ID D8SYL9_SELML Unreviewed; 830 AA.
AC D8SYL9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=Phospholipase D {ECO:0000256|ARBA:ARBA00012027, ECO:0000256|PIRNR:PIRNR036470};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027, ECO:0000256|PIRNR:PIRNR036470};
GN ORFNames=SELMODRAFT_269402 {ECO:0000313|EMBL:EFJ10479.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ10479.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond. {ECO:0000256|PIRNR:PIRNR036470}.
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:PIRNR036470};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913,
CC ECO:0000256|PIRNR:PIRNR036470};
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000256|ARBA:ARBA00010683, ECO:0000256|PIRNR:PIRNR036470}.
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DR EMBL; GL377653; EFJ10479.1; -; Genomic_DNA.
DR RefSeq; XP_002988389.1; XM_002988343.1.
DR AlphaFoldDB; D8SYL9; -.
DR STRING; 88036.D8SYL9; -.
DR EnsemblPlants; EFJ10479; EFJ10479; SELMODRAFT_269402.
DR GeneID; 9637587; -.
DR Gramene; EFJ10479; EFJ10479; SELMODRAFT_269402.
DR KEGG; smo:SELMODRAFT_269402; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_004684_0_0_1; -.
DR InParanoid; D8SYL9; -.
DR OMA; ISHWHEN; -.
DR OrthoDB; 3014064at2759; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0004630; F:phospholipase D activity; IBA:GO_Central.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR CDD; cd04015; C2_plant_PLD; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR024632; PLipase_D_C.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR011402; PLipase_D_pln.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF60; PHOSPHOLIPASE D; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 1.
DR PIRSF; PIRSF036470; PLD_plant; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRNR:PIRNR036470};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036470};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR036470};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR036470};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514}.
FT DOMAIN 1..148
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 349..384
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 673..700
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 830 AA; 93297 MW; CAEF4A0D2814F395 CRC64;
MEDVSLGASS PKVCLLYGTV ELEIIEAKSL PNMDWFSERA SQCFSILGGL QTMCAKPKDK
LAHHRHKITS DPYVVFSLGD AILAKTKVIS NSQIPHWGER FQLHVAHSVP EVLLTVKDND
VFGAQVIGGV KIPAHRIASG PAIVETWFDV VGSGKEGAQL KISIKYTPVE QDKNYQHGVG
AEGAVPRTYF PLRKGCSVKL YQDAHCPDGG LPEITLEGGG AYEHGKCWED ICQAILEAHH
LVYIAGWSVF HKVKIVREPE NHKKFSNDIA NLTLGELLKR KAAEGVRVLL LVWDDKTSHH
TPLFTTKGVM ATYDEETKKF FRHSAVRCVL SPRYGDSKMS WLKQWVVGTF YTHHQKLVIV
DSQGRGNNRK LTSFIGGLDL AQGRYDTPEH PLFKTLGSIH RDDYHNPTFT GTIDHGGPRQ
PWHDLHCRID GPAAYDVLTN FAQRWRKAAT WHEDAMIEID RISWILSPND GDQALMVTEL
DDPETWNVQV FRSIDSGSVK GFPKEPADCQ KQNLVTLKNV AIDTSIHTAY VERIRSAQHF
IYIENQYFLG SSYAWPDYKK GDATHMIPME LALKVASKIR SGDPFAVYVV IPMWPEGVPD
SATVQEILYF QSQTMKMMYK IIAQALNEVG SGNHPTDYLN FYCLANREER SEPGTMAPAE
KSTQWYAQKY KRFMIYIHSK GMIVDDEYVI IGSANINQRS MDGSRDTELA MGAYQPHYTW
AHKKHSHPFG QVYGYRASLW AEHLGDFDPA LFNDPSDIRC VHKVNEIAQG NWKQFVSEEP
SDMKGHLMSY PMSVQVNGEI KPIAGNESFP DVAGQVLGQH SINLPDNLTG
//