ID   D9R943_LACSW            Unreviewed;       307 AA.
AC   D9R943;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   OrderedLocusNames=Closa_1417 {ECO:0000313|EMBL:ADL04018.1};
OS   Lacrimispora saccharolytica (strain ATCC 35040 / DSM 2544 / NRCC 2533 /
OS   WM1) (Clostridium saccharolyticum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lacrimispora.
OX   NCBI_TaxID=610130 {ECO:0000313|EMBL:ADL04018.1, ECO:0000313|Proteomes:UP000001662};
RN   [1] {ECO:0000313|EMBL:ADL04018.1, ECO:0000313|Proteomes:UP000001662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35040 / DSM 2544 / NRCC 2533 / WM1
RC   {ECO:0000313|Proteomes:UP000001662};
RG   US DOE Joint Genome Institute;
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   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Mouttaki H., Lin L., Zhou J., Hemme C.L., Woyke T.;
RT   "Complete sequence of Clostridium saccharolyticum WM1.";
RL   Submitted (JUL-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; CP002109; ADL04018.1; -; Genomic_DNA.
DR   RefSeq; WP_013272109.1; NC_014376.1.
DR   AlphaFoldDB; D9R943; -.
DR   STRING; 610130.Closa_1417; -.
DR   PaxDb; 610130-Closa_1417; -.
DR   KEGG; csh:Closa_1417; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_008325_4_0_9; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000001662; 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; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ADL04018.1}.
FT   DOMAIN          106..197
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   307 AA;  35480 MW;  B12DB34AF16E8D8E CRC64;
     MDIFDIKKIS PMLISEMMDP FDSPDYIYEI KWDGIRCVSY LGTDTDIRNK RNKLMAPLFP
     ELKNLHAQVK TKCILDHELL VLKNGVPDFY EVQKRALMAN SFKIKLAADR YPASIIAYDI
     LYYKDKDITM LPLMERKKYL QDVVIENNMI SVSRYVENEG IMLFDLVKEK GLEGVVAKRK
     NSLYWQGKRS KDWIKFKVMA TDDCIICGYI VKEKSMPSLI LGQYDDDVLV YKGHVSLGVS
     LRILNQYKYQ IIDYSPFGYV PAGNENAVWL APDLVCIVES MPTDKDSFRQ PVFKGIRNDK
     SAIECKV
//