ID A0A0T2QIT7_9SPHN Unreviewed; 179 AA.
AC A0A0T2QIT7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Electron transporter SenC {ECO:0000313|EMBL:KRA84614.1};
GN ORFNames=ASD76_04665 {ECO:0000313|EMBL:KRA84614.1};
OS Altererythrobacter sp. Root672.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=1736584 {ECO:0000313|EMBL:KRA84614.1, ECO:0000313|Proteomes:UP000051125};
RN [1] {ECO:0000313|EMBL:KRA84614.1, ECO:0000313|Proteomes:UP000051125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root672 {ECO:0000313|EMBL:KRA84614.1,
RC ECO:0000313|Proteomes:UP000051125};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA84614.1, ECO:0000313|Proteomes:UP000051125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root672 {ECO:0000313|EMBL:KRA84614.1,
RC ECO:0000313|Proteomes:UP000051125};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRA84614.1}.
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DR EMBL; LMHH01000001; KRA84614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T2QIT7; -.
DR STRING; 1736584.ASD76_04665; -.
DR OrthoDB; 9790194at2; -.
DR Proteomes; UP000051125; 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; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051125}.
FT DOMAIN 18..178
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 56
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 60
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 143
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 56..60
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 179 AA; 19254 MW; 35553042153FD7DF CRC64;
MLFVREPAQP AQMRAGAFDP PRLAPDFALR GSDGSEVTLA RYRGKVVLLT FGFTYCAAVC
PTTLATLAQA RNSLGGAADK VQVIFVTVDP DRDNAAHMRK YLAAFDDSFI GATDAPEVLA
AVREDYGVTA ERQGTGPNYA MAHTSSIFLI DQAGRLRAMM PFGHDATDFI HDVALLLEG
//