ID   H2JI28_9CLOT            Unreviewed;       324 AA.
AC   H2JI28;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=Clo1100_0393 {ECO:0000313|EMBL:AEY64679.1};
OS   Clostridium sp. BNL1100.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=755731 {ECO:0000313|EMBL:AEY64679.1, ECO:0000313|Proteomes:UP000007324};
RN   [1] {ECO:0000313|EMBL:AEY64679.1, ECO:0000313|Proteomes:UP000007324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BNL1100 {ECO:0000313|EMBL:AEY64679.1,
RC   ECO:0000313|Proteomes:UP000007324};
RX   PubMed=23209234; DOI=10.1128/JB.01908-12;
RA   Li L.L., Taghavi S., Izquierdo J.A., van der Lelie D.;
RT   "Complete Genome Sequence of Clostridium sp. Strain BNL1100, a Cellulolytic
RT   Mesophile Isolated from Corn Stover.";
RL   J. Bacteriol. 194:6982-6983(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC         diphosphate.; EC=6.5.1.1; Evidence={ECO:0000256|ARBA:ARBA00034003};
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DR   EMBL; CP003259; AEY64679.1; -; Genomic_DNA.
DR   RefSeq; WP_014312081.1; NC_016791.1.
DR   AlphaFoldDB; H2JI28; -.
DR   STRING; 755731.Clo1100_0393; -.
DR   KEGG; clb:Clo1100_0393; -.
DR   PATRIC; fig|755731.4.peg.395; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_008325_4_0_9; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000007324; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR   CDD; cd07971; OBF_DNA_ligase_LigD; 1.
DR   Gene3D; 3.30.1490.70; -; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR45674:SF15; DNA LIGASE (ATP); 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AEY64679.1}.
FT   DOMAIN          104..198
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   324 AA;  36913 MW;  2C6E22850EE546D2 CRC64;
     MNWIIPMEPV ICPDVKEGSG CIHEIKWDGI RGMVYIQDGN VKIYTKKGKE RTGFYPELDV
     LRKGLGGKNA ILDGEFVVLD EDGVPSFYKS LIRERVRNSG KLQYYTSSYP VCYMVFDILQ
     YGDDILVNMP LIERKQILEE NLSSLTGNDT KIFLAKMYKD GKELFEKMKK QNMEGIVSKK
     TDSLYIGGKK HDAWFKTKFI KKMLCIVGGI QWKSIHPNSL VLGIKPPDSE KLVYVGKASI
     GLKQSDLMLI KEYSGQLEQE ECPFTTDEII QLDKTGEKFT WLYPALTCWI SFLELTNDGH
     LRHPKIEGFA VLPVEEADGK VLTD
//