ID M2W415_GALSU Unreviewed; 553 AA.
AC M2W415;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=sphingomyelin phosphodiesterase {ECO:0000256|ARBA:ARBA00012369};
DE EC=3.1.4.12 {ECO:0000256|ARBA:ARBA00012369};
GN ORFNames=Gasu_21650 {ECO:0000313|EMBL:EME30491.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME30491.1, ECO:0000313|Proteomes:UP000030680};
RN [1] {ECO:0000313|Proteomes:UP000030680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(2013).
CC -!- SIMILARITY: Belongs to the neutral sphingomyelinase family.
CC {ECO:0000256|ARBA:ARBA00006335}.
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DR EMBL; KB454499; EME30491.1; -; Genomic_DNA.
DR RefSeq; XP_005707011.1; XM_005706954.1.
DR AlphaFoldDB; M2W415; -.
DR STRING; 130081.M2W415; -.
DR EnsemblPlants; EME30491; EME30491; Gasu_21650.
DR GeneID; 17089217; -.
DR Gramene; EME30491; EME30491; Gasu_21650.
DR KEGG; gsl:Gasu_21650; -.
DR eggNOG; ENOG502S5SW; Eukaryota.
DR OrthoDB; 5490670at2759; -.
DR Proteomes; UP000030680; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0043603; P:amide metabolic process; IEA:UniProt.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd09078; nSMase; 1.
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 InterPro; IPR017766; Sphingomyelinase/PLipase_C.
DR PANTHER; PTHR16320:SF23; SPHINGOMYELINASE DDB_G0288017; 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 Hydrolase {ECO:0000313|EMBL:EME30491.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030680};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 106..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 258..522
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 63229 MW; B9807C675761AC00 CRC64;
MPIRPQESYS QGLRKRAASL EENAQRDGDD EANKLIVNSK NSSKNKVLEA NDLLDEDKKS
LHHGRQPRTL TSRSPRRDIL SLERHRTCSV TGEPPVPTRK FTASPLLRTC CLLLSGSLVL
FMTSFAVYLR NYMAAAHSVS FVFVTCLFFG PVSFAAVIIG LHGCCAANVS ISKASSKTIR
MTMAIFLIYL VIIYIFPFDR QEWYENTAKQ AYNRWMHSSS SKSNNTFVDP QDYFLSKFLE
SYKFRILSYN IFIRPPGVTS NGNDYKDERL VRFLSHMMRY DIICLQELFT LGSDRWQALT
KAARIFGFYY EAHLKRNLFS WLPKVVDGGV TILSKFPIVA TDSIFFKRSS YSTIDCIVAK
GVLYAKIELP FVEPRYLHLF STHLQAGDEP LEEMMNIKLT QLEQAREFIY SKLNSERKEL
VVFCGDLNVN GRMSVVDGRD SKEYFKMMQL LSASSSSSGY SKIPSLRWKD VIRDSYQGMH
PVTVGDADVD EYGQLLRTWE LQLASKGDRG CRKRLDYILF DPRNSGLDIS NKSSSKVETF
FVSELTGCEQ TRY
//
