ID A0A1N7NHQ0_9BACT Unreviewed; 222 AA.
AC A0A1N7NHQ0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:SIS97943.1};
GN ORFNames=SAMN05421761_11033 {ECO:0000313|EMBL:SIS97943.1};
OS Belliella pelovolcani.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Belliella.
OX NCBI_TaxID=529505 {ECO:0000313|EMBL:SIS97943.1, ECO:0000313|Proteomes:UP000186026};
RN [1] {ECO:0000313|EMBL:SIS97943.1, ECO:0000313|Proteomes:UP000186026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46698 {ECO:0000313|EMBL:SIS97943.1,
RC ECO:0000313|Proteomes:UP000186026};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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DR EMBL; FTOP01000010; SIS97943.1; -; Genomic_DNA.
DR RefSeq; WP_076501748.1; NZ_FTOP01000010.1.
DR AlphaFoldDB; A0A1N7NHQ0; -.
DR STRING; 529505.SAMN05421761_11033; -.
DR OrthoDB; 9811998at2; -.
DR Proteomes; UP000186026; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; SCO1 PROTEIN HOMOLOG; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR603782-1}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..216
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 93
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 97
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 182
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 93..97
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 222 AA; 25516 MW; B3C389F6DCB2E7FC CRC64;
MKGLRILQGF VLLCILMIPV LIIVFLKTMS TNSYDIPIYY EAGVDNPFLE CDFEDGKQHR
IPEFRFTSHL NQEIGSLEMK GKVTIVDFFF TSCPSICPVM STEMERVDDV FRQNDDVQIY
SISIDPEYDT PEILQSYADL HRATPGKWHF LTGDKSEIYD LARCGFILPT IDGEGVPDDF
VHSDKFVLVD EEGRIRGYYS GTNREEVDRL IVETKILLYG KE
//
