ID A0A0D2IYB1_9EURO Unreviewed; 609 AA.
AC A0A0D2IYB1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Metallo-beta-lactamase domain-containing protein {ECO:0000259|SMART:SM00849};
GN ORFNames=Z518_09271 {ECO:0000313|EMBL:KIX01545.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX01545.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX01545.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX01545.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) 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; KN847481; KIX01545.1; -; Genomic_DNA.
DR RefSeq; XP_013268681.1; XM_013413227.1.
DR AlphaFoldDB; A0A0D2IYB1; -.
DR GeneID; 25297342; -.
DR VEuPathDB; FungiDB:Z518_09271; -.
DR HOGENOM; CLU_014655_1_1_1; -.
DR OrthoDB; 5394742at2759; -.
DR Proteomes; UP000053617; 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:0009058; P:biosynthetic process; IEA:UniProt.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053617};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 88..308
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 609 AA; 66976 MW; 3B7BEC1C3C06DB80 CRC64;
MASEKYSPSF ADRIAFDNAS RGLVAKLEPC LIKAPNGRVV WDNDAYDFLN AECPTTAEPK
LWRQGQLLSI QGLFKVVDGI YQIRGFDLSN MTIVEGRSGV IVIDPLISVE CAAAALAFYR
KHRGPREVTG LIYSHSHADH FGGAAGVLTG PSTAKIPILA PEGFMEEVTS ENIFAGPIMR
KRATLMYGTN LPVCPRGQIG CGLAMATSRG ANSLIPPNVL VKATGEEHII DGVKIAFQIV
PETEAPAEVN FYFPQHRALC IAECATHGMH NITTLRGALV RDAKKWSRYL DETVVLFGEI
SDVLFAGHAW PTWGTREIIQ LVSEQRDLYA YMHDQTIRMM NDGMSGIEIA ETLQLPPSLQ
QAWHAQGFYG SLSHNVKGIY QRYMTWFDGN AAHLWQYPPR EEGQRYVACM GGMDEVLRKA
DDFVQKGDTR FAVTLLGHAV AAEPSHTKAK HALASAFEAL GFGAENATWR NFYLSAAQEL
RVGKRNERAL SAMNAINPGL SVELWLAGLS VKIDGPRAAR ENFTIHLHIT DKQEKWALIM
SNGALTYRPL RTNAADNTMG LSLTLTKEEL RKVLSGNFSV ADSKAKGDMT LIRRLLSLAS
NAEGPRTSL
//
