ID   A0A0V0UQK9_9BILA        Unreviewed;      1336 AA.
AC   A0A0V0UQK9;
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:KRX53365.1};
DE   Flags: Fragment;
GN   ORFNames=T09_6766 {ECO:0000313|EMBL:KRX53365.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX53365.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX53365.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX53365.1};
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:KRX53365.1}.
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DR   EMBL; JYDN01000204; KRX53365.1; -; Genomic_DNA.
DR   Proteomes; UP000054681; 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:UP000054681};
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        1064..1092
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1149..1172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1184..1209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1267..1286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1306..1325
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          321..346
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          728..912
FT                   /note="Cullin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50069"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX53365.1"
FT   NON_TER         1336
FT                   /evidence="ECO:0000313|EMBL:KRX53365.1"
SQ   SEQUENCE   1336 AA;  156679 MW;  28982841C20732DB CRC64;
     LVRAGRFQIP WKSEASLPGI FAFIRWKLGS KHDRCFCDAE HNLETVVPEF NNESRIEGLH
     ATWLGHASLL VKMKDGVFLT DPVLNEHHSW YGIKRIMPTP FSVSDLPKIN AVLISHNHYD
     HLDAATVGTL NERFGDSLTW FVPMGLREWF LQFQCKNVHQ LTWWEEMQFK TEEEESFTIV
     CLPAQHWSWR SPLDKNKSLW CSWAIIGRNR RFFFAGDTGY CSSFQDIGNA FGPFDLAAIP
     IGCYEPRWFM KFQHVDPEEA VQIHLDVKAR QSLGIHWGTF RMGAYEHPTE PPCKLRQVLS
     SRNLGNDSFL TLPQGGKPEF YPCNECTRAF WTEFEKEKHV LSCHTGALVW KGVRLMYPSG
     VQSNCRFIFE CELKNRILPE FFDEIEKAID EHVLAGKIIS KNILKYIDVF NRAVSVLYVN
     LKKYENGEFE LDWRSIVEEF KKQYHSLNPV KFEQLFEVLY RVWFWIYFSD QASKFSRREE
     NRRTSCLVCL EDSASCVCEE FRSKIIEANN FLIALDFRIP ELSLLCLRIA QGMVRDKIVI
     VVRRLEEYEF RGLQNIFSYL KKVVFGWLYV VMRRKVEDPF AEDLDVNTFL LRCEANLQMA
     TFEIYGRTLI SMVFQLIESF PSSYQIWMDL RYCMQRTGPC LDGDFINEVK KFVRLRILAQ
     NTTTARILIL YIKLYRALHI VFIPDSMATG IFHNIQAFLK SRCNLLSRAI ALFRRPQLMK
     YLGQELSFNP ETFPDECTNE LENKFKYPVE SLMDRPGIYP ATGKNFITAR MLIDLSGSQQ
     DFFNEYRKIL SAKLIRRFYR ACAFEYHILK SIDSSANSDY HYQCQMMIRD VFNSKAFETA
     YSEKMIRENI KLMPVHCIVA SANSWPEFAK ESLVLPDSIG EYFAKISEYF KQWKRSRILH
     LIPNLGSVHL QMRLNGLEIS IAELCEKLKA PYKEIERSLN FWFQAGVLGS KKNANWYLRP
     SSNWVSQACI GRRPCEEIGI EDEFAISEED GEDAINEYIL SLEEYWPTMR GWFQRFESLT
     PDRAYLMLKI LVRQKEMLTV DIVKRYFQMK LEQVMNDKKS DTEIALLCSV NFTIGILVVV
     INTIPFSILL VMKKFNSEIS LVFVTIQMID GVQFLIRGVR CNAISKWSYV PLVFIGECLM
     TNFEIYLRLF YHLARVCTMT LITVNCILLF LMPRVHQKLE KWNFFQILIL ILTILSVLYA
     TIICLYVWMN GSGGGKIPQF CYYEQVLPRN YRRLAFVFNF VLYNLDHHFQ KRFSDSKEKL
     SESKERIAIV CRLAVFIVIE ASLRIYPKTF FSFMLKESIN LTVPNILYWS SNILASIYSV
     IYCFINPCIK HFFKKF
//