ID A0A2U9B2Q2_SCOMX Unreviewed; 619 AA.
AC A0A2U9B2Q2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Putative N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D {ECO:0000313|EMBL:AWO98058.1};
GN ORFNames=SMAX5B_007829 {ECO:0000313|EMBL:AWO98058.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWO98058.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWO98058.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000256|ARBA:ARBA00004220}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004220}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004395}. Nucleus {ECO:0000256|PROSITE-
CC ProRule:PRU00376}.
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DR EMBL; CP026244; AWO98058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9B2Q2; -.
DR STRING; 52904.ENSSMAP00000000725; -.
DR Proteomes; UP000246464; Chromosome 2.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16909; YEATS_GAS41_like; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR Gene3D; 2.60.40.1970; YEATS domain; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR038704; YEAST_sf.
DR InterPro; IPR005033; YEATS.
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 Pfam; PF03366; YEATS; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR PROSITE; PS51037; YEATS; 1.
PE 4: Predicted;
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00376}; Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT DOMAIN 367..568
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
FT REGION 169..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 619 AA; 70405 MW; 7F7C894458C342A5 CRC64;
MFKKMTEFGP DSGGRVKGVT IVKPIVFGNV ARYFGKKREE DGHTHQWSVY VKPYRNEDMS
AYVKKIQFKL HESYGNPLRV VTKPPYEITE TGWGEFEIII KIFFIDPNER PVTLYHLLKL
FQSDSSAMPK KTVVSEFYDE MIFQDPTAMM QQLLTTSRQL TLGAYKHETE FSEHEQRTKE
KMETAKKRTS QEIAELKDKL KASRENINHG GGGGGGVPME KPSSSGRAAL EETTGLVEED
EVLRGAEGGV VDPRPPRKSS SSRSSRKSFR LDYRLEEEVT KSCRDKHGRW INPWSTWRFP
SHSMLLRFLL FDKNHSNVPT NKEALDSELP VMEPFFVQNP DLSDSGPGLR VTWLGHATVL
VEIDGLNILT DPIFSQRASP LQFMGPKRYR GPPCTVEQLP RIDAVVISHS HYDHLDVGSV
ASLNARFGGE LRWFVPLGLM DWLARMDCEN VMELDWWEEN CVPGHDDITF VCTPSQHWSK
RTALDDNKSL WGSWTVLGPE HRFFFAGDTG YCSSFLEIGR RFGPFDLAAI PIGAYLPRDV
MQGQHVDPAE AVQIHQDLQA KQSVAIHWGT FALAHEYYME PPVHLRDALE QKGLNPKSFF
TLHHGESRLI TSQGGDVFE
//