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Database: UniProt
Entry: A0A0A0M9G1_9GAMM
LinkDB: A0A0A0M9G1_9GAMM
Original site: A0A0A0M9G1_9GAMM 
ID   A0A0A0M9G1_9GAMM        Unreviewed;       216 AA.
AC   A0A0A0M9G1;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN   ORFNames=N791_02285 {ECO:0000313|EMBL:KGO99688.1};
OS   Lysobacter defluvii IMMIB APB-9 = DSM 18482.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1385515 {ECO:0000313|EMBL:KGO99688.1, ECO:0000313|Proteomes:UP000030003};
RN   [1] {ECO:0000313|EMBL:KGO99688.1, ECO:0000313|Proteomes:UP000030003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMMIB APB-9 {ECO:0000313|EMBL:KGO99688.1,
RC   ECO:0000313|Proteomes:UP000030003};
RA   Wang Q., Wang G.;
RT   "Genomic analysis of Lysobacter defluvii.";
RL   Submitted (AUG-2013) 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:KGO99688.1}.
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DR   EMBL; AVBH01000006; KGO99688.1; -; Genomic_DNA.
DR   RefSeq; WP_027069478.1; NZ_AVBH01000006.1.
DR   AlphaFoldDB; A0A0A0M9G1; -.
DR   STRING; 1385515.GCA_000423325_01035; -.
DR   eggNOG; COG1999; Bacteria.
DR   OrthoDB; 9790194at2; -.
DR   Proteomes; UP000030003; 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:UP000030003}.
FT   DOMAIN          45..216
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         83
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         87
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         177
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        83..87
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   216 AA;  23467 MW;  C040CFA64376E1A5 CRC64;
     MFNRTALAVV IIAVAAGLGL VAAQRFFQQA EVPSRWPQTS AVRLFEPARE IPPFSLRQSD
     GTDLLPGELH GHWTLVFIGF THCPDVCPMT LAQLSQAQKE WEALPEATRP RVLFVSVDPE
     RDTPDRIGEY AHHFHPDTLA ATADIPALED FTRSLSLVFA KVPLSADAPA DQYTVDHSAS
     IAVLDPQGRM TGVVQPPLDI PAIAADMRAL TEASAP
//
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