ID A0A177E0T6_ALTAL Unreviewed; 1921 AA.
AC A0A177E0T6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=CC77DRAFT_297676 {ECO:0000313|EMBL:OAG25020.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG25020.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG25020.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG25020.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664}.
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; KV441470; OAG25020.1; -; Genomic_DNA.
DR RefSeq; XP_018390441.1; XM_018531113.1.
DR STRING; 5599.A0A177E0T6; -.
DR GeneID; 29116707; -.
DR KEGG; aalt:CC77DRAFT_297676; -.
DR VEuPathDB; FungiDB:CC77DRAFT_297676; -.
DR OMA; DSLWTKH; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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 InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR001683; PX_dom.
DR PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR SMART; SM00155; PLDc; 2.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
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:UP000077248}.
FT DOMAIN 960..987
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1266..1293
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1354..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1411..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1485..1524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1641..1676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1695..1872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1496..1517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1642..1676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1696..1754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1775..1789
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1792..1815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1829..1847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1921 AA; 214424 MW; B8BCFD9073905C5D CRC64;
MAGSTSSSPM ARSPRSRSPA VSGRTDDSGR LLPPLGAGQA RNETQDLHNP APADGAPKIM
RSAPTGSPLS TKEAGEFPFN APTNANGASI PLGTAEAPLR ATKPSSHISN GSSSSYYPPF
APMSRHPTEG ELSDAPRERK SVQFARSATF TSDPPAANSR QQSWEVEDGE GKGKERSTQS
SSLMGKLRAL AAPIQGHGRS LSALTGSGQE GGSPHGQLSP TSELDEPRYD SEADADGESS
AGEGALRRPR QKRRKSSRRW FDGEGEGTQT APTTPKQSTG GFFSRDSPNM TPTSTRPGFL
RRSTMDDIPE NERQGYSEDE GRSRIAKESA WTRGLHSARG LSYGGLRRHD PNAEESEGQS
RPTGNLRSLT TFRGAAGENG QPSPWRMRSE RTSSLSAQKW KSIKNSLKLL GNRQKVERQI
DHAKSAELMA ELLAGAPAAL FFASMFQRDE HGHRRIPVLL EQLKVTITDT DRPAKKEGDR
HTALRIELEY GSGLTRMKWV VYRSVADFAN LHLKFKVQEK QDAFRSRPAT RMREIKDKAA
KDGENEKEEE KEDPRTKLPR FPRSVLPYLR GLRGYGILDD EGEEEEEEVA VGGAASGPEG
DASATERPNR PKRGKSSFLG RRQSSVSGSQ AQGAVGALVA RQGSFAGAAG QPLQAKQTHH
DRQRKKLEQY LRGLMTYLIF RPDSNRLCKF LELSALGVRL AAEGGYHGKE GYMMIKSSKG
VDNRKGWTKI AMMNRHWPKW FLVRHSYVVC VDSPEEMNVY DVFLVDADFH LDTKSARIRD
KKARDLASEA KASATGHHQL KLVNAERKMK LLARNERMLH QFEESINFMS QNTLWSQRQR
FDSFAPVRKK IYAQWLVDGR DYMWNVSRAI SMARDVIYIH DWWLSPELYL RRPAAISQKW
RLDRLLQRKA QEGVKIFVIM YRNIGAAIPI DSEYSKFSLL DLHPNIFVQR SPNQIRQNTF
FWSHHEKICV IDHTVAFCGG VDLCFGRWDT PQHVVVDDKP TGFELDDTPK DADHCQLWPG
KDYSNPRVQD FFALDKPYEE MYDRSRVPRM PWHDVGMQIV GQPARDLTRH FVQRWNYLLR
QRKPSRPTPF LLPPPDFNPA DIEALGLDGT CEVQILRSAC AWSLGTPNKV EHSIMNAYVQ
MIATSEHFVY IENQFYISSG DVLGTKIENK INDAIVDRIK RAHANDEDWR ACIMLPLMPG
YQNTVDEQEG SSVRLIMTCQ YHSICRGEGS IFGRLRAAGI EPEDYINFYA LRSWGEIGPN
KMLVTEQLYI HAKIMVVDDR VAIIGSANIN ERSMLGSRDS EIAAIIRDTE LLDSYMGGQP
YKVGKFPHTL RMRLMREHLG VDVDCISEEE MLSQMSDADS VGFQTESSGP GSPTAQRATE
EKLEENHSKM QDELIQKAEK LHSFNHDFDW AQDHNPHLQS TKKPSADPRV QHNSAHMKDV
RGEGADHMRE AVETRPVTTL ARDSYIDEHG HEKLVTDVAA EGAAAMPRKS ATLKTRKRSG
TTGTRNSAIS TQTDGTGYAG LPPPKLPRMD TLKLGLTQLS QLPALPLLDD TDIGGPPALQ
RTVSQGSSSI INPFLSEMRR PIVTEDCMRD PINDTFFLDT WHQVAENNTK LFRQVFRCMP
DNEVRTWKEY QEYAAFSERF TKSQGGDKSQ MHKQQDAPGT TGPPGTGLTS KFTSGAGAVG
KQVGALGEKL TEKMTNNSDR VNGESIHSTT HHSSMGGVEQ WANDQEKRVQ SQSPPPPTTR
GGLHVETASG STLNEKLAPE PADDAVVSPM NPAPPEKTFT FPAPPPIPND HTSHTDFATQ
NANGPPQTSH SMRDRSQRVT ISEPPIHPSA LPGNQSHNQN GSTPNRSNTK RSRRRATTKS
SNRQFHATDA DSMLDKEDAK RLLELVQGHI VLWPYDWLES EERGGGWLYN VDQIAPLEIY
N
//
