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Database: UniProt
Entry: D3D8M2_9ACTN
LinkDB: D3D8M2_9ACTN
Original site: D3D8M2_9ACTN 
ID   D3D8M2_9ACTN            Unreviewed;       205 AA.
AC   D3D8M2;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Electron transport protein SCO1/SenC {ECO:0000313|EMBL:EFC80730.1};
GN   ORFNames=FrEUN1fDRAFT_6144 {ECO:0000313|EMBL:EFC80730.1};
OS   Parafrankia sp. EUN1f.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Parafrankia.
OX   NCBI_TaxID=102897 {ECO:0000313|EMBL:EFC80730.1, ECO:0000313|Proteomes:UP000004777};
RN   [1] {ECO:0000313|EMBL:EFC80730.1, ECO:0000313|Proteomes:UP000004777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EUN1f {ECO:0000313|EMBL:EFC80730.1,
RC   ECO:0000313|Proteomes:UP000004777};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Tice H., Bruce D., Goodwin L.,
RA   Pitluck S., Larimer F., Land M.L., Hauser L., Beauchemin N., Sen A.,
RA   Fernandez M., Tisa L.;
RT   "The draft genome of Frankia sp. EUN1f.";
RL   Submitted (JAN-2010) 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:EFC80730.1}.
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DR   EMBL; ADGX01000138; EFC80730.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3D8M2; -.
DR   Proteomes; UP000004777; 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   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR12151:SF5; AT19154P; 1.
DR   PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   Pfam; PF02630; SCO1-SenC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR603782-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR603782-1}.
FT   DOMAIN          38..202
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         77
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         81
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         167
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        77..81
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   205 AA;  21057 MW;  5A213568B6376D25 CRC64;
     MVAAAIAMAG CGAGTDTPGT VVDLSQVEGA AGVRGITLAT PMPKPTTALT DTAGKPFDLR
     AATAGKLTLV FFGFTNCPDI CPTTMADLAA ARSLLGAADQ AQLRVVFVAT DPARDTPAAV
     RRWLGQFDSS FIGVTGTWDD VAHLADQLGV PVQAPRQGSD GSWTVTHGSQ VTAFSPDGVA
     RVAYQAGTSV EDYAHDIPLL LRGEV
//
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