ID MEP1_ASPFC Reviewed; 322 AA.
AC B0XPZ1;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-MAY-2023, entry version 56.
DE RecName: Full=Extracellular metalloprotease AFUB_008060;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN ORFNames=AFUB_008060;
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 144.89 / FGSC A1163 / CEA10;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC proteinaceous substrates. Plays a pivotal role as a pathogenicity
CC determinant during infections and contributes to the ability of the
CC pathogen to persist within the mammalian host (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M43B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDP56105.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DS499594; EDP56105.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; B0XPZ1; -.
DR SMR; B0XPZ1; -.
DR PhylomeDB; B0XPZ1; -.
DR Proteomes; UP000001699; 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:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04275; ZnMc_pappalysin_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR008754; Peptidase_M43.
DR PANTHER; PTHR47466; -; 1.
DR PANTHER; PTHR47466:SF1; METALLOPROTEASE MEP1 (AFU_ORTHOLOGUE AFUA_1G07730)-RELATED; 1.
DR Pfam; PF05572; Peptidase_M43; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Secreted; Signal; Virulence; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..322
FT /note="Extracellular metalloprotease AFUB_008060"
FT /id="PRO_0000407197"
FT ACT_SITE 234
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 272..299
FT /evidence="ECO:0000250"
SQ SEQUENCE 322 AA; 35748 MW; 581AF473138DD473 CRC64;
MLPFNSCVYV LLIISLMSNC RALCRATALQ GRSLCATGGP DAAFRAEHER LSAFESRPSS
GSYDMRRALD PIEIETWFHI VSGETDADLV TDEMVILQLH YLQKAYEKAS ISYRLKGVTR
HINETWARNG DDSAMKKALR RGGYSTLNVY FQTNLQPPST TDFARWTSDG DNRHAYNSDL
APPSVLGFCT LPDPSINSSS PRSSYSKDGC NVLAKTMPGG PMTHYNRGGT AIHEIGHWNG
LLHTFEGESC SEDNAGDYIA DTPQQSVPTD GCPSQKDSCP DSPGLDDIHN FMDYSSDDCY
ASFTSNQLKR MRDMWFSMRK GK
//
