK
YGENALRNGL GKGPAYEFAD YPDNEYEDGY NTDLAIATLK DMLNKNPNKP FFLGLGMKKP
HLDWQAPKKY WDMYNEDDIK LAQQKQGPKD GAAMGLHASF ELRARADIPK KGDITDEQAI
KLKHAYLACV SYIDAQIGRM LKALEESGQR DNTIVILWSD HGWHLGDMGI WGKATNYEIA
TRVPLIINTP NMPKEIKGKK TDALVELVDM YPTLCDLVDV AVPNTVEGQS FKPLLSNPNL
DWKKAVFSQF PTPALREWAA NPLSKGMKET SFGPLIEEVE EKIKKQQGDK WNRDLFENKL
MGYSMRTKEY RFIVWKDYKT KNAKPIFIEL YNHLNDPNET INIAKENPEI VKKLLVQFNK
GWKGNLAQLN
//
