ID U9T196_RHIID Unreviewed; 916 AA.
AC U9T196;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Phosphatidylinositol-glycan-specific phospholipase D {ECO:0000256|ARBA:ARBA00015988};
DE EC=3.1.4.50 {ECO:0000256|ARBA:ARBA00012284};
DE AltName: Full=Glycosyl-phosphatidylinositol-specific phospholipase D {ECO:0000256|ARBA:ARBA00029753};
GN ORFNames=GLOINDRAFT_272538 {ECO:0000313|EMBL:ESA00078.1};
OS Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
OS (Arbuscular mycorrhizal fungus) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=747089 {ECO:0000313|EMBL:ESA00078.1};
RN [1] {ECO:0000313|EMBL:ESA00078.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DAOM 197198 {ECO:0000313|EMBL:ESA00078.1};
RG DOE Joint Genome Institute;
RA Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R.,
RA Charron P., Duensing N., Frei-dit-Frey N., Gianinazzi-Pearson V.,
RA Gilbert B., Handa Y., Hijri M., Kaul R., Kawaguchi M., Krajinski F.,
RA Lammers P., Lapierre D., Masclaux F.G., Murat C., Morin E., Ndikumana S.,
RA Pagni M., Petitpierre D., Requena N., Rosikiewicz P., Riley R., Saito K.,
RA San Clemente H., Shapiro H., van Tuinen D., Becard G., Bonfante P.,
RA Paszkowski U., Shachar-Hill Y., Young J.P., Sanders I.R., Henrissat B.,
RA Rensing S.A., Grigoriev I.V., Corradi N., Roux C., Martin F.;
RT "The genome of an arbuscular mycorrhizal fungus provides insights into the
RT evolution of the oldest plant symbiosis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-
CC myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1D-myo-inositol + a
CC 1,2-diacyl-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:10832,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57997,
CC ChEBI:CHEBI:58608, ChEBI:CHEBI:58700; EC=3.1.4.50;
CC Evidence={ECO:0000256|ARBA:ARBA00034002};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the GPLD1 family.
CC {ECO:0000256|ARBA:ARBA00008652}.
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DR EMBL; KI297475; ESA00078.1; -; Genomic_DNA.
DR AlphaFoldDB; U9T196; -.
DR eggNOG; KOG3637; Eukaryota.
DR HOGENOM; CLU_011756_0_0_1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004621; F:glycosylphosphatidylinositol phospholipase D activity; IEA:UniProtKB-EC.
DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 3.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR001028; Gprt_PLipase_D.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR029002; PLPC/GPLD1.
DR PANTHER; PTHR23221; GLYCOSYLPHOSPHATIDYLINOSITOL PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR23221:SF7; PHOSPHATIDYLINOSITOL-GLYCAN-SPECIFIC PHOSPHOLIPASE D; 1.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF00882; Zn_dep_PLPC; 1.
DR PRINTS; PR00718; PHPHLIPASED.
DR SMART; SM00191; Int_alpha; 4.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 2.
DR PROSITE; PS51470; FG_GAP; 3.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..195
FT /note="Phospholipase C/D"
FT /evidence="ECO:0000259|Pfam:PF00882"
FT REPEAT 436..497
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 516..576
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 660..722
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ SEQUENCE 916 AA; 104205 MW; 4CFEF158B763F8C8 CRC64;
MQMGLKKEVN TILLYNFIIP AAIKEKMKKF RYFLFLFLSL TSIVHGCGMS VHIEVTKRAM
YTFYNTKSKY NKYAEYIHNS PEFVQAGSFF PDWGFKCMGN DEVSEEAHWP PFMRVGAEYM
REKYNNATLE HDHVAQGTIA FIFAIVSHGV ADVTWHSIKM NSGFIRAMAD LNFMNDFGEA
HDVADTGGEF TLSHMSDLDY LVDKWSFPID DLVEIYRRMN RTVDGKQIIG CARRAFAAAQ
ANKRFGKHFF SVYGEKSPFL IEQSELYHKG GFNNMAADVA DCWHELVKWF EFGSTNNIEL
CNTFRMVSGT LPKNRYQPSS NDLVNLLYKY SVEILKTIGY NIRYHEKNGI GTFEIHRELL
RDPITNEPFI ELQDDSSEEE ESVKVEKYGF DQIFQDVPTN YEQIPLSSNK DSYNLLSSNM
INETPFNTKC NLVPDNPITL NIPYSYAQFG HDMVLGDFNG DGIQDLAISA PFYSNIQEIP
QTGAIFIING KKSSSFKVPE STNILDIADK IIYAYNLHDE NNNDPQSRFG WSMSVVDLNK
DGIDDLAVSA PSFGAKKYIY SGKVYVYFGK KNEGLKENKA DLEIYSEQDV LESDWQIEAL
GQYLSSGDVD GDGFDDLLIG CPYCGIYGKS RTFRLLHTGG VFAFLSSSDH KGNVTIFDYD
WSIISPGDQQ YEWFGYSINY FKLESMQNPI IIVGAPGYDD HLKAQMSGRI YGFEIIDKNP
VKVFDLSGIE KFQEFGSSII TGDFHENGKK LLLVASKSET HEKKFPFYNK DWQAGAIRLI
DMQYLKENKR LSDHDMILGK GLLALLHGSE SFSHLGSSLL WDDDEKSFWS SEPFTYWESG
QILKYSVRSL FDSSQAVSQE SIVSDECLVG RERQARFGHK IIKFDFDGDG KKDLVVSSEH
SNHAARLSGS VTIILK
//
