ID A0A080WRT2_TRIRC Unreviewed; 1695 AA.
AC A0A080WRT2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=TERG_02523 {ECO:0000313|EMBL:KFL60898.1};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:KFL60898.1, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
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}.
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DR EMBL; GG700649; KFL60898.1; -; Genomic_DNA.
DR OMA; DSLWTKH; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000008864; 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:UP000008864}.
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..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1607..1663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1512..1536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1607..1621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1695 AA; 192178 MW; A333576606BE693F CRC64;
MDDDGRKGVR EGQTLNPKDI TDGKGSRGTE PLPMVEHAHT GLAEPSSQPA TGTSTPIARR
SIQFTRGDGD NEAPGQGQSY SRPPSESAAD EEIAPKRGHF QFMSKLRALA PSTSRSAGPA
SPVAPSHDRT LSDGAGPLSD LAEFRFPRPE DAGGGSDADA DVESSSEAGF RVQVKRKKRK
TKRPPLDLSH TTPSTPKSAL SVANSVKPYD DPQSANAPLT PPIHRLREGV SEDEGRDRLN
RDNMWRRRSN WLQGSRGRSI TGQRADGHAS QDERRPTNLR RFTGFGGTSE HADGISGAWR
RHKAERGSSL SAQKWKQIKA GFKLIGQRKK QENTVDHVKS AELLAELTSG VPAALLLASM
FQRDEHGSRR IPILLEQLKV HVTDSEFDSH SSGDRHLVFR IELEYGSGMT RMKWVIHRTL
KDFANLHLKY KLQIGTQRYI QLRSHDSGNQ LPRFPKSAFP YMRGVRGLES DMEDEEDEAA
EDTAADATSG NERSRKKKRR SSIALSRRRS SLASRLDAPA NSDRAVDNGT ASKRETYPEK
QRKKLESYLQ KMIRFLIFRP DSNRLCKFLE LSALGVRLAA EGSYHGKEGY LVIQSSKGLD
FRKALNPSMV KSRHSPKWFL VRHSYIVCVD SPEEMHIYDV FLIDPYFQIQ AQKVRLRDQN
PKELKESAKH PQHHTLKIQN SERRMRLLAR NDRQLRQFED SIRLVLETTP WAKPNRFESF
APVRPNCFAQ WLVDGRDYMW VVSRAINQAK DVIYIHDWWL SPELYMRRPA AISQKWRLDR
LLQRKAQEGV KIFVIMYRNI NSAIPIDSEY SKFSLLDLHP NVFVQRSPNQ FRQNTFFWAH
HEKICIVDHT LAFVGGIDLC FGRWDTPQHL ITDDKLTGFE MTDAPKDADH CQLWPGKDYS
NPRVLDFYDL DKPYEEMYDR EVVPRMAWHD ISMHVVGQPA RDLTRHFVQR WNYILRQRKP
TRPTPFLLPP PDFNPADLEA LGLDGTCEIQ IVRSSSMWST GTPDVVECSI MNAYVKMIEK
SDHFVYIENQ FFISSCEIEG KKIENHIGDA LVERIIRAAD NEEAWRAVIL IPLMPGFQNT
VDTEGGTSVR LIMQCQYRSI CRGESSIFGR LRARGIEPED YIQFFSLRSW GRIGPKKNLV
TEQLYIHAKC MIVDDRVAII GSANINERSM LGSRDSECAA VVRDTDLLES RMNGKPYLVG
RFPHTLRMRL MREHLGFDVD EIVEEYTSAF ETTNIDRTPE HLPDVASQPE HGPADGENQA
EKDDLERKQK VQEEFLARFE EMHSFNHDVD WEQAGNPNLK SNRKLTADAR VTRNEDHRKD
LEGHGVDQMK RNGEIVGTTG RDTVLKNSVE VLVTGRVKNN TTPSTMPCDN ASDVAGSMAN
TKQPTAPGTP ETHPRSVSTS SPRMTGQNRS AAANATDDHI QHFSLDATQP KNTSHFLLDE
PRRPILDKDC MKDPLLNSFY LDTWQAIAEN NTKLFRSVFR CMPDSEVKTW KDYKEYTAYA
ERFADMQNHC NASAGSQSCP RNGPSGANNG SPNGGKLGTE LGSALEEVKE KFGTHQSSEK
DKELHANLHQ WAVEANQAQL ERQHQEQLHV DKSVPHADIH SHAFNNADAR SSNSSRNAES
FHTPVAPEKN VEVPRSSQSE APAPSIGMSQ RRRRRANTRS SRKEFHAVDD IMDMHEAAEL
LGSVQGHLVL WPYEW
//
