ID F9UB70_9GAMM Unreviewed; 949 AA.
AC F9UB70;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Sulfatase {ECO:0000313|EMBL:EGV18688.1};
GN ORFNames=ThimaDRAFT_2106 {ECO:0000313|EMBL:EGV18688.1};
OS Thiocapsa marina 5811.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocapsa.
OX NCBI_TaxID=768671 {ECO:0000313|EMBL:EGV18688.1, ECO:0000313|Proteomes:UP000005459};
RN [1] {ECO:0000313|EMBL:EGV18688.1, ECO:0000313|Proteomes:UP000005459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5811 {ECO:0000313|EMBL:EGV18688.1,
RC ECO:0000313|Proteomes:UP000005459};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L.,
RA Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V., Frigaard N.-U.,
RA Bryant D., Woyke T.J.;
RT "The draft genome of Thiocapsa marina 5811.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the sulfatase family.
CC {ECO:0000256|ARBA:ARBA00008779}.
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DR EMBL; AFWV01000006; EGV18688.1; -; Genomic_DNA.
DR RefSeq; WP_007192981.1; NZ_AFWV01000006.1.
DR AlphaFoldDB; F9UB70; -.
DR STRING; 768671.ThimaDRAFT_2106; -.
DR PATRIC; fig|768671.3.peg.2235; -.
DR eggNOG; COG3119; Bacteria.
DR Proteomes; UP000005459; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 1.
DR CDD; cd16025; PAS_like; 1.
DR Gene3D; 3.30.1120.10; -; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR42693; ARYLSULFATASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42693:SF43; BLL2667 PROTEIN; 1.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR PROSITE; PS51782; LYSM; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000005459};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..949
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003394125"
FT DOMAIN 51..94
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 107..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 949 AA; 103899 MW; 4C6E415C282FE113 CRC64;
MAVNLSEPAS PPWRRLAAAL VVAVFLCSGA LQAADNGPRN HAEGAFDAAT GRYEVAKGDD
LAGIAARFGV PVADIKEANK LDSDLINIGQ ELVLSTSATA TEGAAKGALQ DSAQAPPQVT
GVLGSPSATT TISGNQLPAP QPAFGGVIKD DALQSKQWWA PRIVPPKDAP NILLILTDDA
GFGVPSTFGG VIPTPSMDRI AENGLRYNRI FSTSLCSPTR AALITGRNHH SVGFGVIAEQ
ATGFPGYNSV IGADNATIGR ILRDNGYATS WFGKNHNTPT YEASQAGPFN QWPTGMGFDY
FYGFVGGDAN QWGPNLFRNT TQIYPWIGHE GTLKMDRSDP KAAIWPVTGE EPSWNLITAM
ADDAISWMDR IHQTDPTQPI FLHYCPGASH APHHPTKEWV DKISAMHLFD DGYEKLRERI
FENQKKLGVI PPDQELTPWP KDILTPWDEL SDDAKKLFIR QAEVFAAFVA YSDYEIGRVI
QHFEDLGRLD NTLVIYQNGD NGTSAEGGPE GTFSEVAFFN GVKPPVDVQM KFYEAWGTEL
AYNHMSAGWS WAFDTPFDWF KQNASRLGGI NQNMVIQWPA RIKDKGALRE QFMHVIDHVP
TILEVTGIAA PEVVDGIKQR PIEGTSYAYT FDAENAKAPS RHTTQYFEMM GQWAIYHDGW
LMSTKVDRAP WDAFSSANPD PLNNQVFQLY DLTTSWNQSD DIAAQHPEKV TEMRAMFLAE
AKKYQVLPLD ASVGARVAAP RPSLTAGRNE YVYTSPMTGL PQGDAPYLLN TSYTVTADIT
VPEGGAEGMI VTSGGRFAGF GFYLLEGKPV FLWNLLDLER IKWEGPEALA PGKHNIEFDF
TYDGLGAETM AFNNFSGIGR SGTGTLKVDG KEVQTIKMEK TIPIILQWDE SFDVGSDTIT
GVNDADYLPP FPLTAGLDKL TIKVDRPVLS PEEIRKLEAG LQKVEAGRE
//