ID A0A0B7N7X6_9FUNG Unreviewed; 1245 AA.
AC A0A0B7N7X6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN Name=PARPA_05396.1 scaffold 18169 {ECO:0000313|EMBL:CEP11530.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP11530.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP11530.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP11530.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-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|ARBA:ARBA00000798,
CC 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; LN726507; CEP11530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7N7X6; -.
DR STRING; 35722.A0A0B7N7X6; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000054107; 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 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:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 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; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00155; PLDc; 2.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 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:UP000054107}.
FT DOMAIN 283..415
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 421..526
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 653..680
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1039..1066
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 28..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..994
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1245 AA; 143661 MW; 7E3DDA3D2E0CAAB3 CRC64;
MSHPISANME YFKKHDSNQI RTSYFERGGY EQDDEHSDME GDDTEEETTA SKWHSLFRKM
SINIQRDEGT PDRDIVTGTA TNPSDHERAL MLNIPHSDGS EVFETFEDDT LPTVEQVAVD
CVNVENLPST RYFENPFESD STSTDDTMYV AATTATSNEV KPVQIHPLSN SLAANSAGDS
YGSAPEKKKV HGAMFKSSPE SFMKNDITQN ASNKAKTQWA KTFDKIKIVN SLGGSNQRRS
SSAYYTTTKQ PLAPYYPSAF SPGYLALMCR DEHGRKAPPI LFDALNVSIT DSEIDHNAVH
RLWTFRIELQ YGEIKWVINR TIIEFYNLHL TLKFKYISGF ISDPPPSFPS QLAHLTNAAL
TSMRIAREEE DSTWRDVALK RRDALETYLK ALIQGASMVV NYELCEFLEL SAISIVKDMG
WKGKEGYLEY NLNPASIRLF RWHRWQKEWL ILRDSYIAFC KDIGSTAPAD VLLFDKHLKV
VRTQSTFGSI HQTHFIISNS SRRIEVKAPT SKHIDEWIEN LDKVQKESPW IMNHRFGSYA
PVRENAKAKW FVDGHDYFEA VAQAILSAKS EIFIEDWWLS PQLYLRRPSK GNEEYRLDRL
LKRKATEGVM IYIVIYKNVS VALPLDSQHT RDWMHHVHPN IIVQRHANLT SSPFYAHHEK
ILVVDSRLAF VGGLDLCFGR YDTSKHDLTD YKSFDEREVF PGQDYSNPRI KDFYKVSQYD
MELVDKQCTA RMPWHDVHTA MVGPPARDIA RHFIQRWNFI KSNRAKERSE VPLLLPKGEY
VAARDEPKFK GTCRIQVLRS SAEWSLGITR EYSIYSAYME CIFKAKHFIY IENQFFITTT
SPHDKLIKNK IGQAIVERIK RAHQEKQKFR VIVVIPVAPG FEGDFIQVDR RSMPLRFVIK
CPVKSTEQIL NERARRSVAQ YQYRSISRGK YSVFEQLRKA NIPIKDYIGF YSLRNWGKVK
KSTPKPTPVV KDELNQVVPP PPPPPPPPPP PPIRSKRRVK SRSSSQNKSD EDFQQQVQLE
RALLEQQQYN DGRMDFVTEQ VYIHTKLMIV DDRTVICGSA NLNDRSQLGN RDSEIAVVIE
DTDMVDSRMD GRPYKASKYA LSLRMQLFKE HLGLLNVHPS NEYNVNGYRG MRREDVIVMD
PLDNEFYYDI WSKTAEKNTL VYRDVFRCVP DDTVHSVEQH RQFVPDPTRV LPGHVAEPWN
RNNEQIQAKL DDIQGHLVEF PTEYLKNISM TASVIQEAVP PIVFT
//
