ID A0A163K8C8_ABSGL Unreviewed; 1381 AA.
AC A0A163K8C8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN Name=ABSGL_14492.1 scaffold 14663 {ECO:0000313|EMBL:SAM08826.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM08826.1};
RN [1] {ECO:0000313|EMBL:SAM08826.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM08826.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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 -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664}.
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DR EMBL; LT554937; SAM08826.1; -; Genomic_DNA.
DR STRING; 4829.A0A163K8C8; -.
DR InParanoid; A0A163K8C8; -.
DR OMA; IKDKWDR; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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 CDD; cd06093; PX_domain; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
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; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Reference proteome {ECO:0000313|Proteomes:UP000078561}.
FT DOMAIN 706..733
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1059..1086
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 17..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1021
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1051
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1215
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1381 AA; 158222 MW; E56740A2D67E98EB CRC64;
MSNPIADTAN FFQRRSLHHS GKRSHRHSEG GLPGPAAAED AFQHDGRSTS LDHQAPSNNN
HGDSRPWNRV LSRLSHFGHH DNNVAPADST DDLNENDTTL GASHYSNGAD GPRNTFELMR
ENRWFPIHFG GRSSNDTTDH GNCNHDTDDD LLPSTCDFKH GTEDEQDQER ANYFVHPFQP
ATTDEETTIP TIVTSPPPPA EETISDHVPI SFSAPVRFSL PTDDEDTGPG ESSSSSSNDT
TSSPQPGEEE LDPAAKAHWG KTLEKIKLIS SMQQQDTPTT QLDTSATTIV ATSRTLVPYY
PPAFDPLFIA FTRDEHGHKS VSVTDSEFLD GMGQWAFRIE LQYGDVKWVI YRTIAEFVML
HYLLKFKSSL SDYVPAPPTF PNQLQSLYDS AKTTIGWDRK ETDDQDATEL PRHSLDDENE
NEKQRDALDR RIALTTYLRD LFQRAHMQIS YDVCEFLELS AISMVQDMGW KGKEGYLQHQ
INFVNHRCCQ FWTSHKWNTE WVLLRDSYVA FCETIASDRP TDVLMLDKGF TMTASEPSLF
GGYHLTLTNQ TRRIKLKGSK REMDEWWTNI KKVQSESPWV HNHRFGSFAP VRHNAKVKWF
VDAENHFNAV AEAILSAKSE IYIADWWLSP ELYLRRPPSE NEDFRLDRLL QRKAREGVMI
YIVVYKEMSL ALTIDSAHTK QWLQNLHPNI IVQRHPDHAS IDNNVLFWSH HEKIVVIDNR
LAFIGGLDLC FGRYDSHNHS LADYLPHNRD QEVFPGQDYS NPRKKDFVNV AQHDLTLVDR
SEVPRMPWHD VTLATVGPMA RDIARHFIQR WNYLKATKSM HRQNLPFLLP KGEYVAARDE
SKFKGTCRVQ ALRSSAQWSS GVEREHSIYN AYMECISQAK HFIYIENQFF ISATDQDKLL
RNKIAQALVE RIIRAHEEQE KFKVFIIIPL VPAFEGDLSS SESGSARSVM HFQYMSISRG
GNSIIERLTR AGIDPSEYID WYSLRNWGRI RPPKQQQQQE EQSTETDAEP TKLDEDDTTS
PGVKLTDNND ADADNEIDTQ DLAGGDDEEY DDPDQYVTEL LYIHDKIMIV DDKIALIGSA
NINDRSQLGN RDSEIAMIIE DTDMVDAYMD GKKYKAAKFA HTLRLQLWKE HLGLLEFDDW
ASLLHDESPH NDDGTDVETL QVSSAAYPND YDGNSDNSHD DNGHPRQQQS EHHHRRRQHH
GNRHRNKKRH RHAKRNNAQD IQNCEAEEPV QMIDRLSRTR SLYDTYKGVP TTDEQDDHLE
AQALDPLSDQ CYYNLWRKTA HDNTMLYRRL FRCVPDDTVS TYQEHRIFTG MTNANDTSGA
PLFSTAHGHV ADPLLSGQEI RHKLETVRGH LVQFPVNYLK DENMIGSSNL IDSVTPMVIF
T
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