ID A0A0E9NCS4_SAICN Unreviewed; 395 AA.
AC A0A0E9NCS4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Metallo-beta-lactamase domain-containing protein {ECO:0000259|Pfam:PF12706};
GN ORFNames=G7K_1839-t1 {ECO:0000313|EMBL:GAO47639.1};
OS Saitoella complicata (strain BCRC 22490 / CBS 7301 / JCM 7358 / NBRC 10748
OS / NRRL Y-17804).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Taphrinomycotina incertae sedis; Saitoella.
OX NCBI_TaxID=698492 {ECO:0000313|EMBL:GAO47639.1, ECO:0000313|Proteomes:UP000033140};
RN [1] {ECO:0000313|EMBL:GAO47639.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO47639.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=21914972; DOI=10.2323/jgam.57.243;
RA Nishida H., Hamamoto M., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic yeast Saitoella complicata.";
RL J. Gen. Appl. Microbiol. 57:243-246(2011).
RN [2] {ECO:0000313|EMBL:GAO47639.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO47639.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=24646756; DOI=10.2323/jgam.60.7;
RA Nishida H., Matsumoto T., Kondo S., Hamamoto M., Yoshikawa H.;
RT "The early diverging ascomycetous budding yeast Saitoella complicata has
RT three histone deacetylases belonging to the Clr6, Hos2, and Rpd3
RT lineages.";
RL J. Gen. Appl. Microbiol. 60:7-12(2014).
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:GAO47639.1}.
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DR EMBL; BACD03000010; GAO47639.1; -; Genomic_DNA.
DR RefSeq; XP_019021051.1; XM_019165248.1.
DR AlphaFoldDB; A0A0E9NCS4; -.
DR STRING; 698492.A0A0E9NCS4; -.
DR GeneID; 30182095; -.
DR OMA; RMAPMHW; -.
DR OrthoDB; 226459at2759; -.
DR Proteomes; UP000033140; 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 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; 2.
DR PIRSF; PIRSF038896; NAPE-PLD; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000033140}.
FT DOMAIN 117..267
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
FT DOMAIN 303..355
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
FT BINDING 162
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 332
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 395 AA; 44136 MW; 8ACE932211AC73DD CRC64;
MSMAAIPLVT PAAIPSSNPE SAALKAHHPK PGSKRFENPW DSFTDHSLWD FFKSRFFYGT
EWPRHPIPTP EEGLVSVTRD IDWEGPEGER EKARAVWLGH ACFWLKFPAH GGERGLRVLF
DPVFSDRCSP FSFMGPKRYT PPPCPISAVP TPDAVVISHN HYDHLDVATI TYLRDNTSCQ
FFIPLGNKQW LLDSKIPGSR IQELDWWDEL DLSVEGVGSA RVGCLPAQHF TGRGLGDRYH
TLWASWQIRD LTGPKGANIY FAGDTGYRAV PRPTDPTDPI DSMATSKQNK EKFQSLPTCP
AFREIGNHRG PFDLALIPVG AYDPRYLMSP VHCSPEDAVE VFRDVRARKA VGMHWGAWVL
TSEEVMEPVG RLREAMRGVE GEFGVVGIGE GVDVE
//
