MT2_COLGL
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}.
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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