ID I4YFN2_WALMC Unreviewed; 219 AA.
AC I4YFN2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=SCO1 protein {ECO:0000313|EMBL:EIM22774.1};
DE Flags: Fragment;
GN ORFNames=WALSEDRAFT_16755 {ECO:0000313|EMBL:EIM22774.1};
OS Wallemia mellicola (strain ATCC MYA-4683 / CBS 633.66) (Wallemia sebi (CBS
OS 633.66)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=671144 {ECO:0000313|EMBL:EIM22774.1, ECO:0000313|Proteomes:UP000005242};
RN [1] {ECO:0000313|EMBL:EIM22774.1, ECO:0000313|Proteomes:UP000005242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4683 / CBS 633.66 {ECO:0000313|Proteomes:UP000005242};
RX PubMed=22326418; DOI=10.1016/j.fgb.2012.01.007;
RA Padamsee M., Kumar T.K.A., Riley R., Binder M., Boyd A., Calvo A.M.,
RA Furukawa K., Hesse C., Hohmann S., James T.Y., LaButti K., Lapidus A.,
RA Lindquist E., Lucas S., Miller K., Shantappa S., Grigoriev I.V.,
RA Hibbett D.S., McLaughlin D.J., Spatafora J.W., Aime M.C.;
RT "The genome of the xerotolerant mold Wallemia sebi reveals adaptations to
RT osmotic stress and suggests cryptic sexual reproduction.";
RL Fungal Genet. Biol. 49:217-226(2012).
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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DR EMBL; JH668227; EIM22774.1; -; Genomic_DNA.
DR RefSeq; XP_006957169.1; XM_006957107.1.
DR AlphaFoldDB; I4YFN2; -.
DR STRING; 671144.I4YFN2; -.
DR GeneID; 18470704; -.
DR KEGG; wse:WALSEDRAFT_16755; -.
DR eggNOG; KOG2792; Eukaryota.
DR HOGENOM; CLU_050131_0_3_1; -.
DR InParanoid; I4YFN2; -.
DR OMA; IVAHMRP; -.
DR OrthoDB; 169656at2759; -.
DR Proteomes; UP000005242; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:InterPro.
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:InterPro.
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 Metal-binding {ECO:0000256|PIRSR:PIRSR037736-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005242}.
FT BINDING 81
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT BINDING 85
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT BINDING 178
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT DISULFID 81..85
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EIM22774.1"
SQ SEQUENCE 219 AA; 24790 MW; FF92B17EB98440CB CRC64;
PFNWVSASLF VATGVGLYYY FNKAKAEVEE SKKRKISESE KLGKPKIGGP FSLIDAKTEN
SFTHENLLGR FSLVYFGFTN CPDICPDELD KMGTVVDRVV DAKLGQIVQP VFISCDPARD
TTAQTRKYLE GEFLIRFHPR MVGLTGPWEN VRAACKVYRV YFSTPPNISP NEDYLVDHSI
FMYLMDPNGE FVEAFGKNTT AEQMADKVLS YTESYVQNK
//
