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Database: UniProt
Entry: A0A366DH49_9NOCA
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ID   A0A366DH49_9NOCA        Unreviewed;       607 AA.
AC   A0A366DH49;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Alkyl sulfatase BDS1-like metallo-beta-lactamase superfamily hydrolase {ECO:0000313|EMBL:RBO89417.1};
GN   ORFNames=DFR74_10795 {ECO:0000313|EMBL:RBO89417.1};
OS   Nocardia puris.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=208602 {ECO:0000313|EMBL:RBO89417.1, ECO:0000313|Proteomes:UP000252586};
RN   [1] {ECO:0000313|EMBL:RBO89417.1, ECO:0000313|Proteomes:UP000252586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44599 {ECO:0000313|EMBL:RBO89417.1,
RC   ECO:0000313|Proteomes:UP000252586};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Type III
CC       sulfatase family. {ECO:0000256|ARBA:ARBA00033751}.
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:RBO89417.1}.
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DR   EMBL; QNRE01000007; RBO89417.1; -; Genomic_DNA.
DR   RefSeq; WP_067507202.1; NZ_QNRE01000007.1.
DR   AlphaFoldDB; A0A366DH49; -.
DR   STRING; 1210090.GCA_001613185_02062; -.
DR   OrthoDB; 5240502at2; -.
DR   Proteomes; UP000252586; Unassembled WGS sequence.
DR   GO; GO:0018741; F:linear primary-alkylsulfatase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0018909; P:dodecyl sulfate metabolic process; IEA:InterPro.
DR   CDD; cd07710; arylsulfatase_Sdsa1-like_MBL-fold; 1.
DR   Gene3D; 1.25.40.880; Alkyl sulfatase, dimerisation domain; 1.
DR   Gene3D; 3.60.15.30; Metallo-beta-lactamase domain; 1.
DR   Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 1.
DR   InterPro; IPR038536; Alkyl/aryl-sulf_dimr_sf.
DR   InterPro; IPR029229; Alkyl_sulf_C.
DR   InterPro; IPR029228; Alkyl_sulf_dimr.
DR   InterPro; IPR044097; Bds1/SdsA1_MBL-fold.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR   PANTHER; PTHR43223; ALKYL/ARYL-SULFATASE; 1.
DR   PANTHER; PTHR43223:SF1; ALKYL_ARYL-SULFATASE BDS1; 1.
DR   Pfam; PF14864; Alkyl_sulf_C; 1.
DR   Pfam; PF14863; Alkyl_sulf_dimr; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   SUPFAM; SSF55718; SCP-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RBO89417.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252586};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          85..304
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   607 AA;  66195 MW;  2B2E80C95C1D9CF5 CRC64;
     MTANLDYGDT TDFANATRGL VARFDPPAIT AADGRVIWDV RAYDFLTGDC PPTANPSLWR
     QAQLCNEQGL FEVTEGIYQV RNLDLSNMTL VEGREGVIVI DPLISAETAA AALDLYRRHR
     GDRPVTGLIY THSHADHFGG ARGVVPEGHA PVPIVAPAGF LEHAASENVY AGNAMTRRAI
     FMYGAGLAKA PDGQIGCGLG MTTSTGTVTL IPPTLDITRT GQEEEIDGVR IVFQLTPGTE
     APAEMNFLFP DRRALCTAEN ATHNMHNVLT LRGALVRDSR VWAAYLDEAI ALFADHADVA
     FASHHWPTWG QREWTQWLAG QRDMYAYLHD QTLRLTNRGL TGPEIAEQLT LPPALDALWA
     NRGYYGSLSH NVKAVYQRYM GWFDGNPAHL WEHPPVETAR RYVADYGGIP AVIDKATEYA
     RGGDPRFAAT LLNHAVFAEP GNEGARRALA DVYDQLGHGA ENGPWRNFYL VGAAELRSGP
     TPVDIDTTDP AMMMALTVDM IIDSMAVRID GPRAADTGFV MDWHLTDENR VVRLRLSHGA
     LTHRTASPNA PLRGDPDVTL TLTKASLVAA LTGQGMDGIE VEGDEKLLST LLSLLETPDP
     RFDIVTP
//
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