MEP1_UNCRE
ID MEP1_UNCRE Reviewed; 269 AA.
AC C4K014;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Extracellular metalloprotease UREG_07765;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN ORFNames=UREG_07765;
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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; CH476619; EEP82900.1; -; Genomic_DNA.
DR RefSeq; XP_002582992.1; XM_002582946.1.
DR AlphaFoldDB; C4K014; -.
DR SMR; C4K014; -.
DR EnsemblFungi; EEP82900; EEP82900; UREG_07765.
DR GeneID; 8442292; -.
DR KEGG; ure:UREG_07765; -.
DR VEuPathDB; FungiDB:UREG_07765; -.
DR eggNOG; ENOG502RYKG; Eukaryota.
DR HOGENOM; CLU_048726_0_0_1; -.
DR InParanoid; C4K014; -.
DR OrthoDB; 1569419at2759; -.
DR Proteomes; UP000002058; 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..269
FT /note="Extracellular metalloprotease UREG_07765"
FT /id="PRO_0000407206"
FT REGION 207..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 220..246
FT /evidence="ECO:0000250"
SQ SEQUENCE 269 AA; 28951 MW; C79B8EAB14A5C73B CRC64;
MRLSVSLLAL AFGSLVAAAP NTKPRTCGSK PSMEFLAKSA EFAAKEASGE LLNSLATIEV
ETYFHVVASG RTPSQGYLSD AMLANQLRVM NSDYGPHGIQ FNLVRTTRTV NANWARDGDE
LGMKRALRQG GYNALNVYFL GDLGSLLGYC YFPTNASPGS TAFIRDGCVV VGQSVPGGNI
SNYNLGKTAT HEVGHWFGGC FGSGDGVSDT PPQRSSTQGC PSSRDSCPGG GVDPIHNYMD
YSYDVCMNQF TSGQRTRIYN MWNQYRARG
