ID A0A091WJJ5_OPIHO Unreviewed; 1099 AA.
AC A0A091WJJ5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=N306_05014 {ECO:0000313|EMBL:KFR15043.1};
OS Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC Opisthocomus.
OX NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR15043.1, ECO:0000313|Proteomes:UP000053605};
RN [1] {ECO:0000313|EMBL:KFR15043.1, ECO:0000313|Proteomes:UP000053605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR15043.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664, ECO:0000256|PIRNR:PIRNR009376}.
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DR EMBL; KK735627; KFR15043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091WJJ5; -.
DR STRING; 30419.A0A091WJJ5; -.
DR PhylomeDB; A0A091WJJ5; -.
DR Proteomes; UP000053605; 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; cd09842; PLDc_vPLD1_1; 1.
DR CDD; cd09844; PLDc_vPLD1_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR025202; PLD-like_dom.
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; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF57; PHOSPHOLIPASE D1; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR Pfam; PF00787; PX; 1.
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; 2.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50003; PH_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 Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Reference proteome {ECO:0000313|Proteomes:UP000053605}.
FT DOMAIN 79..222
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 229..338
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 482..509
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 917..944
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 540..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1099 AA; 125960 MW; E3F4152E87D984B0 CRC64;
MSLRDESRAA ASTLKKIAAD MSNIIESLDT RELHFEGEEV DSEVLNDPKA AVCIPFSAIY
HTRGFKEPGT QTYLTGCPIR VRVLEVERFT STKKVPSPNV YTIELTHGEF TWQVKRKFKH
FQEFHRELLR YKAFVRIPIP TRRRFRERDA GLKEEEKCYL DPLVFFPPFL VSLWESRSFR
GGMCTPADPR KQLEDYLTNI LKMPMYRNYH GTMEFLGVSQ LSFIHDLGPK GIEGLIMKRS
GGHRIPGLNC CGQGRVCYRW SKRWLVVKDS FLLYMKPDSG AIAFVLLVDK EFNIKIGQKE
TETKYGLQID NLSRSLILKC NSYRHAQWWR QGIDEFIRKH GKDFLTQHRF GSYAAVQQNT
LAKGGGARRG CGRIAVPYVN AKWYFEDVAN AMEAAKEEIF ITDWWLSPEI FMKRPVVEGN
RWRLDCILKR KAQQGVRVFV MLYKEVELAL GINSEYSKRT LMHLHPNIKV MRHPDHVSSS
VYLWAHHEKL VIVDQSVAFV GGIDLAYGRW DDDEHRLTDV GSVKRMTAVK SVSATNLASA
AESSEHVPQQ SQALSSESPV FQRNADDAPD ISKMKGVGKP KKFSRFTIYR HLHKHGMQHA
DSVSSIDSES SYSNPTRSQP NIIQSLKPHL KMFHHHTESK QGLAEPREDK GSIRSLKTGV
GELLGETRFW HGKDYCNFVF KDWVQLDKPF ADFIYRYTAP RMPWHDIASA VHGKAARDVA
RHFIQRWNFT KIMKPKYRSL SYPFLLPKSQ QTANELKYQA PEAVHATVQV IRSAADWSAG
IKYHEESIHN AYVSVIENSK HYIYIENQFF ISCADDKVVW NKIGDAIAQR ILKAHRANKR
FRVYVVIPLL PGFEGDISTG GGTALQAIMH FNYRTMCRGE NSILGQLKTE VGDKWINYIS
FCGLRTYAEL EGKLVTELIY VHSKLLIADD NTVIIGSANI NDRSMLGKRD SEIAIIVQDT
ETVPSVMDGE DYSAGKFAQS LRLRCFRVVL GGSDLNPEHK DPVCDKFFKE VWISTAARNA
TIFDKVFRCL PSDQVNNLTQ LRDFINKPKL ANDDPVKAAE ELKKIRGFLV QFPFRFLEEE
YLLPSVGTKE SMVPMEVWT
//
