ID A0A1Q5MD47_9ACTN Unreviewed; 562 AA.
AC A0A1Q5MD47;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=(2Fe-2S)-binding protein {ECO:0000313|EMBL:OKK11975.1};
GN ORFNames=AMK09_30415 {ECO:0000313|EMBL:OKK11975.1};
OS Streptomyces sp. CB02488.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703920 {ECO:0000313|EMBL:OKK11975.1, ECO:0000313|Proteomes:UP000186200};
RN [1] {ECO:0000313|EMBL:OKK11975.1, ECO:0000313|Proteomes:UP000186200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02488 {ECO:0000313|EMBL:OKK11975.1,
RC ECO:0000313|Proteomes:UP000186200};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKK11975.1}.
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DR EMBL; LIVO01000016; OKK11975.1; -; Genomic_DNA.
DR RefSeq; WP_073738182.1; NZ_LIVO01000016.1.
DR AlphaFoldDB; A0A1Q5MD47; -.
DR STRING; 1703920.AMK09_30415; -.
DR OrthoDB; 159930at2; -.
DR Proteomes; UP000186200; 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:UP000186200}.
FT DOMAIN 359..436
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT REGION 1..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..214
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 57852 MW; 13FE3B68BC8C715A CRC64;
MSNEDHTEQH GGWEPIPQSG EYDGESTAFV HLPPEDLANI PLAAPGQGYV PPMILPLTPA
AGIDPAATGS WVVRTPDGQD SRGDGQDHAP GAEQPAPEAV HWPDPNQQQA PYGYQQTPYQ
PHPPAEQYPD RYREDRAATG QWNFAESAES AEPAGHTGQW QIPVADGDLP EESGEFSPSA
AAAWYADRTP PATLPGGAPA PWATREPEPP AGDSAPPQGA DHDGTPDAPD GAADAHEVPP
EAALQDASQP AMEHPGPAEP VTEPGTEPVA EPAADPVAEP VAEDAPDTGA TDAETAPDTD
VTAPDATDTP AEADATDPGV TEHAPTPDLA PDLDADPDVT DPEAAPAPRL DLPSEHPSVS
YALHVNGVDR PVTGAWIGES LLYVLRERLG LAGAKDGCSQ GECGACNVQV DGRLVASCLV
PAATAAGSEV RTVEGLAVDG EPSDVQRALA DCGAVQCGFC IPGMAMTVHD LLEGNHAPSE
LETRQALCGN LCRCSGYRGV LDAVNEVIAG REAASAPAPE SAEQSTGQST EQSAKQDEAR
IPHQAPPGAG SVQAHLQDGG MA
//