ID   MEP1_VERA1              Reviewed;         284 AA.
AC   C9S5C6;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Extracellular metalloprotease VDBG_01143;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   ORFNames=VDBG_01143;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS985214; EEY15034.1; -; Genomic_DNA.
DR   RefSeq; XP_003009460.1; XM_003009414.1.
DR   AlphaFoldDB; C9S5C6; -.
DR   SMR; C9S5C6; -.
DR   MEROPS; M43.008; -.
DR   EnsemblFungi; EEY15034; EEY15034; VDBG_01143.
DR   GeneID; 9531043; -.
DR   KEGG; val:VDBG_01143; -.
DR   eggNOG; ENOG502RYKG; Eukaryota.
DR   HOGENOM; CLU_048726_0_0_1; -.
DR   OMA; HIVYENT; -.
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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..284
FT                   /note="Extracellular metalloprotease VDBG_01143"
FT                   /id="PRO_0000407207"
FT   ACT_SITE        201
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         204
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        236..263
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   284 AA;  30337 MW;  99AF3F5EBEA35710 CRC64;
     MLFKSLFVAA ATAVGVSGHV AREAPRTFGC GTHEPSAEHV GMSKVLAAQE ARVLESGNLT
     ARATINVNVY FHVVAASQTV ANGYLTDKMV TDQIAVLNRD FAPHDVAFRL AGTDRTVNTG
     WARDSNEIAM KRALRKGTYK DLNLYTQVSL TDNALGYAYF PTSGATSGST TFIRDGVSIK
     AQTVPGGSQA GFNLGKTGTH EVGHWLGLYH TFQGGCTGSG DQVSDTPAQA SFSSGCPIGR
     DSCPGQAGLD PIHNYMDYSD DSCYEEFTPG QDARIHSFWT TYRA