ID A0A1S1QG49_9ACTN Unreviewed; 315 AA.
AC A0A1S1QG49;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Electron transporter SenC {ECO:0000313|EMBL:OHV33773.1};
GN ORFNames=CC117_05225 {ECO:0000313|EMBL:OHV33773.1};
OS Parafrankia colletiae.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC Parafrankia.
OX NCBI_TaxID=573497 {ECO:0000313|EMBL:OHV33773.1, ECO:0000313|Proteomes:UP000179627};
RN [1] {ECO:0000313|Proteomes:UP000179627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cc1.17 {ECO:0000313|Proteomes:UP000179627};
RA Ghodhbane-Gtari F., Swanson E., Gueddou A., Morris K., Hezbri K., Ktari A.,
RA Nouioui I., Abebe-Akele F., Simpson S., Thomas K., Gtari M., Tisa L.S.,
RA Hurst S.;
RT "Sequence Frankia sp. strain CcI1.17.";
RL Submitted (JUL-2016) 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:OHV33773.1}.
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DR EMBL; MBLM01000130; OHV33773.1; -; Genomic_DNA.
DR RefSeq; WP_071086840.1; NZ_MBLM01000130.1.
DR AlphaFoldDB; A0A1S1QG49; -.
DR OrthoDB; 9790194at2; -.
DR Proteomes; UP000179627; 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:UP000179627}.
FT DOMAIN 106..273
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 145
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 149
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 235
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 145..149
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 315 AA; 32583 MW; 39360B140F6DAE09 CRC64;
MPRRSQTSTH HHHTTGRSRP ATTPSEGSAP DQTGQTGRSG HVSGPGGPGR AGRIGHPRRR
CAGLAFAAVL ALGATLGACS NGDGGAGVTI VDVGDGTNEG LHGVIPTERF AKPALGLTDT
EDRPFDLRTR TQGKITLLFF GYTMCPDVCP TTMADVAAAL DEVDQSVRDQ VSVVFVSTDP
ERDTAPVLDR WLNQFDESFI GVRGPFEKVK AQAEAIGVAL EEPRVQADGS VLVAHGSQVI
AFGRDARARV LYLAGTPVAD YVADLPVLTA ERLGPDESAT VSPSRTSDRD ATPGPAPAAT
AGTAGAAAAT REVTG
//
