ID A0A016W1Y7_9BILA Unreviewed; 1317 AA.
AC A0A016W1Y7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN Name=Acey_s0001.g14 {ECO:0000313|EMBL:EYC33879.1};
GN Synonyms=Acey-pld-1 {ECO:0000313|EMBL:EYC33879.1};
GN ORFNames=Y032_0001g14 {ECO:0000313|EMBL:EYC33879.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC33879.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000798,
CC ECO:0000256|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664, ECO:0000256|PIRNR:PIRNR009376}.
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:EYC33879.1}.
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DR EMBL; JARK01001337; EYC33879.1; -; Genomic_DNA.
DR STRING; 53326.A0A016W1Y7; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR CDD; cd01254; PH_PLD; 1.
DR CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 2.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00155; PLDc; 2.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 3.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50035; PLD; 2.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635}.
FT DOMAIN 82..304
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 553..580
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1126..1153
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1317 AA; 150616 MW; 5BD0F27A85D43BD0 CRC64;
MMNGKQVTVD EHYEQADTYN LEDEDDYSTD DEIQYCDCIA SALAQTLPGM PGKKGIIPYD
SVFDTQTQAR RRGYWIPGVP VNAKIVSVER NTDRRIHLIN TLLYTIQLEH GQFKWSVVRN
YKDFTLLNNR LKAHRAAQQI LAPVRRAQER VDSMLESVGI DVIPDHKEDC PYYRHPTKRR
HSKLPVLKRD SNAFDVVKSA PLASSEATTS PSSEEARVKM EEAVQSGILQ DDDATTSPTG
TKKRKLRTRK KHGLPRFPMM PDSMVTNSEL RKDQLEHWLQ MLLHIPINRN HHETAEFLEV
SRFSFVNELG GKHTEGFVKK RPGGARVYLG WKQCCVRYML PWSKRWLMVR DSFIAYMDHR
TEQIRLVLLM DRDFKVAAGG KEAEGIPTGL IITNTQHELH LKCRRIQDTA RWKAIIEQAM
HGIGSIWIQP HRFSSSFPVR ENCYGKWFVD ARTYMAHAAD MMELAREEIF IAGWWLSPEI
YMKRPALEGN YWRLDEILKR KANQGVRIFI LMYKEMEMAL GLNSMYSKRT LQALHPNVKV
MRHPDHYPST GTFFWAHHEK LVIVDQLIAF VGGVDLCFGR WDDNHHLLTD LGSVQFGQQH
LITQDISMTT GLRALVKAPL TLSPLGLEEN ENVVCDKIEE GVEVPRDEEN KERRRQVTKI
AVGSVEEVNC SDFLDNAGSD GEVIFADTDT GGVMLKVFKK GTRSVSADSP RRTPTSEQPS
PSPTNTASKI AAVSGKKPTL LNVVEDAKGK KHVRRAASAA ARSRVPLDML DKAGPAPSMF
EKATKMGMDF QTAAEKYKEY VESGAVQKEK HRSQTPPMKR RESRLSRAVG NWRSNRAKRK
WKQVLDSDEV MAGYELDFLR LKQMDTDDKD SIDGGVKLWV GKDYVNYIHK DFVEVDLPFH
DFIDRGATPR MPWHDIHSVT FGAPARDVAR HFIQRWNATK TEKLKDDNNY PYLLPKSHEN
LKVPRVFRSS NFSYNVNIQV LRSLSNWSGL INQTEDSIQM AYLSLIANSK HYIYIENQFF
VSMIDSNDVL NEICKVICNR VIRAYKEKQP FRVYIMIPLM PGFEGNVGAP GGSSLQAVLH
WTYQSLSRGP NSLFERLKAV VPNPHEYISV SSLRTYDTLC GKLVTELIYI HCKLLIVDDE
HVIIGSANIN DRSQVGNRDS EVCLLYTDVQ KERSIMNGRP YEAGKFAKSL RLQCMKEHLG
LLPDARRPSK FKYEVSCDDP VAESFFVDVW QNTAHSNMLI YEEVFRTYPT DNVETFEEFE
KWTGQMPLAE YSPQQAQEKL RDLNGTLVEF PLNFLCKANL TPGITSKEGL VPNAVFT
//
