Y251_CLOBJ
ID Y251_CLOBJ Reviewed; 645 AA.
AC C1FQT8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=UPF0313 protein CLM_0251 {ECO:0000255|HAMAP-Rule:MF_01251};
GN OrderedLocusNames=CLM_0251;
OS Clostridium botulinum (strain Kyoto / Type A2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kyoto / Type A2;
RA Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01251};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000255|HAMAP-Rule:MF_01251};
CC -!- SIMILARITY: Belongs to the UPF0313 family. {ECO:0000255|HAMAP-
CC Rule:MF_01251}.
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DR EMBL; CP001581; ACO87244.1; -; Genomic_DNA.
DR RefSeq; WP_011948014.1; NC_012563.1.
DR AlphaFoldDB; C1FQT8; -.
DR EnsemblBacteria; ACO87244; ACO87244; CLM_0251.
DR GeneID; 5187168; -.
DR KEGG; cby:CLM_0251; -.
DR eggNOG; COG1032; Bacteria.
DR HOGENOM; CLU_018288_2_0_9; -.
DR OMA; YKLEYYE; -.
DR Proteomes; UP000001374; 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:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.80.30.20; -; 1.
DR HAMAP; MF_01251; UPF0313; 1.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR InterPro; IPR022946; UPF0313.
DR InterPro; IPR024560; UPF0313_C.
DR InterPro; IPR013704; UPF0313_N.
DR PANTHER; PTHR32331; PTHR32331; 1.
DR Pfam; PF11842; DUF3362; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF08497; Radical_SAM_N; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDG01069; UPF0313; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR03904; SAM_YgiQ; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; S-adenosyl-L-methionine.
FT CHAIN 1..645
FT /note="UPF0313 protein CLM_0251"
FT /id="PRO_1000165087"
FT DOMAIN 295..566
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 598..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 309
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01251"
FT BINDING 313
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01251"
FT BINDING 316
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01251"
SQ SEQUENCE 645 AA; 74555 MW; AA2CFA5147DDFD57 CRC64;
MSNMDFLPIS KEDLKKRNID VLDFIIVTGD AYVDHPSFGT AIIGRVLERE GFTVGIIAQP
NWNNIEDFKK LGKPKYGFLV NSGNIDSMVN HYTASKKKRH DDFYSPGGKS GYRPDRAVIV
YCNKIKEAFK DSPIIIGGIE ASLRRFAHYD YWDNSVRRSI LEDSSADLLI YGMGEKPIVQ
VSNLLRYGMK IDSIKNVRGT TYIEKDISSL KDYIEIPSFE EVSTNKKSYA EAYKIQYYEQ
DSIRGKTLVQ KHKERYVVQN PPQPPLSQEE MDEVYALPYA RTYHPMYEAE GGIPAIKEVK
FSITSHRGCY GSCSFCALTF HQGRVIQNRS QDSILKEANM MTNMKDFKGY IHDVGGPTAN
FRHRACKVQE KHGTCKNKQC VFPKACKNLI VDHKEYLSLL RKIRKIPNVK KVFIRSGIRF
DYLMYDKNDE FFKELCEHHI SGQLKVAPEH ISDKVLNLMG KPTRNVYDSF VKKYYDINKK
IHKNQFLVPY LMSSHPGSDL KAAIELAQYI KKMGYTPEQV QDFYPTPGSL STTMYYTGIN
PLTEEKVYIP KDQKEKRMQR ALLQFSIHDN YDLVKEALIK AHREDLIGNG PDCLIPYNKP
YKKSHKKNNA KNNNNHYNKN NNYNKNKDIS KKNKKNSLSK HKKRK