ID A0A0C1U374_9CLOT Unreviewed; 619 AA.
AC A0A0C1U374;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Radical SAM superfamily protein {ECO:0000313|EMBL:KIE47299.1};
GN ORFNames=U732_1203 {ECO:0000313|EMBL:KIE47299.1};
OS Clostridium argentinense CDC 2741.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE47299.1, ECO:0000313|Proteomes:UP000031366};
RN [1] {ECO:0000313|EMBL:KIE47299.1, ECO:0000313|Proteomes:UP000031366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE47299.1,
RC ECO:0000313|Proteomes:UP000031366};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
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:KIE47299.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYSO01000015; KIE47299.1; -; Genomic_DNA.
DR RefSeq; WP_039632036.1; NZ_AYSO01000015.1.
DR AlphaFoldDB; A0A0C1U374; -.
DR STRING; 29341.RSJ17_14180; -.
DR OrthoDB; 9806827at2; -.
DR Proteomes; UP000031366; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR InterPro; IPR023862; CHP03960_rSAM.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR045784; Radical_SAM_N2.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR NCBIfam; TIGR03960; rSAM_fuse_unch; 1.
DR PANTHER; PTHR42731:SF1; RADICAL SAM DOMAIN PROTEIN; 1.
DR PANTHER; PTHR42731; SLL1084 PROTEIN; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF19864; Radical_SAM_N2; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000031366}.
FT DOMAIN 251..493
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 619 AA; 71635 MW; 1AB6DD8131CDA0DC CRC64;
MNKISDDILY KVEKPARYVG GEFNSYNKDK SVVDIRYAFC FPDVYEVGMS HLGSKILYYV
LNEREDTFCE RCFAPWPDME KQLRENHIPL YALESKDSLS EFDFLGFTLQ YEMSYTNILN
MLDMAGVPLR ASQRDEKSPI VMMGGPCAYN PEPLYDIADI FVLGESEIVI HEILDLYKEY
KNKSKKDYLR AVCEIEGVYV PSLYEVTYKD DNTIKEFKPI YDDVPKTIKK RIINNFDENV
YPDKLIVPYT EIVHDRITLE TFRGCTRGCR FCQAGMIYRP VREKKTDTLI DQVDEILKKT
GYEEVSLTSL SICDYSDIQN LIFSLVKKYE GEKIGVSLPS IRIDSFSVDL INEIQKVRKT
GLTFAPEAGS QRMRDIINKG VNEENLLESS RSAFEAGWST LKLYFMIGLP YETMEDVIGI
AELGEKVVEQ YFNVPKHIRK RGLRVTISTS IFVPKPFTPF QWAPMDTMPS VKEKISNLRN
SIKSKAIVYN WHESPVSYME AVFARGDRRL CDVLIKAFEK GARFDGWGEY FSFDTWKESM
DDCNVDGDFY AYRERDYEEI LPWDFIDIGV TKEFLIKENN KAKEAIVTPD CRGICERCGI
NVSFKEGKCF EGAILNKIH
//