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Database: UniProt
Entry: W1QA40_OGAPD
LinkDB: W1QA40_OGAPD
Original site: W1QA40_OGAPD 
ID   W1QA40_OGAPD            Unreviewed;       270 AA.
AC   W1QA40;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Protein SCO1, mitochondrial {ECO:0000313|EMBL:ESW97264.1};
GN   ORFNames=HPODL_01367 {ECO:0000313|EMBL:ESW97264.1};
OS   Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS   Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=871575 {ECO:0000313|EMBL:ESW97264.1, ECO:0000313|Proteomes:UP000008673};
RN   [1] {ECO:0000313|EMBL:ESW97264.1, ECO:0000313|Proteomes:UP000008673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC   {ECO:0000313|Proteomes:UP000008673};
RX   PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA   Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA   Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA   Skryabin K.G.;
RT   "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT   DL1.";
RL   BMC Genomics 14:837-837(2013).
RN   [2] {ECO:0000313|Proteomes:UP000008673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC   {ECO:0000313|Proteomes:UP000008673};
RA   Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
RA   Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
RT   "Genome sequence of the methylotrophic yeast Hansenula polymorpha DL1.";
RL   Submitted (OCT-2013) 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:ESW97264.1}.
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DR   EMBL; AEOI02000009; ESW97264.1; -; Genomic_DNA.
DR   RefSeq; XP_013933349.1; XM_014077874.1.
DR   AlphaFoldDB; W1QA40; -.
DR   STRING; 871575.W1QA40; -.
DR   GeneID; 25770830; -.
DR   KEGG; opa:HPODL_01367; -.
DR   eggNOG; KOG2792; Eukaryota.
DR   HOGENOM; CLU_050131_0_1_1; -.
DR   OMA; IVAHMRP; -.
DR   OrthoDB; 169656at2759; -.
DR   Proteomes; UP000008673; Chromosome VI.
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:UP000008673};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        46..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         123
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT   BINDING         127
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT   BINDING         214
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT   DISULFID        123..127
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   270 AA;  30966 MW;  4E1552DFA9C7A0D9 CRC64;
     MSLNELKPND PKPEEEAPKK RKPLSRLPVG GPDYSKQTLK KNPIEFMTWK AVVVFVIFGS
     ALTYVFTSEK EKLKLRREAE QNRGVGKPLI GGPFNLIDTE GKPFTQENLK GKFSIIYFGF
     THCPDICPDE LDKLGLILDG LKSKYNIELQ PIFITCDPAR DSPEVVKEYL KDFHPSIIGL
     TGDYDEIKKC CKNYRVYFST PRNVKPGQDY LVDHSIFFYF MDPEGEFIDV LGRQYDAEEA
     IDKIKSNISV YQPRAEREKA KAGWLGFLYK
//
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