ID A0A2U3A0P3_9ACTN Unreviewed; 662 AA.
AC A0A2U3A0P3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=2Fe-2S ferredoxin-type domain-containing protein {ECO:0000259|PROSITE:PS51085};
GN ORFNames=DI272_31080 {ECO:0000313|EMBL:PWI18096.1};
OS Streptomyces sp. Act143.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2200760 {ECO:0000313|EMBL:PWI18096.1, ECO:0000313|Proteomes:UP000245455};
RN [1] {ECO:0000313|EMBL:PWI18096.1, ECO:0000313|Proteomes:UP000245455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Act143 {ECO:0000313|EMBL:PWI18096.1,
RC ECO:0000313|Proteomes:UP000245455};
RA Valanrebinro G., Kumari S., Rameshkumar N.;
RT "Actinomycin D producing novel Streptomyces isolated from the rhizosphere
RT of saline tolerant kaipad rice and its draft genome analysis.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:PWI18096.1}.
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DR EMBL; QFRX01000001; PWI18096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U3A0P3; -.
DR OrthoDB; 159930at2; -.
DR Proteomes; UP000245455; Unassembled WGS sequence.
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:UP000245455}.
FT DOMAIN 462..539
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 65218 MW; 434034AAF1713856 CRC64;
MTDDQHGEGT APHSGGRWDP LPQGDYDDGA TAFVKLPEGG IDALLASDSP LAAPGHGYVP
PQITVTPGGA AGTDPAATGT WAAAPVGGAQ WPDPNAVPQD GHAGQGGHGA GNDQFTYHPG
ATGQWTFQDA AESAPAPGHD VTGQWSIPVA GGDLPDESGE FTTSSLVEQW GGTPPATLPG
GAPAPWATQA GQPWDPQTPE TGPGHAAPVG DGDREAAGGG HGHVAPGGAV GDEAAVDAHA
QAPIAAHPGT HAVADAPDHQ TADQHAPDAD VHARVQADPD EPAPGQPFDA APASPQAPAA
QAHGGAQVLP DGAPVPDAAP APDGPQVHAS EGPPAAAADV FDAFEGAPAA AADAFEGAPA
AAADAFEGAP GAVTHASEGA PAAAASQAAP RDGEDAAAPE TPEGAQGAAE GAEEASEAGA
EHTPADGGDT EPDAEGAPEH AADSGAPAEQ SPGLPGEEHP LAGYVLRVNG VDRPVTDAWI
GESLLYVLRE RLGLAGAKDG CSQGECGACN VQVDGRLVAS CLVPAVTAAG SEVRTVEGLA
EDGRPSDVQR ALARCGAVQC GFCVPGMAMT VHDLLEGNPA PTELETRQAL CGNLCRCSGY
RGVVDAVKEV VAEREAHAAG DSESDGDEAR IPHQAGPGGG GVNPSAFEPR HDQAYGPDGG
QA
//