ID A0A0B7N5K6_9FUNG Unreviewed; 784 AA.
AC A0A0B7N5K6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN Name=PARPA_04488.1 scaffold 14269 {ECO:0000313|EMBL:CEP10723.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP10723.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP10723.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP10723.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LN725192; CEP10723.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7N5K6; -.
DR STRING; 35722.A0A0B7N5K6; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000054107; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
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; 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 InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF186; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 3.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 4: Predicted;
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:UP000054107}.
FT DOMAIN 161..188
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 570..597
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 492..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 784 AA; 90291 MW; A4DB6D58E1534CCC CRC64;
MSFFTTLIEQ VKDVFEAASD NTPEDQDDDL LEQKLMNEKH RYDSFAAVRH DASVKFYIDG
QNYCWAVSEA IENAEECIYI EDWWLTPELY LRRPPSKYPD YRLDRLLKKK ADAGVKIYVV
VYKEVEMALT LDSRHTKDSL QALSENIIVL RHPDHNIQGT FFWSHHEKFV VVDNKIAFLG
GIDLCFGRWD THGHPLADFS GSDPESELFP GQDYSDARQG APVLDVARHF CERWNFIKHE
KAKNKDNIPF LQPPLGGMGQ QQRYIEEEPE EHHYRRQRHK HRTRGVTGTM RAQVLRSSAK
WSSGVELEHS IQNAYISTIL AAQHYVYIEN QFFISATDDK EKNIIKNQIG NAILQRIIRA
HEEKEKFKVF VLMPLMPAFP ADLSTKDAAT ARLVMHYQYI SICRGSDSIV EKLKANGIDP
DQYIRFYSLR SYDRINRSQL EELLLQQAGY SNTTQQQLDN AGGQEGSRIG IVHRAGDQDF
ARGTRGEFSV EEEVEYGRVR DDEEVERRRN RYNQDREDGD YDEGIASDSI AKDAMLHGDV
ESEPWVNDTK EEQPRDAEAA AEEASDYVTE ELYIHAKLLI ADDKVVIMGS SNLNDRSQCG
DRDSEIALIV EDKDTIPSQM NGKYYEASRF AATLRRNLWK EHLGLLPHTK PDKVTKAMLP
LPVPQIDDTS SKEDQLVMDP LDEETLERWN STAKTNTEAF REVFHCVPDD TVTNWEEYKA
FYPDPSEIDI GHVHDPEMSV DEIRDHLGNI HGHLVEFPYH FLEGVDLQGE SIPFVGDDIQ
ELYT
//
