ID   SMD_TRIRC               Reviewed;         323 AA.
AC   F2SCC4;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 38.
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=TERG_01406 {ECO:0000312|EMBL:EGD85130.1};
OS   Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4607 / CBS 118892;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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}.
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DR   EMBL; GG700648; EGD85130.1; -; Genomic_DNA.
DR   RefSeq; XP_003239421.1; XM_003239373.1.
DR   AlphaFoldDB; F2SCC4; -.
DR   SMR; F2SCC4; -.
DR   STRING; 559305.F2SCC4; -.
DR   EnsemblFungi; EGD85130; EGD85130; TERG_01406.
DR   GeneID; 10374817; -.
DR   VEuPathDB; FungiDB:TERG_01406; -.
DR   eggNOG; ENOG502S5U7; Eukaryota.
DR   HOGENOM; CLU_059400_0_0_1; -.
DR   InParanoid; F2SCC4; -.
DR   Proteomes; UP000008864; 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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..323
FT                   /note="Sphingomyelinase D"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000431988"
FT   MOTIF           308..315
FT                   /note="SMD-tail"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        59
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         79
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         81
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         127
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
SQ   SEQUENCE   323 AA;  36108 MW;  494959CB300EFE01 CRC64;
     MISLLRLCSF LAAGSILVQG SPIIAPSAPT WDTPNNFTSP SNFTSKPGNE ASPFWLIGHR
     VLTKGGVRAA LGHGANALEV DITGWWNGWY GDHDGLPSSA GDKVADLFDE IAYRRRQGAQ
     VSFVWLDLKN PDFNKNGVNI VSLMTLCREK LEPAGVRVLF GFYSSQTSGH AFRFVKQVLN
     ENEAIGIDGS FEPVEKDFEK NGIRVEKRVF SSGLFNPDFN FGTCQDRASG VCTQLREGKE
     SHKFGKVFGW TVSSYTRKDH VYKMMEVGVD GLIYGFVASH YYNHKDIRQT IRTIRGWLDE
     HRDTHRLATN DDNPWSMSSR KSS