ID MEP5_ARTOC Reviewed; 632 AA.
AC C5FX29;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 22-FEB-2023, entry version 54.
DE RecName: Full=Extracellular metalloproteinase 5;
DE EC=3.4.24.-;
DE AltName: Full=Fungalysin MEP5;
DE Flags: Precursor;
GN Name=MEP5; ORFNames=MCYG_07688;
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480;
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEQ34869.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DS995707; EEQ34869.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; XP_002843905.1; XM_002843859.1.
DR AlphaFoldDB; C5FX29; -.
DR SMR; C5FX29; -.
DR MEROPS; M36.001; -.
DR GlyCosmos; C5FX29; 3 sites, No reported glycans.
DR GeneID; 9228027; -.
DR eggNOG; ENOG502QTDC; Eukaryota.
DR HOGENOM; CLU_012703_3_0_1; -.
DR OrthoDB; 2786251at2759; -.
DR Proteomes; UP000002035; 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 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Virulence; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..244
FT /evidence="ECO:0000250"
FT /id="PRO_0000384085"
FT CHAIN 245..632
FT /note="Extracellular metalloproteinase 5"
FT /id="PRO_0000384086"
FT ACT_SITE 428
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 632 AA; 69546 MW; E39A4963B743DEDB CRC64;
MHGLLLAAGL LSLPLHVLAH PQPGTSLAGR AVDLNAYRMA DRASYMSSDE MQAQQPHIAS
VSAGGYVETA TEVVKRVMPG MTFRLVDDHY VGVSGISHVY FRQTMHGMDI DNSDFNVNIG
KDGKVLSYGN SFYTGPAPDK APMVKRDFSD PMQALHGVRK ALNLPITADK ATVKTVNEHE
VTFMGTTGAL SDPSAKLCYM AKEDGSLALT WRVETDMGDN WLLSYVDAKS TDQVHNVVDY
VSHATYQVYR WPIPDPTEGK REILENPWNL RTSPFTWISD GKNNYTTTRG NNAIAQANPD
GGNEYLNNYR PNNKNLKFEY PYSPNMSPPK TYIDASITQL FYSANMVHDL YYMLGFTEKA
GNFQVNNRGQ GGKGNDFVIL NAQDGSGTNN ANFATPPDGQ PGRMRVYIWT KAQPARDSSF
EAGTVIHEYT HGLSNRLCGG PANSACLNGL ESGGMGEGWG DFFATAIRLK PNDNRNANYV
HGEWVNNSPK GNRLFPYSTS LKTNPLVYTS CNKYNEVHAI GTVWASILYE VLWNLIDKHG
KNDGPTPVFE NGVPKDGKYL SLKLVLDGMA IQPCKPNFVQ ARNAIIDADK NLTKGANKCE
LWKAFAKRGL GTGAKYDPKN RTGSTAVPKE CQ
//
