ID A0A0U3PRW8_9ACTN Unreviewed; 605 AA.
AC A0A0U3PRW8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=(2Fe-2S)-binding protein {ECO:0000313|EMBL:ALV35410.1};
GN ORFNames=AS200_27700 {ECO:0000313|EMBL:ALV35410.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV35410.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV35410.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV35410.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP013743; ALV35410.1; -; Genomic_DNA.
DR RefSeq; WP_058925020.1; NZ_CP013743.1.
DR AlphaFoldDB; A0A0U3PRW8; -.
DR STRING; 1725411.AS200_27700; -.
DR KEGG; scx:AS200_27700; -.
DR OrthoDB; 159930at2; -.
DR Proteomes; UP000068029; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR PANTHER; PTHR44379; OXIDOREDUCTASE WITH IRON-SULFUR SUBUNIT; 1.
DR PANTHER; PTHR44379:SF8; XANTHINE DEHYDROGENASE IRON-SULFUR-BINDING SUBUNIT XDHC-RELATED; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000068029}.
FT DOMAIN 404..481
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..238
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 60346 MW; 92491DEB998CE0E9 CRC64;
MTDDQHGEGT PPQSGGRWDP LPQGDYDDGA TAFVKLPEGG IDALLAAADS PLAARGHGYV
PPQIQSTPGP GADPEAPGAW GAPADGGQWP DPNAVPHGAG NDQFTYNPAT TQQWAYEEPP
RAEGGPGSGQ HVTGQWSIPV AGGDLPDESG EFTTSSLVQQ WGGTPPATLP GGAAAPWATE
GAGLPWGQEA AELTGTDGAG RPLASAAGTD TAPAPADGGQ PYGHPGAPPM PGGHGPDAAP
GPHQPLHREP TGHGPADEDG TGYAPDAARG HVGEEPREAS APAGGAGQDD GPAGPPAAGH
GGSYASDAAT AASQAVHDAR EAARVAEAAQ EATEGAEGPV EAFTAPGDGA EPESAAAGAA
DAPDTADTAP AAEGPDPEAA PDEDTPDTSE EPPPALPGEE HPLAAYVLRV NGVERPVSDA
WIGESLLYVL RERLGLAGAK DGCSQGECGA CNVQVDGRLV ASCLVPAVTA AGSEVRTVEG
LAEDGRPSDV QRALARCGAV QCGFCVPGMA MTVHDLLEGN PAPTELETRQ ALCGNLCRCS
GYRGVVDAVQ EVVAERRAHH AADAEHDGDE ARIPHQAGPG AGGVNPSAFD PAPHDQAYGQ
DGGQA
//
