ID A0A1X2IDY9_9FUNG Unreviewed; 1382 AA.
AC A0A1X2IDY9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=BCR42DRAFT_417551 {ECO:0000313|EMBL:ORZ14730.1};
OS Absidia repens.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ14730.1, ECO:0000313|Proteomes:UP000193560};
RN [1] {ECO:0000313|EMBL:ORZ14730.1, ECO:0000313|Proteomes:UP000193560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ14730.1,
RC ECO:0000313|Proteomes:UP000193560};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-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 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:ORZ14730.1}.
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DR EMBL; MCGE01000014; ORZ14730.1; -; Genomic_DNA.
DR STRING; 90262.A0A1X2IDY9; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000193560; 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; 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; 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; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR Pfam; PF00787; PX; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 2.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
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:UP000193560}.
FT DOMAIN 345..482
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 726..753
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1111..1138
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1382 AA; 157483 MW; 852FF6D0620CCD4F CRC64;
MSHPLSEAAG YFAKKNEQTN RSTTSLGLVV SQQSPALSLE DQSSPNSPES RTIRRTSPSR
LEDDSNFDPK AQWQRIMNKI TSHGADDTNS QRTRFQQPTL QHKGRRTGNS SNLDNLDENI
NHGENDDEGN SDNEHHIELS FMEPRFGRPR YQQHDDDATL PTPKELEAES NNDSHITSNT
VTANNGGARK DQSNYFAHPF SPDEMSPLSP SELSIPAPTY PGLSGPSNTT QATPGSQFDY
HHNQHHYFHQ HHHPQENGEN ISTSDSETDD HGNNNLFDGR ARLHWGKTLD KIRLIANLQK
PHMSQQNADT DASTSLVPFC SALFDPPFVA LSKDIHGRRP PPIILQFLHL DITDSVLDTQ
GINQWVFRIE LQYGDVKWVI RRTIADFVSL HYTLKIKANL LDNVAAPPNF PNQLHSWINS
AKETLRRDDT GHRENDGGKE RKEIALQRRR ELTKYLRQLL TRAHIMVSYD ICEFLEISAI
SIVQDMGWKG KEGYLENRVN FVTPRFCHIF RPHLWQKEWV ILRDSFIAFC SDIGSTSPTD
VLVLDKSFRI SNNRPGILGR YHHHIILSNN FRRVEIKGNK RQVDEWVEGI AKVQEESPWV
KNHRFGSFAP IRYDSKVKWF VDAEDHYNAV AEAILSARTD IYICDWWLSP ELYLRRPPEK
NEEFRIDRLL QRKAREGVMI YVVVYKEMSL ALPINSAHTK LWLQNCHPNI IVQRHPDHRS
IDNNVLFWSH HEKIVVVDNR LAFLGGLDLC YGRYDSHAHS LVDTPAEGIP HEIFPGQDYS
NPRVKDFSNV VNFDQTLVDR KITPRMPWHD MTIGVVGPAA RDVARHFVQR WNFLKASKGM
HRSTVPFLMP KGEYVAARDE SKFKGTCRTQ ILRSSAEWSS GIEREHSIYN AYMECISKAK
HYVYIENQFF VSSTTYDKVL RNKIGQAIVE RIKKAHAKGE KFKIFIMVPL IPAFEGDLAS
SDASAARTVM HFQYISISRG GNSILEKLKE AGIDATQYIG WYCLRNWAKN KPATNANKGG
KDKRMDSGTA LGQHSDSMAT LDDKNSGHSE QPISSTPESV NSSSSPASSS SKKSPPIMAT
DAVVNDPLQN TAYLNAAENE TEDDRKYYVS ELIYIHDKLL IVDDRIVLVG SANINDRSQL
GNRDSEIAML IEDTDIVSSY MDGKKYNASK FALSLRLQLM KEHLGLLEFD DWYKLLADDD
ETVPPTMNGM TPEAEQTSTT PPIRTKSATE EEIRQYERTR PDQVLDDGSY KTMNSNNAPN
GGQKSAQYNP AISDDKRALD PLSDQFYYNI WRQTANKNTL VYRDLFRCVP DDTVTTFTQH
RQFLPSVPHG HVADPSLSEQ DIRKKLSKVQ GHLVEFPTDY LKDENMLGSY IRETVTPMVI
FT
//
