ID   SMD_UNCRE               Reviewed;         349 AA.
AC   C4JUE5;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 44.
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=UREG_04748 {ECO:0000312|EMBL:EEP79906.1};
OS   Uncinocarpus reesii (strain UAMH 1704).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX   NCBI_TaxID=336963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 1704;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476617; EEP79906.1; -; Genomic_DNA.
DR   RefSeq; XP_002584059.1; XM_002584013.1.
DR   AlphaFoldDB; C4JUE5; -.
DR   STRING; 336963.C4JUE5; -.
DR   PRIDE; C4JUE5; -.
DR   EnsemblFungi; EEP79906; EEP79906; UREG_04748.
DR   GeneID; 8442566; -.
DR   KEGG; ure:UREG_04748; -.
DR   VEuPathDB; FungiDB:UREG_04748; -.
DR   eggNOG; ENOG502S5U7; Eukaryota.
DR   HOGENOM; CLU_059400_0_0_1; -.
DR   InParanoid; C4JUE5; -.
DR   OrthoDB; 1048800at2759; -.
DR   Proteomes; UP000002058; 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.
DR   SUPFAM; SSF51695; SSF51695; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Magnesium; Metal-binding;
KW   Reference proteome; Secreted; Signal; Virulence.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..349
FT                   /note="Sphingomyelinase D"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000431989"
FT   MOTIF           310..317
FT                   /note="SMD-tail"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        52
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         72
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         74
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         123
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
SQ   SEQUENCE   349 AA;  39447 MW;  8962E033D2A0593E CRC64;
     MLLSSLISLA LLSSQVVADP AWAPPDKGLK PEVARLLPPF LRYRRPIYAI AHRVVTVGGI
     KDAISHGANA FEVDMCADSI GEGWWANHDC TNGRKAGDSA RKIFETFAAE RKRGKTVTFV
     WLDFKNPDAC VKNQGCSIEA IQQLCRDILE KQGIRVLYGF YKAEDSRAFK TIRNNLNDRE
     AISLNGATTK VLKLFEGTAP KVSKHQRVMD YGDTYLDKGF GDCTEKDWYT CTELRQGADL
     RRKGKLGKVF AWTSTVNQGR LVDQLLGKAH VDGIIYGFKL TDYYDHADSR AAANDIISWV
     KRRRALYYMA TNDNNPWIDI HKLFLYLLSW FSCILLLMMN EWTCPQDGA