ID   A0A1T4X8E4_9BACT        Unreviewed;       925 AA.
AC   A0A1T4X8E4;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=SAMN02745166_01219 {ECO:0000313|EMBL:SKA85872.1};
OS   Prosthecobacter debontii.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC   Verrucomicrobiaceae; Prosthecobacter.
OX   NCBI_TaxID=48467 {ECO:0000313|EMBL:SKA85872.1, ECO:0000313|Proteomes:UP000190774};
RN   [1] {ECO:0000313|EMBL:SKA85872.1, ECO:0000313|Proteomes:UP000190774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700200 {ECO:0000313|EMBL:SKA85872.1,
RC   ECO:0000313|Proteomes:UP000190774};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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,
CC         ECO:0000256|RuleBase:RU000617};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; FUYE01000003; SKA85872.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4X8E4; -.
DR   STRING; 48467.SAMN02745166_01219; -.
DR   Proteomes; UP000190774; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07898; Adenylation_DNA_ligase; 1.
DR   CDD; cd07972; OBF_DNA_ligase_Arch_LigB; 1.
DR   Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 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   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
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; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR011108; RMMBL.
DR   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45674:SF7; DNA LIGASE; 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   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   Pfam; PF07521; RMMBL; 1.
DR   SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000617};
KW   DNA damage {ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000617}.
FT   DOMAIN          702..825
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   925 AA;  103661 MW;  50520186BD598477 CRC64;
     MAEHLTNIIW LRLLSVALPM TPLLKVEYRK GIYLPEADLW LDPHHGVKRA FISHAHSDHV
     ARHEWTCCSA LTRELMRVRY GMSKDGHVEA LPMRQDFEWE GWRLRLFPAG HIVGSAMLHL
     TRMSDGASLL YTGDYKLRQG LSSERCELLT ADTLIMETTF GLPMFRFPPT AVVIEQMLRW
     VRETLDEGEI PVLLGYSLGK AQEILCALGD AGYPVMVHPS IWEMTQVVAP WLGRLPDYQL
     FDPARAKGHV LLFPPGGARS QAIRKLKICR TAMLSGWAMQ SGAKYRYQVD AAFPLSDHAD
     YPELLETVKV VKARRVFLVH GYTREFAADL RARGYDAWTL EGADQLEMSL DGMPDRLDAL
     PPDASGAAKG VVEACDSLAR WSQVGELAAA ESSRLKKTAL LAEYLRALES ENDVALAVRY
     CAGLLFDPAA AEGPVNAGWA IIRRALQELS GLSDAEYRAI SRSQADAGRT AYLVLSRMNL
     LDPQTVTLGE TDQFFRAVRE VRGPVPKTKL LKEQLLRLTA HTGSWLIRLL TGELRMGSKE
     GLIEEAVAAA FDQNADQVRE AAMLCGDIGR AAVLARRAEL HAAAPQPMVP IKVMLASPEE
     TAAEVWQRMT ALGAQSIWLE DKYDGIRAQL HVTPQRMEIF TRDLKPITDQ FPEIALAARQ
     MTDAVILDGE IIAYSDDKKL SFFDLQKRLG RRDQADLFLP SDITVRYVVF DLLWQNDRSW
     LDRSLQERRQ QLESLQLPQG LALIGVQRAH SVEEVEAAFM AARRRNNEGL IIKDPDSHYS
     PGRRGKSWLK LKKAFATLDV VVVKAEQGHG KRSHVLSDYT FAVRDEESDN ALRVIGKAYS
     GLTDVEIEEL TEHFQQTTLE QKGRVRTVIP QIILEIAFDS IQASDRHDSG LALRFPRIKA
     IRKDKAVEEI DTLTYARKLA GLPGK
//