(data stored in ACNUC7421 zone)

SWISSPROT: NPIIC_ASPFU

ID   NPIIC_ASPFU             Reviewed;         450 AA.
AC   Q4WA45;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 3.
DT   11-DEC-2019, entry version 70.
DE   RecName: Full=Neutral protease 2 homolog AFUB_070680;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin AFUB_070680;
DE   Flags: Precursor;
GN   ORFNames=AFUA_4G02700;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
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.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC       proteinaceous substrates. Shows high activities on basic nuclear
CC       substrates such as histone and protamine. May be involved in virulence
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage of bonds with hydrophobic residues in
CC         P1'. Also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain.;
CC         EC=3.4.24.39;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M35 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL84418.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
DR   EMBL; AAHF01000016; EAL84418.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_746456.2; XM_741363.2.
DR   SMR; Q4WA45; -.
DR   GeneID; 3503899; -.
DR   KEGG; afm:AFUA_4G02700; -.
DR   EuPathDB; FungiDB:Afu4g02700; -.
DR   HOGENOM; HOG000193008; -.
DR   InParanoid; Q4WA45; -.
DR   KO; K19305; -.
DR   OrthoDB; 1038868at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   Proteomes; UP000002530; 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:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR029463; Lys_MEP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001384; Peptidase_M35.
DR   Pfam; PF02102; Peptidase_M35; 1.
DR   PRINTS; PR00768; DEUTEROLYSIN.
DR   SMART; SM01351; Aspzincin_M35; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WA45.
DR   SWISS-2DPAGE; Q4WA45.
KW   Cleavage on pair of basic residues; Disulfide bond; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted;
KW   Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..172
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407136"
FT   CHAIN           173..450
FT                   /note="Neutral protease 2 homolog AFUB_070680"
FT                   /id="PRO_0000407137"
FT   ACT_SITE        301
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   METAL           300
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   METAL           304
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   METAL           315
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        179..251
FT                   /evidence="ECO:0000250"
FT   DISULFID        258..276
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   450 AA;  47911 MW;  3FCAC99DC02732F2 CRC64;
     MKITALASAI LAVAQGALAL PARAPALDIT LSQVNNTRIK AVVKNSGTEK ITFVHLNFFN
     DPSPVKKVSL YRNATEVEFT GIKQRLRSDG LSNDALTTLA PGATYEDEFD IASTANLTQG
     GPVTVRTQGF VPIAMNNKIA GYIPYSSNEL ELEVDAEKAV AVPASIKPLD RRTKITSSCT
     GNRATVLNTA LRNAASIASK AADAASSGSS ALFTEYFKST SGNIRSAVAA RLKAVASEAS
     MNGGGSTTYY CSDPYGYCDS NVLAYTLPST NEVVNCELFY TLQEVTNDCH GQDQATTIIH
     EFTHAPGVYP PGTEDLGYGY SAATALSTSN ALNNADSYAL FANAVYLNCQ GQTGGQTTWD
     GYSQPGQTEP GTQTMWDGYS QPGQTEPGTQ TMWDGYSQPG QTEPGTQTTW DGYSQPGQIE
     PCTQTMWDGG SEPGQTEPDA QTMWDNFYQA
//

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