ID J5JMP0_BEAB2 Unreviewed; 664 AA.
AC J5JMP0;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Sphingomyelin phosphodiesterase {ECO:0000256|PIRNR:PIRNR000948};
GN ORFNames=BBA_06698 {ECO:0000313|EMBL:EJP64316.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP64316.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP64316.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP64316.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
CC -!- FUNCTION: Converts sphingomyelin to ceramide.
CC {ECO:0000256|PIRNR:PIRNR000948}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR000948-1};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR000948-
CC 1};
CC -!- SIMILARITY: Belongs to the acid sphingomyelinase family.
CC {ECO:0000256|PIRNR:PIRNR000948}.
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DR EMBL; JH725169; EJP64316.1; -; Genomic_DNA.
DR RefSeq; XP_008600017.1; XM_008601795.1.
DR AlphaFoldDB; J5JMP0; -.
DR STRING; 655819.J5JMP0; -.
DR GeneID; 19889710; -.
DR HOGENOM; CLU_014743_1_0_1; -.
DR InParanoid; J5JMP0; -.
DR OrthoDB; 205363at2759; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006685; P:sphingomyelin catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00842; MPP_ASMase; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR041805; ASMase/PPN1_MPP.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR011160; Sphingomy_PDE.
DR PANTHER; PTHR10340; SPHINGOMYELIN PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR10340:SF34; SPHINGOMYELIN PHOSPHODIESTERASE; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF000948; Sphingomy_PDE; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000948-2};
KW Glycosidase {ECO:0000256|PIRNR:PIRNR000948};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000948};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000948-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR000948-1}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..664
FT /note="Sphingomyelin phosphodiesterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003783678"
FT DOMAIN 167..434
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT DISULFID 59..135
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 88..99
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 189..194
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 195..219
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 567..571
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
SQ SEQUENCE 664 AA; 73463 MW; 025E2851DE93559E CRC64;
MRVGHLVALL GATAPIITAA QGDHHLAPRA AEVTALTQSL NQPGLAGDIW DTIKGVASCA
ACQGILGLLK GIAFFGEAAF INTAKIVCKV SKVEDPDVCD GIMELEGPTL ARLVWELSLY
GRTSKLFCGA VLGLCDMPDS LKPKLKFPPK PENMTSGRPT PSGKEPIKVV HFSDIHIDHH
YTPGSNTQCS KPICCRAYTE KDAPGTTENP AGPFGDHKCD TPVDLERSMY RAIQDIAPDA
AFTLFTGDIP DHTIWNTTKK STIHDINHAM SIMNSNLDTV YGTVGNHEIS PVNLFPSTQY
AKKQTSAKWV YDLLADYWTE WTGDSARQDI SEIGAYSAKY PHGKLRIISI NTNLYYRHNF
EVYRDKTERD PNGQFQWLVQ QLDEAEKAGD RAYILGHMPM GDMDALRDGS RAFDQIVNRY
ADTIAAMFFG HTHVDHFELH YSDYKNRDFS NARAVSYIAP SLTPTSGMPA FRVYSVDPDT
FAVLDSVQYA ADMTRADYQT AGPTWTRYYS AKDVYGPLVH PPLTDNDAAV ELTPAFWHNV
TVAFAADEAV FDQYMQRKSR GWKHQPCADD CARVEVCMLR GGRAEDNCYK PKPGISLRRR
VGLLTRRTDM GNNAHDDCGA SASVAMLDSI ASNKEVLEKL KEIFDEMGAK AGAKSFDPEK
GWLF
//
