ID W9YPH1_9EURO Unreviewed; 1292 AA.
AC W9YPH1;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=A1O1_02823 {ECO:0000313|EMBL:EXJ94428.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ94428.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ94428.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ94428.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:EXJ94428.1}.
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DR EMBL; AMWN01000002; EXJ94428.1; -; Genomic_DNA.
DR RefSeq; XP_007721922.1; XM_007723732.1.
DR STRING; 1182541.W9YPH1; -.
DR GeneID; 19157721; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_2_2_1; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000019484; 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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF186; PHOSPHOLIPASE D; 1.
DR Pfam; PF13091; PLDc_2; 1.
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:UP000019484}.
FT DOMAIN 377..404
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1061..1088
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..545
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..665
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1292 AA; 142769 MW; E35564FCE923D857 CRC64;
MSYQRPSDED ALAYGDDYSQ SRGSRQEGTE RSVLGDTFRM FKSGYDKYKT PSSQNYGYSS
SGTSQQCYGQ PTPATGYPQP GQAAYPGGPP MQQPEGKPDL GAKLLGTLHN TIHSIGSDIA
NLLGPDGKPA RYSNQPSGQQ PEGPSTYSGY ANAPTSSEQA HGQYRFDSFA SEKPGNDVKW
YVDGCAYFWA VSQALEGARE SIWILDWWLS PEVYLRRPPS QNEQWRLDRT LQRAAQRGVK
VNIIVYKEVT QALSAYLSPI MINYLHSLVP QAAGTFTSFL VALGLRATTT SLNYAEKENP
LILPPLALSS AHTKHELEKL SPNISVFRHP DHLPDAQTAQ SSLISSLQNL KLDAAGVSKL
GADALKGVYG LDEDVILYWA HHEKLCLIDG KIAFMGGLDL CFGRWDTNQH AIVDAHPLNI
SDIVFPGQDY NNARVMDFSN VADPFQNKLD RTKSSRMGWS DIALSLQGSC VQDLRHHFID
RWNFIFEEKY NVRKDARYSR IIDDYPHSTS GPARRPQAHP QSPEKIQPSA PGGAFPPPPG
SRPYAPPAWH STSRPHTPGS EPYQNQLSTT PGNQPASYGA ASSPSIQHTY PQPAGPQTSY
VQGMGPAVHG DQGQSLAATG GYPQISSPTP QGAYNQPTGI GGQSPNPYFQ QAFPPPPPGP
PSQPSPGLGY DHTGYSPQIK PEPTYAPFQQ GASELSSQQT PNHAYEYHSY QQQTSPAVSG
QPYQPQIHQQ SGTEENRGLD DYGYGDESER GFDSERGLRG KVDRYRTEGK RIGQELSSVG
SLVSSGMEGR MHHIQGKYLG ATDSYGRPYS QARGAMTCQL LRSCTQWSNG TPLEHSIQNA
YIDVIRNSQH FVYIENQFFI TATGDKQKPV KNLVGQAIVE RIMRAAKAGE RYKVIVVIPA
VPAFAGDLRD EGSLGTRAIM EFQYFSINRG GHSIMEEIAQ AGYNPMDYIR FYNLRNYDRI
NCGGAMAQAE QQSGVKYEEA RKEHDNVMGA GYGSSGERTG VTQMSRVSQY QQYQSAAQNT
SAAPGSRWDS VAECYMLGGQ DIRTVPWDGT PEAELDAFVS EELYIHSKCM IADDRVVICG
SANLNDRSLL GSHDSEIAIL INDPTPVQTY VAGQPYQVSR FAASLRRYLT RKHLGLVRPQ
DMRRPDPNYE PVGVPNVYDW GSPEDNIVSD PLSDAFQSLW NSRARTNTDI FRKAFRAVPD
DHVTTWAEYK ECYEYFYHAD AKDAGKDGTK VPPRVEYGHV VREDFPGGVQ ELKELLSHVE
GTLVEMPLCF LQNEDIAKEG LTLNALTEEL YT
//
