ID A0A072NZ82_9EURO Unreviewed; 382 AA.
AC A0A072NZ82;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Metallo-beta-lactamase domain-containing protein {ECO:0000259|Pfam:PF12706};
GN ORFNames=A1O9_11548 {ECO:0000313|EMBL:KEF52308.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF52308.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF52308.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF52308.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:KEF52308.1}.
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DR EMBL; AMGV01000018; KEF52308.1; -; Genomic_DNA.
DR RefSeq; XP_013254898.1; XM_013399444.1.
DR AlphaFoldDB; A0A072NZ82; -.
DR STRING; 1182545.A0A072NZ82; -.
DR GeneID; 25286446; -.
DR VEuPathDB; FungiDB:A1O9_11548; -.
DR HOGENOM; CLU_020884_2_0_1; -.
DR OrthoDB; 226459at2759; -.
DR Proteomes; UP000027920; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR024884; NAPE-PLD.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR15032; N-ACYL-PHOSPHATIDYLETHANOLAMINE-HYDROLYZING PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR15032:SF4; N-ACYL-PHOSPHATIDYLETHANOLAMINE-HYDROLYZING PHOSPHOLIPASE D; 1.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR PIRSF; PIRSF038896; NAPE-PLD; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000027920}.
FT DOMAIN 105..334
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
FT REGION 13..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153
FT /ligand="N-acyl-1,2-diacyl-sn-glycero-3-
FT phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:62537"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-50"
FT BINDING 311
FT /ligand="N-acyl-1,2-diacyl-sn-glycero-3-
FT phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:62537"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-50"
SQ SEQUENCE 382 AA; 42649 MW; 6E8415212E3D1CE0 CRC64;
MVTINSLPSL LPGEAKSHHV GNPPTGFQNP WPSFPHQSQG LMNVFKTRFS KDKPPFKPVP
DRSELVQVQK IDFAFPDPGF KVTWIGHASF LLQTSTPAGA SRGFNILCDP LFSERTSPVT
FLGPKRYNPA PCTIHELLDN VEIDLILISH NHYDHADAET LKAICAHRKS KVHILVGLHS
SRWLVGHGIS RSCITEVDWW DQFEVQVEDV GSVKITCTPS QHFSGRSPFD RNYDLWCSFG
IEELQGDQKK LFFSGDTAYR AIADPNLTHE EEESHPACPA FKQIGDLLGP FDLALLPIGL
CEPRVFMSAV HANPWDSIHI HRDVRSKKSI GMHYGTVRGG LSQYYEDVRT PPKNWKEAAD
TAGLKWGEEI GLVNIGETLV LG
//