ID E4UX06_ARTGP Unreviewed; 1718 AA.
AC E4UX06;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=MGYG_05643 {ECO:0000313|EMBL:EFR02645.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS989825; EFR02645.1; -; Genomic_DNA.
DR RefSeq; XP_003173056.1; XM_003173008.1.
DR STRING; 535722.E4UX06; -.
DR GeneID; 10028333; -.
DR VEuPathDB; FungiDB:MGYG_05643; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_0_1_1; -.
DR InParanoid; E4UX06; -.
DR OMA; DSLWTKH; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000002669; 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 PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00155; PLDc; 2.
DR SMART; SM00312; PX; 1.
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:UP000002669}.
FT DOMAIN 377..576
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 836..863
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1142..1169
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1356..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1516..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1593..1664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1605..1621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1718 AA; 194864 MW; 0C06A3A97DC7D51F CRC64;
MDENGGKGVH EGRALNTEDT ADGNGNRGTE PLATVERAHT GHAEPGLQPT TGASTPTARR
SVQFSRTEGD NDAQGQRQSY SRPPSELAAD EEIAPKRGHF QFMSKLRALA PSTSRSAGPA
SPVGPSHDRT MSDGAGPLSD LAEFRFPRSE DAGGGSDADA DVESSSEAGF GVQMKKKKRK
TKRLPLDISN TTPSTPKSGL SAANSIHPYD DPQSANAPLT PPLHRLREGF SEDEGRDRLN
RDNMWRRRSN WLQGTRGRSI TGQRADGQTS QDERRPTNLR RLTGFGGTSD HADGISGAWR
RHKAERGSSL SAQKWKQIKA GFKLIGQRKK QENTVDHVKS AELLAELTSG VPAALLLASM
FQRDEHGSRR IPILLEQLKV HVTDSEFDSH SSGDRHLVFR IELEYGSGMT RMKWVIHRTL
KDFANLHLKY KLQIGTQRYI QLRSHDSGHQ LPHFPKSAFP YMRGVRGLDS DIEDEEDEAA
EDTAADATSG NERSRKKKRR SSIALTRRRS SLASRLDAPA NSDRAVDNST SNKRETYPEK
QRKKLESYLQ KMIRFLIFRP DSNRLCKFLE LSALGVRLAA EGSYHGKEGY LVIQSSKGLD
FRKALNPSMV KSRHSPKWFL VRHSYIVCVD SPEEMHIYDV FLVDPYFQIQ AQKVRLRDQN
PTELKESAKH PQHHTLKVQN SERRLRLLAR NDRQLRQFED SIRLMLETTP WAKPNRFDSF
APVRPNCFAQ WLVDGRDYMW VVSRAINQAK DVIYIHDWWL SPELYMRRPA AISQKWRLDR
LLQRKAQEGV KIFVIMYRNI NSAIPIDSEY SKFSLLDLHP NVFVQRSPNQ FRQNTFFWAH
HEKICIVDHT LAFVGGIDLC FGRWDTPQHL ITDDKLTGFE MTDSPKDADH CQLWPGKDYS
NPRVLDFYDL DKPYEEMYDR EVVPRMAWHD ISMHVVGQPA RDLTRHFVQR WNYILRQRKP
TRPTPFLLPP PDFNPVDLET LGLDGTCEIQ IVRSSSMWST GTPDVVECSI MNAYVKMIEK
SDHFVYIENQ FFISSCEIEG KKIENHIGDA LVERIIRAAN NEEAWRAVIL IPLMPGFQNT
VDTEGGTSVR LIMQCQYRSI CRGESSIFGR LRARGIEPED YIQFFSLRSW GRIGPKKSLV
TEQLYIHAKC MVVDDRVAII GSANINERSM LGSRDSECAA VVRDTDLIES HMNGKPYLVG
RFPHTLRMRL MREHLGFDVD EIVEEYTSAP AENASIDRTF GNQPEVTIQA ENIPTDGENQ
PEKDDLEKKQ KVQEEFLARF EEMHSFNHDV DWEQAGNPNL KSNRKLTADA RVTRNEDHRK
DLEGHGVDQM KRNEEIVGTT GRDTFHKNSV EVLVTGRTKN NSAPSTAPCD NVSGVAGSTA
DAKQQTAPGT PETHPRSASM SSPRMTGQNR PAAANATDDH IQHFSLDATQ PKNTSHFPLD
EPKRPILDKD CMKDPLLDSF YLDTWQAIAE NNTKLFRSVF RCMPDSEVKT WKDYKEYTAY
AERFADMQNH CNASAGNQSC PRNGPSGTNN NSSNGGKLGT ELGNALEEVK EKFAAHHSSE
KDKELHANLH QWAVEANQAQ LERQQQELLH VDKSIPHPDT PSHIANNADA RSSNSSRHAE
YSHTPVAPER NLELPRSSHS EAPAPSIGMS QRRRRRATTR SSRKEFHAVD DIMDMHEAAE
LLGLVQGHLV TWPYEWLERE EQGGNWLYTL DQISPLEI
//
