NPIIA_ASPFU
ID NPIIA_ASPFU Reviewed; 370 AA.
AC Q4WQR6;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Neutral protease 2 homolog AFUA_4G13750;
DE EC=3.4.24.39;
DE AltName: Full=Deuterolysin AFUA_4G13750;
DE Flags: Precursor;
GN ORFNames=AFUA_4G13750;
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;
OC Aspergillus subgen. Fumigati.
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}.
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DR EMBL; AAHF01000005; EAL89418.1; -; Genomic_DNA.
DR RefSeq; XP_751456.1; XM_746363.1.
DR AlphaFoldDB; Q4WQR6; -.
DR SMR; Q4WQR6; -.
DR MEROPS; M35.002; -.
DR EnsemblFungi; EAL89418; EAL89418; AFUA_4G13750.
DR GeneID; 3509585; -.
DR KEGG; afm:AFUA_4G13750; -.
DR eggNOG; ENOG502SGF5; Eukaryota.
DR HOGENOM; CLU_039313_1_1_1; -.
DR InParanoid; Q4WQR6; -.
DR OMA; DVTFVHL; -.
DR OrthoDB; 1038868at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
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:0006508; P:proteolysis; 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;
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_0000407092"
FT CHAIN 173..370
FT /note="Neutral protease 2 homolog AFUA_4G13750"
FT /id="PRO_0000407093"
FT ACT_SITE 301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT DISULFID 178..250
FT /evidence="ECO:0000250"
FT DISULFID 257..275
FT /evidence="ECO:0000250"
SQ SEQUENCE 370 AA; 39405 MW; 2E25B5DB2D3C2817 CRC64;
MKVTILASAI LALINGALAL PANTPTLDVT LTQVDNTRIK ATVKNTGNEK VTFVHLNFFQ
DAAPVKKVSL FRNATEVEFT GIKRRLLTEG LSDDALTTLA PGATFEDEFD VASTADLTEG
GTVTIRTDGF VPITTDRKVS GYIPYQSNEL EIEVDAAKAA AVPQAIKLLD RRTKVASCSG
SRASALSTAL RNAASLANAA ASAASSGSST RFQEYFKTTS SSTRNTVAAR FRAVASEASS
QSSGKTTYYC TDPYGYCDSN TLAYTLPSSN LIANCDIYYS YLPALTSSCH AQDQATTTLH
EFTHAPAVYS PGTDDYAYGY RASTALSASQ ALLNADTYAL FANGTPPPPP SPLHIHFQML
DTNNGYSREP
