ID A0A0V0W9Q3_9BILA Unreviewed; 1405 AA.
AC A0A0V0W9Q3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE SubName: Full=N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D {ECO:0000313|EMBL:KRX72375.1};
DE Flags: Fragment;
GN Name=NAPEPLD {ECO:0000313|EMBL:KRX72375.1};
GN ORFNames=T06_14539 {ECO:0000313|EMBL:KRX72375.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX72375.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX72375.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX72375.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000256|PROSITE-
CC ProRule:PRU00330, ECO:0000256|RuleBase:RU003829}.
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:KRX72375.1}.
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DR EMBL; JYDK01000208; KRX72375.1; -; Genomic_DNA.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15032; N-ACYL-PHOSPHATIDYLETHANOLAMINE-HYDROLYZING PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR15032:SF4; N-ACYL-PHOSPHATIDYLETHANOLAMINE-HYDROLYZING PHOSPHOLIPASE D; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR SUPFAM; SSF75632; Cullin homology domain; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT TRANSMEM 1123..1151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1158..1175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1208..1231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1243..1267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1293..1314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1335..1355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1375..1394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 336..361
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 743..979
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX72375.1"
FT NON_TER 1405
FT /evidence="ECO:0000313|EMBL:KRX72375.1"
SQ SEQUENCE 1405 AA; 164819 MW; E61F1884F33A970F CRC64;
LFYDVKKWSP LVRAGRFQIP WKSEASLPGI FAFIKWKLGS KHDRCFCDAE HNLETVVPEF
NNESRIEGLH ATWLGHASLL VKMKDGVFLT DPVLNEHHSW YGIKRIMPTP FSVSDLPKIN
AVLISHNHYD HLDAATVGTL NERFGDSLTW FVPMGLREWF LQFQCKNVHQ LTWWEEMQFK
TEEEESFTIV CLPAQHWSWR SPLDKNKSLW CSWAIIGRNR RFFFAGDTDI GNAFGPFDLA
AIPIGCYEPR WFMKFQHVDP EEAVQIHLDV KARQSLGIHW GTFRMGAYEH PTEPPCKLRQ
VLSSRNLGND SFLTLPQGGK MNLLFQYEKI AEPEFYPCNE CTRAFWTEFE KEKHVLSCHT
GALVWKGVRL MYPSGVQSNC RFIFECELKN RILPEFFDEI EKAIDEHVLA GKIISKNILK
YIDVFNRAVS VLYVNLKKYE NGEFELDWRS IVEEFKKQYH SLNPVKFEQL FEVLYRVWFW
IYFSDQASKF SRREENRRTS CLVCLEDSAS CVCEEFRSKI IEANNFLIAL DFRIPELSLL
CLRIAQGMVR DKIVIVVRRL EEYEFRGLQN IFSYLKKVVF GWLYVVMRRK VEDPFAEDLD
VNTFLLRCEA NLQMATFEIY GRTLISMVFQ LIESFPSSYQ IWMDLRYCMQ RTGPCLDGDF
INEVKKFVRL RILAQNTTTA RILILYIKLY RALHIVFIPD SMATGIFHNI QAFLKSRCNL
LSRAIALFRR PQLMKYLGQE LSFNPETFPD ECTNELENKF KYPVESLMDR PGIYPATGKN
FITARMLIDL SGSQQDFFNE YRKILSAKLI RRFYRACAFE YHILKSIDSS ANSDYHYQCQ
MMIRDVFNSK TFETAYSEKM IRENIKLMPV HCIVASANSW PEFAKESLVL PDSIGEYFAK
ISEYFKQWKR SRILHLIPNL GSVHLQMRLN GREMQYIVEP CCACIILQFA NNIEISIAEL
CEKLKAPYKE IERSLIFWFQ AGVLGSKKNA NWYLRPSSNW VSQACIGRRP CEEIGIEDEF
AISEEDGEDA INEYILSLEE YWPTMRGWFQ RFESLTPDRA YLMLKILVRQ KEMLTVDIVK
RYFQMKLEQG ALISDNGASE NQNLFLNQCF CEVMNDKKSD TEIALLCSVN FTIGILVVVI
NTIPFSILLV MKKFNSEISL VFVTIQMIDG VQFMIRGVRC NTISKWSYVP LVFIGECLMT
NFEIYLRLFY HLARVCTMTL ITVNCILLFL MPRVHQKLEK WNFFQILILI LTILSVLYAT
IICLYVWMNG SGGGKIPQFC YYEQVLPRNY RRLAFVFNFV LYNLDVFFII FIILKHHFQK
RFSDSKEKLS ESKERIAIVC RLAVFIVIEA SLRIYPKTFF SFMLKESISL TVPNILYWSS
NILASIYSVI YCFINPCIKH FFKKF
//
