ID   A0A166LLG6_9PEZI        Unreviewed;       283 AA.
AC   A0A166LLG6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Protein SCO1 (SCO1/SenC) {ECO:0000313|EMBL:KZL63672.1};
GN   ORFNames=CT0861_04140 {ECO:0000313|EMBL:KZL63672.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL63672.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL63672.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL63672.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|PIRNR:PIRNR037736}.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996, ECO:0000256|PIRNR:PIRNR037736}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZL63672.1}.
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DR   EMBL; LFIV01000339; KZL63672.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166LLG6; -.
DR   STRING; 708197.A0A166LLG6; -.
DR   OrthoDB; 169656at2759; -.
DR   Proteomes; UP000076552; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016531; F:copper chaperone activity; IEA:InterPro.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0006878; P:intracellular copper ion homeostasis; IEA:UniProtKB-UniRule.
DR   GO; GO:0008535; P:respiratory chain complex IV assembly; IEA:InterPro.
DR   CDD; cd02968; SCO; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR003782; SCO1/SenC.
DR   InterPro; IPR017276; Synth_of_cyt-c-oxidase_Sco1/2.
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   PIRSF; PIRSF037736; SCO1; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|PIRSR:PIRSR037736-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Membrane {ECO:0000256|PIRNR:PIRNR037736};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037736-1};
KW   Mitochondrion {ECO:0000256|PIRNR:PIRNR037736};
KW   Mitochondrion inner membrane {ECO:0000256|PIRNR:PIRNR037736};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076552}.
FT   REGION          33..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         148
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT   BINDING         152
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT   BINDING         239
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT   DISULFID        148..152
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   283 AA;  32367 MW;  F50CB68318B3F079 CRC64;
     MSHATSRLLW KSISSTSSTQ CRRCISQAAI PKQTRPTAAP NMFQTRPSPA QRRTKTYKTV
     EEAKSRYRAG PFSWKAGLLF VGTGVGLTWY FEYEKQRMER KRIADATKGM GRPKVGGPFE
     LIDQNGNKFT SEDMKGRYAL VYFGFTHCPD ICPDELDKMA QMYDLVEQKR PGSILPIFIT
     CDPERDNPAV VKEYLSEFHP KFIGLTGTYD EIKAMCKLYR VYFSTPQHVK PGQDYLVDHS
     IYFYLMDPEG DFVEALGRQH SPSAAAKIIL DHMNDWQGGW KKD
//