ID A0A080WJP5_TRIRC Unreviewed; 303 AA.
AC A0A080WJP5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Mitochondrial metallochaperone Sco1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=TERG_02692 {ECO:0000313|EMBL:KFL60937.1};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:KFL60937.1, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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}.
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DR EMBL; GG700649; KFL60937.1; -; Genomic_DNA.
DR RefSeq; XP_003237984.1; XM_003237936.1.
DR AlphaFoldDB; A0A080WJP5; -.
DR GeneID; 10376939; -.
DR VEuPathDB; FungiDB:TERG_02692; -.
DR eggNOG; KOG2792; Eukaryota.
DR OrthoDB; 169656at2759; -.
DR Proteomes; UP000008864; 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:UP000008864}.
FT REGION 41..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 159
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT BINDING 163
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT BINDING 252
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT DISULFID 159..163
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 303 AA; 34322 MW; 63B84BFC543DAD82 CRC64;
MASASMASTL LRSLRAAQQC AHRPCQIRQY SQLLSRTAET TRHSLRPLSR QARPDRSNAF
STSTVRPAKT IEQLKARSST GPFSWKSAVL FVLTGAGMIV YFQYEKARLE RERIVEMSKG
VGKPRVGGPF VLKDLNGETF TEENLKGKYS FVYFGFTHCP DICPDELDKM AEIIDEVRAR
SNGQEVMRPV FITCDPARDS PEVLRGYLNE FHKDIIGLTG TYEQVKDVCR QYRVYFSTPQ
NIKPGEDYLV DHSIYFYLMD PEGDFVECIG RQDTPQTASK VILDHIGDWK RAGKPLDVTP
SSK
//
