ID MT2_COLGL Reviewed; 27 AA. AC Q00369; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 03-AUG-2022, entry version 49. DE RecName: Full=Metallothionein-like protein CAP5; GN Name=CAP5; OS Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum; OC Colletotrichum gloeosporioides species complex. OX NCBI_TaxID=474922; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Conidium; RX PubMed=7770033; DOI=10.1007/bf00293196; RA Hwang C.-S., Kolattukudy P.E.; RT "Isolation and characterization of genes expressed uniquely during RT appressorium formation by Colletotrichum gloeosporioides conidia induced by RT the host surface wax."; RL Mol. Gen. Genet. 247:282-294(1995). CC -!- DEVELOPMENTAL STAGE: Expressed in the conidium only during the process CC of appressorium formation induced by avocado surface wax. CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 8 family. CC {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; U18757; AAA77680.1; -; Genomic_DNA. DR PIR; S55030; S55030. DR AlphaFoldDB; Q00369; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. PE 2: Evidence at transcript level; KW Copper; Metal-binding; Metal-thiolate cluster. FT PEPTIDE 1..27 FT /note="Metallothionein-like protein CAP5" FT /id="PRO_0000197363" FT REGION 1..27 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 10..27 FT /note="Cys residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 4 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P02807" FT BINDING 6 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P02807" FT BINDING 6 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P02807" FT BINDING 9 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P02807" FT BINDING 9 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P02807" FT BINDING 13 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="6" FT /evidence="ECO:0000250|UniProtKB:P02807" FT BINDING 20 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P02807" FT BINDING 20 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="6" FT /evidence="ECO:0000250|UniProtKB:P02807" FT BINDING 22 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P02807" FT BINDING 22 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P02807" FT BINDING 25 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P02807" FT BINDING 25 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P02807" SQ SEQUENCE 27 AA; 2549 MW; 20BC8D61413B3A95 CRC64; MAPCSCKSCG TSCAGSCTSC SCGSCSH //