MEP3_ARTBC
ID MEP3_ARTBC Reviewed; 633 AA.
AC D4AL88;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Probable extracellular metalloproteinase 3;
DE EC=3.4.24.-;
DE AltName: Full=Fungalysin MEP3;
DE Flags: Precursor;
GN Name=MEP3; ORFNames=ARB_05085;
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; ABSU01000002; EFE36147.1; -; Genomic_DNA.
DR RefSeq; XP_003016792.1; XM_003016746.1.
DR AlphaFoldDB; D4AL88; -.
DR SMR; D4AL88; -.
DR MEROPS; M36.001; -.
DR PRIDE; D4AL88; -.
DR EnsemblFungi; EFE36147; EFE36147; ARB_05085.
DR GeneID; 9526269; -.
DR KEGG; abe:ARB_05085; -.
DR eggNOG; ENOG502QTDC; Eukaryota.
DR HOGENOM; CLU_012703_3_0_1; -.
DR OMA; WALIEAH; -.
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 Gene3D; 1.10.390.10; -; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR001842; Peptidase_M36.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF02128; Peptidase_M36; 1.
DR PRINTS; PR00999; FUNGALYSIN.
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..246
FT /evidence="ECO:0000250"
FT /id="PRO_0000397730"
FT CHAIN 247..633
FT /note="Probable extracellular metalloproteinase 3"
FT /id="PRO_0000397731"
FT ACT_SITE 430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 633 AA; 69248 MW; 7360CAECB241D345 CRC64;
MHGLLLAGLL ALPMNVLAHP AEQHASNVLS RRGVDIESFR LPLKAKYMDS DATAQKIQAM
SFSKDDDYVS TATKLVKSTF PKSTFRVVDD HYIGTNGIGH VHFKQTAHGL DIDNSDFNVN
IGRDGKVFSF GNSFFTGEIP KENPMVKRAF SDPVKALKGA VKALNLPVKS DNAKAKTAAG
KESFEFMGTT GALSAPKANL VYLQKEDGSL ALTWKVETDV GDNWLLTYVD AHNSETVHNV
VDYVASAEYK VFAWGLNDPT EGNPTSIRDP WTDASPYTWN SDGMTKYPTT RGNNAIAQDN
PTGGSTYINN YRPQSPNLIF SYPWSPTATP PSSYKDFSIT QLFYTTNRYH DLLYSFGFNE
AAGNFQVNNG NKGGKGNDFA IVNAQDGSGT NNANFATPPD GSPGRMRMYN WTTARPNRDG
CLEAGIVIHE YTHGLSNRLC GGPANSACLN ALESGGMGEG WGDFYATAIR LKPRDTKDTN
YSMGAWAANN PKGIRAYLYS TNLQTNPYMY TSVNSLREVH QIGTVWASML YDLMWALIEA
HGGTYSADPV FRNGVPQDGR HLTMKLVMDG MALQPCNPNF VQARDAILDA DRALTNSANK
CTIWKAFAKR GLGYGAKYDA RNRTGSNKLP PGC