ID A0A1C1C8D8_9EURO Unreviewed; 1263 AA.
AC A0A1C1C8D8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 02-APR-2025, entry version 34.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=CLCR_05364 {ECO:0000313|EMBL:OCT44731.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT44731.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-2015) 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:OCT44731.1}.
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DR EMBL; LGRB01000020; OCT44731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1C8D8; -.
DR STRING; 86049.A0A1C1C8D8; -.
DR VEuPathDB; FungiDB:CLCR_05364; -.
DR VEuPathDB; FungiDB:G647_07405; -.
DR eggNOG; KOG1329; Eukaryota.
DR OrthoDB; 14911at2759; -.
DR Proteomes; UP000094526; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:TreeGrafter.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter.
DR CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR FunFam; 3.30.870.10:FF:000032; Phospholipase; 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; PF00614; PLDc; 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:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000094526}.
FT DOMAIN 321..348
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1032..1059
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..86
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..485
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..553
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..640
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..661
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..691
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1263 AA; 139311 MW; DB381403469D41B8 CRC64;
MSYQQQPEDD GLAYGDDYSR SRGGGGTDRS LLGDIGKKFK TEFDKYKTGS PASQNYGYSS
TGGSNQGYYG QQGPTTGYPA TGQSPYPGGP PTQQPQGRPD IASKLLTGLH GTLHNIGSDV
ANLLGPDNNP SQQYASQAPG QAGHSHYAAA PGQPTIVSGP NRYDSFASEK PGNDVKWYVD
GCGYFWAVSQ ALEGARHSIW ILDWWLSPEV YLRRPPSQNE QWRLDRTLQR AAQRGVKVKV
IVYKEVTQAL TLSSAHTKHE LEKLHPNIAV FRHPDHLPDA QTAQSSLISS FQSLKLDAAA
VSKLGHDALK GIYGVTDDII LYWAHHEKLC LIDDKIAFMG GLDLCFGRWD TNQHSIADAH
PSDLNQIIFP GQDMNNARWA DFNDVANPFQ NKLDRTKSSR MGWSDIAICV QGTVVQDLRH
HFVDRWNFIY DEKYNVRKDQ RYYRLLDDLP HTASGPGHRP QSRPPSQSGP QPQGSLQASA
AAGGYAPPPG SQPYTEPAWH TTSRPHTPGG TYGTAPHSTA HGVQHQPPPT QSPYGQVQSP
PPQVVQSPPP PPGIYGQVPG GSPPQATHQP ITGAYDHHAT PMQAPPQGSM DPYNQFASPP
PQTAPVQGPA STASGYQQPT GQSPHQNYPP PPPGPPPQTS PSPATTYPGY PPPPSASPPY
TPYQQGATEL PSQQSPGLPY QHQSYQPYQQ PGSEQARGFD DYGQESSRGF NEYGPGNEDE
RGFGGERGMR GRFDHYKQEG RLLGQELSSI GSVVSGGLGD RAHQLQGKYL GGTDSYGRPY
NRPQGVMTCQ LLRSCTTWSN GTPLEHSIQN AYIEVIRNSQ HFVYIENQFF ITATGDQQKP
VKNLIGQAIV ERILRAARNS EKYKIIVVIP AVPAFAGDLR DDASLGTRAI MEFQYNSINR
GGHSIMEKIA QAGFNPMDYI RFYNLRNYDR INAGGTMQRV EQQSGVSYED ARKQHDDAVG
AGYGPLGERT NTAQLSQASQ YQQYQTTAQN MGQPGSGRWD SVAECYMLGG QDIRTVPWDG
PPEAELDAFV SEELYIHSKT LIADDRIVIC GSANLNDRSQ LGSHDSEIAL LIEDPTKVQS
YMNGQPYQAS SFAASLRRQL TRKHLGLIRP QYFFRPDPNF EPVGVPNAYD WSSPEDNVVM
DPLSDTFQAL WNSRARTNTE VFRKAFRAVP DDYVHSWSEY KEFYEYFYQP AETDAQGKPS
KLPPRVEYGH VVRADFPGGV RELKELLSQV KGTLVEMPLC FLQNEDIAKE GLTLNALTEE
IYT
//
