ID   E6TTD1_EVAC2            Unreviewed;       300 AA.
AC   E6TTD1;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=ATP dependent DNA ligase {ECO:0000313|EMBL:ADU28471.1};
GN   OrderedLocusNames=Bcell_0182 {ECO:0000313|EMBL:ADU28471.1};
OS   Evansella cellulosilytica (strain ATCC 21833 / DSM 2522 / FERM P-1141 / JCM
OS   9156 / N-4) (Bacillus cellulosilyticus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Evansella.
OX   NCBI_TaxID=649639 {ECO:0000313|EMBL:ADU28471.1, ECO:0000313|Proteomes:UP000001401};
RN   [1] {ECO:0000313|Proteomes:UP000001401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4
RC   {ECO:0000313|Proteomes:UP000001401};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Brumm P., Mead D.,
RA   Woyke T.;
RT   "Complete sequence of Bacillus cellulosilyticus DSM 2522.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002394; ADU28471.1; -; Genomic_DNA.
DR   RefSeq; WP_013486812.1; NC_014829.1.
DR   AlphaFoldDB; E6TTD1; -.
DR   STRING; 649639.Bcell_0182; -.
DR   KEGG; bco:Bcell_0182; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_008325_4_0_9; -.
DR   Proteomes; UP000001401; 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   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
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; 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:0000313|EMBL:ADU28471.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001401}.
FT   DOMAIN          105..224
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   300 AA;  34603 MW;  85093889427B4377 CRC64;
     MLFTPVKPML LTMGKEPTNH PEHLYDIKWD GWRILIHKQG NRIEAYTRHG NQVTNQFPEL
     QEALSHINKH TAILDCEGVV LRNGNSVFED FAYRGRLKST EKIRKAMITH PVTFVAFDIL
     ATDKPLLKET LIKRKQYLKD IITPSNVLLA TPYVIEDGQT LHTLTKEKGM EGIVEKPLNS
     LYHLDTRSPN WLKHKHFKRL DTVIMGYKEN PFTMIVGSTF SNGKLKPVAQ VEFGFNPEDK
     QAFRGIANRL ITKEENGVFW LEPLLCCSTQ YLEKTSKNML RITSFKGFLP EKKVEECVFT
//