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 03-AUG-2022, entry version 81.
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;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL84418.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AAHF01000016; EAL84418.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_746456.2; XM_741363.2.
DR AlphaFoldDB; Q4WA45; -.
DR SMR; Q4WA45; -.
DR MEROPS; M35.002; -.
DR GeneID; 3503899; -.
DR KEGG; afm:AFUA_4G02700; -.
DR eggNOG; ENOG502SGF5; Eukaryota.
DR HOGENOM; CLU_039313_1_1_1; -.
DR InParanoid; Q4WA45; -.
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_0000407136"
FT CHAIN 173..450
FT /note="Neutral protease 2 homolog AFUB_070680"
FT /id="PRO_0000407137"
FT REGION 364..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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
