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Database: UniProt
Entry: A0A0T2QIT7_9SPHN
LinkDB: A0A0T2QIT7_9SPHN
Original site: A0A0T2QIT7_9SPHN 
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
//
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