ID A0A5N6DXT4_ASPPA Unreviewed; 608 AA.
AC A0A5N6DXT4;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Beta-lactamase-like protein {ECO:0000313|EMBL:KAB8208920.1};
GN ORFNames=BDV34DRAFT_39351 {ECO:0000313|EMBL:KAB8208920.1};
OS Aspergillus parasiticus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=5067 {ECO:0000313|EMBL:KAB8208920.1, ECO:0000313|Proteomes:UP000326532};
RN [1] {ECO:0000313|EMBL:KAB8208920.1, ECO:0000313|Proteomes:UP000326532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117618 {ECO:0000313|EMBL:KAB8208920.1,
RC ECO:0000313|Proteomes:UP000326532};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Petersen T.I., 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., Mondo S.,
RA Pangilinan J., Riley R., Salamov A., Simmons B.A., Magnuson J.K.,
RA Henrissat B., Mortensen U.H., Larsen T.O., De vries R.P., Grigoriev I.V.,
RA Machida M., Baker S.E., Andersen M.R.;
RT "Fungal friends and foes A comparative genomics study of 23 Aspergillus
RT species from section Flavi.";
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; ML734949; KAB8208920.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N6DXT4; -.
DR VEuPathDB; FungiDB:BDV34DRAFT_39351; -.
DR OMA; YTHSHID; -.
DR Proteomes; UP000326532; 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:UP000326532};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 86..306
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 608 AA; 67510 MW; CBA58DC28AE94BF6 CRC64;
MTFSPSFSDR ADFDNATRGF IHALKPCIIR NSSGRVVWNN DEYDFLQDAE CPATAEPKLW
RQGQLNSIQG LFQVADGIYQ IRGFDLSNMT VVEGDKGVIV IDPLTSVECA AAALSLYREH
RGDRPVTGLI YSHSHVDHFG GAQGVLQPGT STSIPIIAPE GFMAEATSEN IYVGDAMRRR
AGYMYGMRLP KGPDGHIGCG LGMMPSSGTM SLIPPNVSIC HTGEERTVDG VRIEFQMVPE
TEAPAEMNFY FPEHKALCIA ECATHCLHNI ITLRGALVRD AKAWARYLDE TAVLYGQKSN
VLFGGHNWPT WGQDEIVKFI SEQRDLYTYL HDQTVRMMNL GLTGIEIAER FTLPPALQMA
WHAQGYYGSV SHNVKGIYQR YLGWFDGNPA HLWEYPAAEA GQRYIDCMGG VDEVVRKARK
YASDGDSRFA VTLLGHVIAS HPEHKESRLA LASVYTKLAY GCENATWRNF YLSGAQDMHS
PARPDRPEPP KREYRAALSV EQLLTLLSVQ LDGPKAATES FTIDLDLQEQ KESWRLILSN
GALTYRIKTD HDRSIDTSGL RLTLTKKELV EILNGGRGIR ENSSEGDVSL LFKLMRLVGA
SVPPASLL
//