ID   G8NTR2_GRAMM            Unreviewed;       661 AA.
AC   G8NTR2;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   OrderedLocusNames=AciX8_2056 {ECO:0000313|EMBL:AEU36386.1};
OS   Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Granulicella.
OX   NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU36386.1, ECO:0000313|Proteomes:UP000007113};
RN   [1] {ECO:0000313|EMBL:AEU36386.1, ECO:0000313|Proteomes:UP000007113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8
RC   {ECO:0000313|Proteomes:UP000007113};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Rawat S., Mannisto M.,
RA   Haggblom M., Woyke T.;
RT   "Complete sequence of Granulicella mallensis MP5ACTX8.";
RL   Submitted (NOV-2011) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003130; AEU36386.1; -; Genomic_DNA.
DR   RefSeq; WP_014265264.1; NC_016631.1.
DR   AlphaFoldDB; G8NTR2; -.
DR   STRING; 682795.AciX8_2056; -.
DR   KEGG; gma:AciX8_2056; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_005138_6_0_0; -.
DR   OrthoDB; 9767858at2; -.
DR   Proteomes; UP000007113; Chromosome.
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   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   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF13; DNA LIGASE-RELATED; 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   SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007113}.
FT   DOMAIN          395..555
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   661 AA;  71326 MW;  7AFAE79C7406B3C9 CRC64;
     MAFFVALATL AEKLSQEGSR LKKRAAIAEA IASLHAAAPE SSDAGRFALY LAGQPFAEND
     ARKLNAGGAL LSRAVLTVAG ADNAQLTAAY RRHGDLGAAA HDLLVAPHGK APSTATLTLD
     DVADAFAAMA VARTTAARSS LVEGLLTRAT AVEAKYLLKL MLGDMRIGVK QSLIEEAIAV
     ASGTEVAAVR HGVMLEADLV CAVGRAFAGT LAAARMTLFH PLGFMLASPV ETPEAAVERF
     TEAPAKEKPA KVAKPKKARK KRVGEDFVDL APVQEVVARD APEEGLAEDA QIEALASGEL
     SAGSSGVLAF LEDKYDGMRA QVHCGDPSQP GRVAIYSRNR EDITQSFPEL AEAFAQVEEP
     MILDGEILGW DFGKSQALPF AVMGQRIGRK VVSDEVRRQI PAVFMAFDLL FVGDELLLPL
     PLTRRRMLLE EVVARWSEHA RSALAADSTR KADQAGLFSE TAPVAEQKTR WMLSPSQPVT
     DAAAIDQAYR DARARANEGV MLKRADSAYL PGRRGLAWVK LKRELATLDV VITGAEFGHG
     KRAGLLSDYT FAVRGQAGQL LNVGKAYSGL TDAEILEMTA WLKAHTLEDR GYFRTVEPQI
     VLEVAFNNIM RSSRHASGFA LRFPRILHIR RDKPVSEIDT LEQVEAVYQT QPDRPDESLE
     E
//