(data stored in ACNUC7421 zone)

SWISSPROT: Q4WNR0_ASPFU

ID   Q4WNR0_ASPFU            Unreviewed;       627 AA.
AC   Q4WNR0;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 76.
DE   RecName: Full=Sphingomyelin phosphodiesterase {ECO:0000256|PIRNR:PIRNR000948};
GN   ORFNames=AFUA_4G06640 {ECO:0000313|EMBL:EAL90124.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL90124.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL90124.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL90124.1}.
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DR   EMBL; AAHF01000005; EAL90124.1; -; Genomic_DNA.
DR   RefSeq; XP_752162.1; XM_747069.1.
DR   STRING; 746128.CADAFUBP00006198; -.
DR   EnsemblFungi; EAL90124; EAL90124; AFUA_4G06640.
DR   GeneID; 3509254; -.
DR   KEGG; afm:AFUA_4G06640; -.
DR   EuPathDB; FungiDB:Afu4g06640; -.
DR   HOGENOM; HOG000216889; -.
DR   InParanoid; Q4WNR0; -.
DR   KO; K12350; -.
DR   OMA; LCRHLMP; -.
DR   OrthoDB; 1142100at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0008081; F:phosphoric diester hydrolase activity; IBA:GO_Central.
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; IPR008139; SaposinB_dom.
DR   InterPro; IPR011160; Sphingomy_PDE.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF000948; Sphingomy_PDE; 1.
DR   SMART; SM00741; SapB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WNR0.
DR   SWISS-2DPAGE; Q4WNR0.
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR000948-2};
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR000948};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000948, ECO:0000313|EMBL:EAL90124.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000948-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR000948-1}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..627
FT                   /note="Sphingomyelin phosphodiesterase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004246561"
FT   DOMAIN          36..114
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000259|SMART:SM00741"
FT   METAL           151
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT   METAL           153
FT                   /note="Zinc 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT   METAL           223
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT   METAL           223
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT   METAL           260
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT   METAL           374
FT                   /note="Zinc 2; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT   METAL           408
FT                   /note="Zinc 2; via pros nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT   METAL           410
FT                   /note="Zinc 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT   DISULFID        38..114
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT   DISULFID        67..78
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT   DISULFID        166..171
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT   DISULFID        172..196
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT   DISULFID        538..542
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
SQ   SEQUENCE   627 AA;  68420 MW;  8D2799A723127F16 CRC64;
     MRLTTFVAAL ASLATIHGAS SENWASTIWD DIKETITCAG CEGLLGTLKL VAGLGENVLI
     NVLTDVCKLA KVEDPDVCAG IIRAEGPAAY YVLKQLKVGS HTSKSFCSQM VGLCDYPEVR
     PYKISFPVPK PSTHRPPPSG QPPIRVAHIS DTHVDRAYET GANYECSKPI CCRVYTENDA
     PGKTSFPCGP YGHPKCDPPL RLEESMVAAI AAMDPAFSIY TGDVVPHDVW SVNQTEVLHD
     LNATYSLLDQ LGLVYAALGN HDTAPVNLFP SERIPLSHNP QWAYDALAED WTNLVGGPLS
     APVVHATDQF GSYSAVHPGG KLRIISYNSV FYYTYNFYAY QEPMEYDPNG QLAWLISELQ
     AAETAGQRVW LIAHIPTGGT DTLHDYSHYL DQIIQRYDAT IAALFFGHTH TDLFQVSYAD
     PAHPSADSAS AVGYITPSLT PTSGPPAFRI YDIDPVTFAV LDYTVYTANV STEATPQWTK
     YYSAKESYGS LITPPVTDPT AELTPAFWHN VTVLMETDNS VFQAWWARTT RGFKVRECNA
     QCARDQICSL RAADAQYGCV RGTLSITKRD GLNLAGVAPA SASGPQVHVH STRPQCEEGG
     LARVLAAVIR ETDDLQGLLL QRAELYI
//

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