ID   SMD_ARTBC               Reviewed;         339 AA.
AC   D4AZV8;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Sphingomyelinase D {ECO:0000303|PubMed:24223912};
DE            Short=SMase D {ECO:0000303|PubMed:24223912};
DE            EC=3.1.4.41 {ECO:0000250|UniProtKB:B8NQ51};
DE   Flags: Precursor;
GN   ORFNames=ARB_01728 {ECO:0000312|EMBL:EFE31333.1};
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=24223912; DOI=10.1371/journal.pone.0079240;
RA   Dias-Lopes C., Neshich I.A., Neshich G., Ortega J.M., Granier C.,
RA   Chavez-Olortegui C., Molina F., Felicori L.;
RT   "Identification of new sphingomyelinases D in pathogenic fungi and other
RT   pathogenic organisms.";
RL   PLoS ONE 8:E79240-E79240(2013).
CC   -!- FUNCTION: Catalyzes the hydrolysis of sphingomyelin. Sphingomyelinases
CC       D are produced by some spider in their venoms, but also by arthropods
CC       such as ticks, or pathogenic bacteria and fungi. They might play a role
CC       in pathogenicity through different mechanisms, such as membrane
CC       destabilization and host cell penetration, but also pulmonary
CC       inflammation and cutaneous lesions. {ECO:0000250|UniProtKB:B8NQ51}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine 1-phosphate +
CC         choline + H(+); Xref=Rhea:RHEA:20984, ChEBI:CHEBI:15354,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17636,
CC         ChEBI:CHEBI:57674; EC=3.1.4.41;
CC         Evidence={ECO:0000250|UniProtKB:B8NQ51};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q8I914};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8I914};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- DOMAIN: The SMD-tail motif is highly conserved and may be responsible
CC       for structural stabilization. {ECO:0000303|PubMed:24223912}.
CC   -!- SIMILARITY: Belongs to the sphingomyelinase D/phospholipase D family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ABSU01000022; EFE31333.1; -; Genomic_DNA.
DR   RefSeq; XP_003011973.1; XM_003011927.1.
DR   AlphaFoldDB; D4AZV8; -.
DR   SMR; D4AZV8; -.
DR   STRING; 663331.D4AZV8; -.
DR   EnsemblFungi; EFE31333; EFE31333; ARB_01728.
DR   GeneID; 9519297; -.
DR   KEGG; abe:ARB_01728; -.
DR   eggNOG; ENOG502S5U7; Eukaryota.
DR   HOGENOM; CLU_059400_0_0_1; -.
DR   OMA; WLDLKNP; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050290; F:sphingomyelin phosphodiesterase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.190; -; 1.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Magnesium; Metal-binding;
KW   Reference proteome; Secreted; Signal; Virulence.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..339
FT                   /note="Sphingomyelinase D"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000431987"
FT   REGION          313..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           309..316
FT                   /note="SMD-tail"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        313..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        60
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         80
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         82
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
SQ   SEQUENCE   339 AA;  37485 MW;  A795CCFAA4B12755 CRC64;
     MVSLLRLCSF LLAAGSILVQ GSPIIAPSIP PCEPPSNFTG PSNFTSRPGN GASPFWLIAH
     RVLTKDGVKA ALGHGANALE MDITGWWSGW FGDHDGLLTS AGDTVSDLFD EIASRRTQGD
     PVSFVWLDLK NPDFNKNGVN IVSLMILCRE KLEKVGVRVL YGFYSSQTNG PSFKFVKQVM
     NENEAIGIDG KFETVEKDFE EKGIPLQKRV FSSGLFNPDF NFGNCEVHSS GVCAQLREGK
     ESHEFSKVFG WTVSSYTRKD HVYKMMEVGV DGLIYGFVAS HYYDHADIRH TLSTIRGWLE
     EHKDTHRLAT VDDNPWSSMS KKGSSKSSWV KGEVPSIAH