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Database: UniProt
Entry: A0A0D6PKX2_9PROT
LinkDB: A0A0D6PKX2_9PROT
Original site: A0A0D6PKX2_9PROT 
ID   A0A0D6PKX2_9PROT        Unreviewed;       221 AA.
AC   A0A0D6PKX2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Electron transport transmembrane protein Sco1/SenC/PrrC {ECO:0000313|EMBL:GAN82046.1};
GN   ORFNames=Aam_148_002 {ECO:0000313|EMBL:GAN82046.1};
OS   Acidocella aminolytica 101 = DSM 11237.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidocella.
OX   NCBI_TaxID=1120923 {ECO:0000313|EMBL:GAN82046.1, ECO:0000313|Proteomes:UP000032668};
RN   [1] {ECO:0000313|EMBL:GAN82046.1, ECO:0000313|Proteomes:UP000032668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=101 / DSM 11237 {ECO:0000313|Proteomes:UP000032668};
RA   Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT   "Whole genome sequence of Acidocella aminolytica 101 = DSM 11237.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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:GAN82046.1}.
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DR   EMBL; BANC01000145; GAN82046.1; -; Genomic_DNA.
DR   RefSeq; WP_048880431.1; NZ_FQVJ01000033.1.
DR   AlphaFoldDB; A0A0D6PKX2; -.
DR   STRING; 1120923.SAMN02746095_03084; -.
DR   OrthoDB; 9790194at2; -.
DR   Proteomes; UP000032668; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02968; SCO; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR003782; SCO1/SenC.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   PANTHER; PTHR12151:SF25; LDI DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02630; SCO1-SenC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Membrane {ECO:0000313|EMBL:GAN82046.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032668};
KW   Transmembrane {ECO:0000313|EMBL:GAN82046.1}.
FT   BINDING         96
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         100
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         185
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        96..100
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   221 AA;  23240 MW;  E8A76AC6AAB8733C CRC64;
     MRIIRNLGIG ICLALAVIIS IVAIDPSLLK LGQGNLSAPL PGSESGGQMA TTTNSGIPPG
     APIGGPFQLT NQLGQPVSDA TYRGKYMLVF FGYSHCPDEC PLTLQKMALT MNALGPLAQH
     IAPIFITIDP TRDTPPALKP YLSKFGPDLM GLTGSNAQIA GVAHEYAVAF NTNNLEASGA
     SVISHSTYIY LMGPDGKFLN LFPFTITVAQ LTSVLKAQIN P
//
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