ID A0A5N6HW53_9EURO Unreviewed; 626 AA.
AC A0A5N6HW53; A0A5N7D9C0;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Beta-lactamase-like protein {ECO:0000313|EMBL:KAE8402904.1};
GN ORFNames=BDV37DRAFT_294906 {ECO:0000313|EMBL:KAE8402904.1};
OS Aspergillus pseudonomiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1506151 {ECO:0000313|EMBL:KAE8402904.1, ECO:0000313|Proteomes:UP000325579};
RN [1] {ECO:0000313|EMBL:KAE8402904.1, ECO:0000313|Proteomes:UP000325579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119388 {ECO:0000313|EMBL:KAE8402904.1,
RC ECO:0000313|Proteomes:UP000325579};
RG DOE Joint Genome Institute;
RA Mondo S., Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Riley R.,
RA Salamov A., Simmons B.A., Magnuson J.K., Henrissat B., Mortensen U.H.,
RA Larsen T.O., Devries R.P., Grigoriev I.V., Machida M., Baker S.E.,
RA Andersen M.R., Cantor M.N., Hua S.X.;
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Type III
CC sulfatase family. {ECO:0000256|ARBA:ARBA00033751}.
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DR EMBL; ML736782; KAE8402904.1; -; Genomic_DNA.
DR OrthoDB; 5394742at2759; -.
DR Proteomes; UP000325579; 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:UP000325579};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 626 AA; 69596 MW; 3B6D11EB272DDE58 CRC64;
MSSTSYPPED PTDSANASRG LITSLEPCVV YSDTNPTRAI WDNDSFGFLS EEHAPQFANP
SLWRQSQLCH KQGLFKVRDG IYQVRGLDLS NITFIECPNT KGVAVIDPLT CIETAKKALG
LYQAQFPDRV IKALIYTHSH VDHFGGAKAI ADAAAEGLKV YAPHGFLEHA VSENVYSGNA
MGRRAVYMYG ESLPRQRDGQ IGCGLGLTVS MGVSGLIPPT TSINQTGEEI IVDDDLEIEC
QLTPGTEAPA EMNMYFPQYN ALCMAENATH TLHNIQTLRG ALVRDARVWA KYLDEAIVRY
GKDADVVFSS HHWPTWDNVN VNDFLTKQRD LYAYLHNETL RLLNMGQTGI EIAEKFHLPP
SLNNTWSARG YYGSISHNVK AIYNRYMGWF DGNPAHLWEH PPVESATRYV KCMGGIEKVI
DLGKEFADEG DLRFAATLLN HAVYADQNND RARNELASVY RKLGYGAENG VWRNFYLTGA
RELEPRNKPQ GSQLSMSAEL LMALDLEQLF DTFAMRVEGP KAWDRSFTID FMIADMHRGW
HLNLSNGALT GHEIEYREPR DATGSSLVIW LTHKDLVALA ARDRKNLDGL TTTGDVKCWA
TLASLLTAPD PAFAIVTPSA IYSSSA
//
