ID A0A0W0F1N4_9AGAR Unreviewed; 1073 AA.
AC A0A0W0F1N4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Putative inositol phosphophingolipids phospholipase C {ECO:0000313|EMBL:KTB30234.1};
GN ORFNames=WG66_17248 {ECO:0000313|EMBL:KTB30234.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB30234.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB30234.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB30234.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KTB30234.1}.
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DR EMBL; LATX01002393; KTB30234.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0F1N4; -.
DR eggNOG; ENOG502RCE4; Eukaryota.
DR Proteomes; UP000054988; 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:UP000054988};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 981..1000
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1006..1026
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 636..908
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT REGION 1..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1073 AA; 116296 MW; 9168EFEFC62139E9 CRC64;
MDVTIPSSSN PQNFVNHLTP DSFLNTNPTS STGIVDAPSN ETPAKRRPGR PKGSGKKDPS
STTPQNGTPT GKRPVGRPRK DGLPAGSAGP SRPRKSAASD ISDASTSLPT NHNLYSSTST
DGTSHGGTST TPRSNSFPIE HDWAELARTK PTMFLTALLL SLSNMPSVPA TSSLTVEEAF
KSHLVSLAPT PSQNHHIPSL YSILKTFWLP SSPAYFALTA STSTARTPSD HRFLYWDPQP
LVFNGISCPN CSSPLSNQGR IKSGPIKIYD IERPFFIIGC EYVCKSTTCM ASKNSEGRKY
ASTDPSILRS LPTKLKDEFP ARLVNETDSG SGPDVWNWNA RGVSKLLWNL VRNSLKAGLQ
KDGIMELLWN VQRGYPGDED KKMDDHEDSS HSGNATNGNG YSNGTYSKAV QQGSGGFTDA
YNNAWRANTA VVGARDSITS TATISSTPDL PPIVPSSTPS LPTSSSQNST PVFPHTYTPS
VYTHSPNSNF TSYQFTPQDF TTTTVSPKIH HPSASAPVSS ANNPPPNPLP TIIAPTTLVS
STPGTPVPSH STPVNASAHL PNTNGNSNPA PSELGTKRPY PFGPPSLGDT SDFQPLPHPQ
SGSSVNHLSL LSGEMPPRKR SPRHCSKGLK YVSKNRRQRI EALASELASS EEYDIIALQE
IWVFADYQHL LESVQKVTEA EVGFSGALGS GLAIFSRFPI IGSGAHPYSL NGQPIDVAGG
DWFVGKAAVS VILQHPVLGH LQVFNTHFYA KGGEDGPEHF RAHRLINAWE FAKLVKQAAS
MGRYIITLGD YNSIPTSLPM ALIREYTGVS DSWLVTHPYG NPSPDTIPTP EEAIEKYGMT
ADSPLCSWSA GKPLGGHALQ YGGKRLDYCL YRPPMSHSAE NLPTLRATDC RVTLRHNVPG
TNMSFSDHFA LRATLEIVNY NAGAAEPTTP FGDTPPHHAH ESSQDAWSDH LTDLSQESIT
TTIQALAGCY RFAKQRSQNE LYIFGLCIFI LVVIIVGSAF FPHPWINPIF ILLTIALSWL
GTTMLYEGFL YGNWERNALM NVIEELEIYK SALEIQSGSS SSRDRTSEEL LRR
//
