ID MEP4_ARTBC Reviewed; 643 AA.
AC D4AX35;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Probable extracellular metalloproteinase 4;
DE EC=3.4.24.-;
DE AltName: Full=Fungalysin MEP4;
DE Flags: Precursor;
GN Name=MEP4; ORFNames=ARB_00762;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
CC -!- FUNCTION: Secreted metalloproteinase probably acting as a virulence
CC factor. {ECO:0000250}.
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:0000269|PubMed:21247460}.
CC -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR EMBL; ABSU01000016; EFE32240.1; -; Genomic_DNA.
DR RefSeq; XP_003012880.1; XM_003012834.1.
DR AlphaFoldDB; D4AX35; -.
DR SMR; D4AX35; -.
DR MEROPS; M36.001; -.
DR GlyCosmos; D4AX35; 4 sites, No reported glycans.
DR GeneID; 9522958; -.
DR KEGG; abe:ARB_00762; -.
DR eggNOG; ENOG502QTDC; Eukaryota.
DR HOGENOM; CLU_012703_3_0_1; -.
DR OMA; SKFATHR; -.
DR OrthoDB; 2786251at2759; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09596; M36; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR001842; Peptidase_M36.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR33478; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR PANTHER; PTHR33478:SF1; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF02128; Peptidase_M36; 1.
DR PRINTS; PR00999; FUNGALYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Virulence; Zinc; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..254
FT /evidence="ECO:0000250"
FT /id="PRO_0000397734"
FT CHAIN 255..643
FT /note="Probable extracellular metalloproteinase 4"
FT /id="PRO_0000397735"
FT REGION 47..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 437
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 643 AA; 70687 MW; 2641F0074F1FA681 CRC64;
MHGLLLAGLL ALPLNVLAHP TESHSSGVSR RAIDITSYRL PQISKYTKSD AVPKQDGESF
TTSSTGDDNV SSGDYVTTAT NWLKKTLPKA TYRLVNDHYI GDSGIGHVHF RQTAHGIDID
NTDFNVNIGR DGKVFSFGNS FYDGEIPKAN PMVKRDFSDP VNALHGAIQT LNLPVTAKPE
NVKAKPVEGK ENFKFEGTSG ALSDPKAQLV YLQKDGGLVL SWKVETDVGD NWLLTYVDAN
KNDQVHSVVD YVSAAEYQVY PWGINDPTEG NRTSIHLPWL KTLSTDWHID GKGWYPTTRG
NNAIAQENPT GHPEYENNYR PKSPLFIFKY PYSLAMTPPS SYRDASITQL FYTTNVYHDV
LYILGFNEKA GNFQINNWNK GGVGGDFAIL NSQDGSGVNN ANFATPPDGQ PGRMRMYTWN
ASTPERDGCF EAGIVIHEYT HGVSNRLTGG PENSRCLAAL ESGGMGEGWS DFFATAIRLK
PGDTRATDYT MGEWASNRPN GIRKYRYSTS LTTNPHMYVD ADGLTSVHAI GTIWASMLYE
LLWNLIDKHG KGDVTKIRPV LKNGVPTDGR HLAMKIVLDG MALQPCLPNF VQARDAILDA
DKNLTQGSNK CEIWKAFAKR GLGVGAAFNQ TKRTGSNELP AGC
//
