ID A0Z698_9GAMM Unreviewed; 231 AA.
AC A0Z698;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=SCO1/SenC family protein/methylamine utilization protein MauG, putative {ECO:0000313|EMBL:EAW40443.1};
GN ORFNames=MGP2080_08776 {ECO:0000313|EMBL:EAW40443.1};
OS marine gamma proteobacterium HTCC2080.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae.
OX NCBI_TaxID=247639 {ECO:0000313|EMBL:EAW40443.1, ECO:0000313|Proteomes:UP000004719};
RN [1] {ECO:0000313|EMBL:EAW40443.1, ECO:0000313|Proteomes:UP000004719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2080 {ECO:0000313|EMBL:EAW40443.1,
RC ECO:0000313|Proteomes:UP000004719};
RX PubMed=20472793; DOI=10.1128/jb.00511-10;
RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the
RT OM60/NOR5 clade of the Gammaproteobacteria.";
RL J. Bacteriol. 192:3842-3843(2010).
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:EAW40443.1}.
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DR EMBL; AAVV01000008; EAW40443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0Z698; -.
DR eggNOG; COG1999; Bacteria.
DR Proteomes; UP000004719; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004719};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..231
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002631208"
FT DOMAIN 57..230
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 95
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 101
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 194
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 95..101
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 231 AA; 25853 MW; F85DB6D39EEE9DB9 CRC64;
MIWPRANAMR QWLIGLLGWC AVSALAAPHQ HEPPVVLAPG YEDLQFEPPS AGSYQLPSMG
EAADGLILNT LGNAGRLHDY LGDKATVLSF IFTTCNDVNG CPLATYVMSG VQKAVLKDPD
LVDQVRIVSF SFDPEKDTPS VLGRYGDQFR AEGFDWEFLT TASEDALRPT LDAYDQWVIR
DYDEEGNYLG TMSHILRVYL IDSDRRIRNI YSTSYLHADT VVNDLRTLLM Q
//
