ID G2Y8Z7_BOTF4 Unreviewed; 296 AA.
AC G2Y8Z7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Sco1 protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BofuT4_P029490.1 {ECO:0000313|EMBL:CCD49073.1};
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD49073.1, ECO:0000313|Proteomes:UP000008177};
RN [1] {ECO:0000313|Proteomes:UP000008177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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DR EMBL; FQ790300; CCD49073.1; -; Genomic_DNA.
DR AlphaFoldDB; G2Y8Z7; -.
DR STRING; 999810.G2Y8Z7; -.
DR eggNOG; KOG2792; Eukaryota.
DR HOGENOM; CLU_050131_0_1_1; -.
DR InParanoid; G2Y8Z7; -.
DR Proteomes; UP000008177; Unplaced contigs.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd02968; SCO; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12151:SF5; AT19154P; 1.
DR PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|PIRSR:PIRSR603782-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 85..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 161
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 165
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 257
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 161..165
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 296 AA; 32627 MW; C57A2BBEA4F0FD68 CRC64;
MLSTISKTGA KNAKTFGLQC QRLSTICASR IPRGVQNKAC LSGLNGFNGS ASAGVKTVGL
GEGSAGRRGY KTVQEQRSRY KSGPFSWTAG VLFLGAGAGL IFYFRYEKAR MERKRIAEAA
KGVGRPKVGG PFELLDHKGG KFSSEDMKGK YSLVYFGFTH CPDICPEELD KMAQMIDLIN
NSPTRTSSTP ALLPIFITCD PARDTPAVLA TYLAEFHPSI IGLTGTWEQI KDICKKYRVY
FSTPEGVQKG QDYLVDHSIY FYLMDPEGDF VEAIGRQHSP EQAARIIQEH VGDWKR
//
