ID   MEP2_VERA1              Reviewed;         276 AA.
AC   C9SSK8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Extracellular metalloprotease VDBG_07883;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   ORFNames=VDBG_07883;
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136;
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
CC   -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC       proteinaceous substrates. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M43B family. {ECO:0000305}.
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DR   EMBL; DS985224; EEY21773.1; -; Genomic_DNA.
DR   RefSeq; XP_003001624.1; XM_003001578.1.
DR   AlphaFoldDB; C9SSK8; -.
DR   SMR; C9SSK8; -.
DR   MEROPS; M43.008; -.
DR   PRIDE; C9SSK8; -.
DR   EnsemblFungi; EEY21773; EEY21773; VDBG_07883.
DR   GeneID; 9529679; -.
DR   KEGG; val:VDBG_07883; -.
DR   eggNOG; ENOG502RYKG; Eukaryota.
DR   HOGENOM; CLU_048726_0_0_1; -.
DR   OMA; RIYQTWD; -.
DR   Proteomes; UP000008698; 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; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR008754; Peptidase_M43.
DR   Pfam; PF05572; Peptidase_M43; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..276
FT                   /note="Extracellular metalloprotease VDBG_07883"
FT                   /id="PRO_0000407209"
FT   ACT_SITE        192
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         195
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        227..254
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   276 AA;  30250 MW;  DB5C0723DF468ED6 CRC64;
     MQSKFLWIAA ASAATAAAQV PARLCGTAQP TMDDLVIAAG LAAEGKDNRR GLHPEDPIVV
     PTLFHVLAIN ETVAGGYLTE KSLQDQLDVM NADFGPSNVI FNLTATTRTV NRRWAQDLDE
     IPMRRALRQG GQETLNIYFM PYVSGYLGYC TFPNFWDAGS DEFIYDGCAV LSDSLPGGSL
     ARYNLGRTAT HEIGHWFDLF HTFSGGCGCV GDMIHDTPAM LNATGGCPVG KDTCPDRPGL
     DPIHNYMDYS DDACMNEFTP GQNFRMRSAW YNIRTK