ID L8WU79_THACA Unreviewed; 448 AA.
AC L8WU79;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Inositol phosphophingolipids phospholipase C {ECO:0000313|EMBL:ELU40298.1};
GN ORFNames=AG1IA_05687 {ECO:0000313|EMBL:ELU40298.1};
OS Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU40298.1, ECO:0000313|Proteomes:UP000011668};
RN [1] {ECO:0000313|EMBL:ELU40298.1, ECO:0000313|Proteomes:UP000011668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX PubMed=23361014; DOI=10.1038/ncomms2427;
RA Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA Wang L., Liu H., Li P.;
RT "The evolution and pathogenic mechanisms of the rice sheath blight
RT pathogen.";
RL Nat. Commun. 4:1424-1424(2013).
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00004760}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the neutral sphingomyelinase family.
CC {ECO:0000256|ARBA:ARBA00006335}.
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:ELU40298.1}.
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DR EMBL; AFRT01001465; ELU40298.1; -; Genomic_DNA.
DR AlphaFoldDB; L8WU79; -.
DR STRING; 983506.L8WU79; -.
DR HOGENOM; CLU_034001_2_0_1; -.
DR OMA; IEESSMF; -.
DR Proteomes; UP000011668; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IEA:InterPro.
DR GO; GO:0043603; P:amide metabolic process; IEA:UniProt.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR038772; Sph/SMPD2-like.
DR PANTHER; PTHR16320:SF1; ENDONUCLEASE_EXONUCLEASE_PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G01540); 1.
DR PANTHER; PTHR16320; SPHINGOMYELINASE FAMILY MEMBER; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000011668};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 371..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..309
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT REGION 323..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 49236 MW; 5519821E8484C1A6 CRC64;
MSERDIELSH SRAQPSTDIT TAEPLAMDTP DSQLRVLTLN CWGLKFVSKD RVVRTRAIGD
EIAASNYDIV GLQELWVQGD YDYIKAKVAH KLPYSKYFLS GALGAGLAIF SRFPIKSTSL
HPYSLCGSPL DVAGGDWFVG KAVVGAIIDH PLLGELEIFN THVSGESPSK PQMAHRLVGA
YEFSRRVNIS ASLGRHVLAV GDFNCVSKSP AMQFIYTMTG LRDAWGSTHG SFVLPQADGV
HSPHHAVSDR GVTVFDEHAR KYLGKRLDYI LFRPPTSKPA QYTHELRCRD SSVGFTHYVP
GTEISFSDHF SVTATFECAP VHRSGQNGHR PITPPRGTSY SPSTRSEVLE YAISTMGAAY
SSARQDSHKK LVWFAGLVVL LIALIVGSAW VPESGVNPLL IFVGGLITWG GTTLLYAGFL
GGGWETRALM RTMEELEMLL QSEERRIY
//
