MT1_COLGL
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}.
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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