ID A0A255HZT4_9BURK Unreviewed; 194 AA.
AC A0A255HZT4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=SCO family protein {ECO:0000313|EMBL:OYO32253.1};
GN ORFNames=CD932_14780 {ECO:0000313|EMBL:OYO32253.1};
OS Janthinobacterium sp. PC23-8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=2012679 {ECO:0000313|EMBL:OYO32253.1, ECO:0000313|Proteomes:UP000216749};
RN [1] {ECO:0000313|EMBL:OYO32253.1, ECO:0000313|Proteomes:UP000216749}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC23-8 {ECO:0000313|EMBL:OYO32253.1,
RC ECO:0000313|Proteomes:UP000216749};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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:OYO32253.1}.
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DR EMBL; NJGY01000001; OYO32253.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255HZT4; -.
DR OrthoDB; 9790194at2; -.
DR Proteomes; UP000216749; 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:SF27; PUTATIVE-RELATED; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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}.
FT DOMAIN 32..194
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 70
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 74
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 159
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 70..74
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 194 AA; 21441 MW; 25A13E2172748B23 CRC64;
MKKLFCLLLT TLLLAGCGKP EAPKPVFQNT DVTGLGYARE FALTDHTGKP RTLADYKGKV
VLMFFGYTQC PDVCPTTMAD MAQVMKDMGP QADQVQVLFV TVDPERDTQA LLAEYVPAFD
KRFVGLYGDA AATARVAKEF KVYYAKVEGE TDSSYTVDHT AGTYVFDRQG KIRLFVRHGE
KPAAIAHDLK LLLS
//