ID MT1_COLGL Reviewed; 26 AA. AC Q99334; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 03-AUG-2022, entry version 53. DE RecName: Full=Metallothionein-like protein CAP3; GN Name=CAP3; 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 / MRNA]. 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 -!- MISCELLANEOUS: The seven cysteines bind six copper (cuprous) ions. CC {ECO:0000250}. 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; U18756; AAA77679.1; -; Genomic_DNA. DR EMBL; L22549; AAA74033.1; -; mRNA. DR PIR; S55029; S55029. DR AlphaFoldDB; Q99334; -. 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..26 FT /note="Metallothionein-like protein CAP3" FT /id="PRO_0000197362" 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 12 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P02807" FT BINDING 12 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P02807" FT BINDING 14 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="6" FT /evidence="ECO:0000250|UniProtKB:P02807" FT BINDING 18 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P02807" FT BINDING 18 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="3" FT /evidence="ECO:0000250|UniProtKB:P02807" FT BINDING 20 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P02807" FT BINDING 23 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P02807" FT BINDING 23 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P02807" SQ SEQUENCE 26 AA; 2519 MW; C1D173B2921BDCFC CRC64; MSGCGCASTG TCHCGKDCTC AGCPHK //