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Database: UniProt
Entry: T0PCN2_9CLOT
LinkDB: T0PCN2_9CLOT
Original site: T0PCN2_9CLOT 
ID   T0PCN2_9CLOT            Unreviewed;       436 AA.
AC   T0PCN2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EQB87748.1};
GN   ORFNames=M918_07810 {ECO:0000313|EMBL:EQB87748.1};
OS   Clostridium sp. BL8.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1354301 {ECO:0000313|EMBL:EQB87748.1, ECO:0000313|Proteomes:UP000015873};
RN   [1] {ECO:0000313|EMBL:EQB87748.1, ECO:0000313|Proteomes:UP000015873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL8 {ECO:0000313|EMBL:EQB87748.1,
RC   ECO:0000313|Proteomes:UP000015873};
RX   PubMed=25076986; DOI=10.1186/1757-4749-6-30;
RA   Marathe N.P., Shetty S.A., Lanjekar V.B., Rasane M.H., Ranade D.R.,
RA   Shouche Y.S.;
RT   "Genome sequencing of multidrug resistant novel Clostridium sp. BL8 reveals
RT   its potential for pathogenicity.";
RL   Gut Pathog. 6:30-30(2014).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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:EQB87748.1}.
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DR   EMBL; AUPA01000186; EQB87748.1; -; Genomic_DNA.
DR   RefSeq; WP_021283831.1; NZ_AUPA01000186.1.
DR   AlphaFoldDB; T0PCN2; -.
DR   STRING; 1354301.M918_07810; -.
DR   PATRIC; fig|1354301.3.peg.2725; -.
DR   OrthoDB; 9801424at2; -.
DR   Proteomes; UP000015873; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031419; F:cobalamin binding; 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   CDD; cd02068; radical_SAM_B12_BD; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR034466; Methyltransferase_Class_B.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   PANTHER; PTHR43409; ANAEROBIC MAGNESIUM-PROTOPORPHYRIN IX MONOMETHYL ESTER CYCLASE-RELATED; 1.
DR   PANTHER; PTHR43409:SF12; BLL1977 PROTEIN; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR   SFLD; SFLDG01123; methyltransferase_(Class_B); 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00022485};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015873}.
FT   DOMAIN          17..149
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   DOMAIN          188..414
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   436 AA;  50717 MW;  3171E45CA767C174 CRC64;
     MKDIDVMIIN LFTEESMSID STGSKISTMP PLGQLYISSV LQSNGYEVMV LDLGVENMSN
     KQILEKIQQH SPKIVGFSSY YGSWSMLKEI TTLIKREFED IVITVGGNSA TFNYEEILNE
     MKVNYIILGE GEFSFLKLCD YVIRETIPLE HVEGIAYKQD NSIRKTEVKR ISNLDELPFP
     NRELIKLHRY RHPFTIATAR GCIGKCIFCS SQAFWKDKIT FRSIDNVILE LEHIKNKFDA
     KEFFIIDDTF TLNKARVLEF CDKLIKKDLS FYWFCESRVD VISEEVLIAM YEAGCRWIQF
     GMESGNDEIL AGIRKNISFS EIEEAIRLAT NIGFRINLSL IIGHHLDTKD TIKETLEKAK
     YLKRKYQVNV LAGINTPYPG TEVFEKRDEY GLKILTKNWD RYKMDNPVMD TKYLKANELK
     RLHFNFMKEL EHMDRS
//
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