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Database: UniProt
Entry: F6ELY0_HOYSD
LinkDB: F6ELY0_HOYSD
Original site: F6ELY0_HOYSD 
ID   F6ELY0_HOYSD            Unreviewed;       394 AA.
AC   F6ELY0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Radical SAM core domain-containing protein {ECO:0000259|PROSITE:PS51918};
GN   OrderedLocusNames=AS9A_4328 {ECO:0000313|EMBL:AEF42761.1};
OS   Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS   (Amycolicicoccus subflavus).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC   Hoyosella.
OX   NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF42761.1, ECO:0000313|Proteomes:UP000009235};
RN   [1] {ECO:0000313|EMBL:AEF42761.1, ECO:0000313|Proteomes:UP000009235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX   PubMed=21725023; DOI=10.1128/JB.05388-11;
RA   Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA   Wu X.L.;
RT   "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT   actinomycete isolated from crude oil-polluted soil.";
RL   J. Bacteriol. 193:4538-4539(2011).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR   EMBL; CP002786; AEF42761.1; -; Genomic_DNA.
DR   RefSeq; WP_013809109.1; NC_015564.1.
DR   AlphaFoldDB; F6ELY0; -.
DR   STRING; 443218.AS9A_4328; -.
DR   KEGG; asd:AS9A_4328; -.
DR   eggNOG; COG0535; Bacteria.
DR   HOGENOM; CLU_009273_4_3_11; -.
DR   OrthoDB; 9782387at2; -.
DR   Proteomes; UP000009235; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01335; Radical_SAM; 1.
DR   CDD; cd21123; SPASM_MftC-like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR023913; MftC.
DR   InterPro; IPR017200; PqqE-like.
DR   InterPro; IPR007197; rSAM.
DR   NCBIfam; TIGR03962; mycofact_rSAM; 1.
DR   NCBIfam; TIGR04085; rSAM_more_4Fe4S; 1.
DR   PANTHER; PTHR11228:SF7; PQQA PEPTIDE CYCLASE; 1.
DR   PANTHER; PTHR11228; RADICAL SAM DOMAIN PROTEIN; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF13186; SPASM; 1.
DR   PIRSF; PIRSF037420; PQQ_syn_pqqE; 2.
DR   SFLD; SFLDF00316; C-terminal_tyrosine_decarboxyl; 1.
DR   SFLD; SFLDG01216; thioether_bond_formation_requi; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009235};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          11..221
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          372..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   394 AA;  42778 MW;  D1B5A3B54E303762 CRC64;
     MRLVEHFKEG LDAPICLTWE LTYACNLSCT HCLSASGKRD PRELTTAECK AVIDELERMQ
     VFYVNIGGGE PTVRPDFWEL LDYAIDHNVG VKFSTNGVRI TPDRARQLAA TDYVDIQISI
     DGATAEVNDA VRGPGSFATA MRAMENLADA GFTGFKISVV MTRHNVSQLD EFKAIADKFD
     AQLRITRLRP SGRGADVWDD LHPTAEQQLR IYEWLLDHGE DVLTGDSFFH LNALGSSPLP
     GLNLCGAGRV VCLIDPVGDV YACPFAIHSE FLAGNVREKG GFASVWRTSE LFEQLRQPQT
     GGVCKSCPAF DACQGGCMAA KFFTGLPLDG PDPECVRGNG ERALAAVGSS SIPRPEKDHT
     HTAKRKGVQL GMPLAPRNSV PDRPCNASPV AGLI
//
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