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Database: UniProt
Entry: A0A074YQU7_AURPU
LinkDB: A0A074YQU7_AURPU
Original site: A0A074YQU7_AURPU 
ID   A0A074YQU7_AURPU        Unreviewed;       230 AA.
AC   A0A074YQU7;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=SCO1 protein {ECO:0000313|EMBL:KEQ89221.1};
GN   ORFNames=M438DRAFT_262400 {ECO:0000313|EMBL:KEQ89221.1};
OS   Aureobasidium pullulans EXF-150.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ89221.1, ECO:0000313|Proteomes:UP000030706};
RN   [1] {ECO:0000313|EMBL:KEQ89221.1, ECO:0000313|Proteomes:UP000030706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ89221.1,
RC   ECO:0000313|Proteomes:UP000030706};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
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; KL584974; KEQ89221.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074YQU7; -.
DR   STRING; 1043002.A0A074YQU7; -.
DR   HOGENOM; CLU_050131_0_2_1; -.
DR   OrthoDB; 169656at2759; -.
DR   Proteomes; UP000030706; 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|SAM:Phobius};
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:UP000030706};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         94
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT   BINDING         98
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT   BINDING         185
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT   DISULFID        94..98
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   230 AA;  26433 MW;  71670149F420D38C CRC64;
     MRYKTVEEAK SRYRFGPFSW QAGILFLSAG VGMGLYFRYE KERMARKRIA EHSKGVGRPL
     VGGPFQLIDQ DRKPFTEQNL KGKYSLVYFG FTHCPDICPE ELDKMAGMID NVKEKHGDVM
     RPVFITCDPA RDTPEVTKEY LKEFHDDLIG LTGEYEQVKA TCKAFRVYFS TPQNVLPGQD
     YLVDHSIYFY LMDPEGDFVE AIGRNFTVEQ ASRVINDHVA DWKGKIDKSA
//
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