ID   A0A1V6QHJ3_9EURO        Unreviewed;       600 AA.
AC   A0A1V6QHJ3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Metallo-beta-lactamase domain-containing protein {ECO:0000259|SMART:SM00849};
GN   ORFNames=PENANT_c004G10851 {ECO:0000313|EMBL:OQD88326.1};
OS   Penicillium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD88326.1, ECO:0000313|Proteomes:UP000191672};
RN   [1] {ECO:0000313|Proteomes:UP000191672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQD88326.1}.
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DR   EMBL; MDYN01000004; OQD88326.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6QHJ3; -.
DR   OrthoDB; 5394742at2759; -.
DR   Proteomes; UP000191672; 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   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191672};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          77..297
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   600 AA;  66031 MW;  9075C00AF573D041 CRC64;
     MTDFDNASRG YIGTLEPGVI KTQAGQLAWD NSEYDFVQRG NCPESVHPKL WRQAQLCTKH
     GLFEVAPGVY QVRGFDLSNM TLAEGQKGVI IIDPLISNEC AAAAFSLYKK HRGERPLTGL
     IYSHSHVDHF GGARGVLAEG MENEIPIVAP EGFMEEATSE NIYVGTAMRR RARFMYGSSL
     PRNPEGQVGC GLGMATSQGT TSLIPPNMLI ATTGEERVID GVRIEFQIVS GTEAPSEFNF
     YFPDSKSLYI SECATHCMHN IITLRGALVR DSKAWSQGLD ESLVLFGDRA AVLFAGHHWP
     TWGQRDIARL LVEQRDMYAF MHDQTVRLMN EGLTGVEIAE KLSLPPTLDK AWHIQGYYGS
     LSHNIKAIYQ RYMTWFDGNP VNLWRHTPTE EGKRYVACMG GGDKTVALGN EYAAKGDLRF
     AATLLGHVIA AEPKHPQGRK SLSAVFTKLG HGAVNATWRN FYLTGAMDLE QDATPALPPG
     GKVPGLNPLM SVDQWLSGIS VQIDGPRAAS ENVVIDIKLT DQGQTWRLTL SNGALTYRVA
     SDDTPITGGA GLHLTATKEE MGQLLLARMK PESKAFKGDI KLFNRLLQYL PWANSLESRL
//