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Database: UniProt
Entry: C1AD68_GEMAT
LinkDB: C1AD68_GEMAT
Original site: C1AD68_GEMAT 
ID   C1AD68_GEMAT            Unreviewed;       529 AA.
AC   C1AD68;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   Name=lig {ECO:0000313|EMBL:BAH40445.1};
GN   OrderedLocusNames=GAU_3403 {ECO:0000313|EMBL:BAH40445.1};
OS   Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS   100505).
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatimonas.
OX   NCBI_TaxID=379066 {ECO:0000313|EMBL:BAH40445.1, ECO:0000313|Proteomes:UP000002209};
RN   [1] {ECO:0000313|Proteomes:UP000002209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505
RC   {ECO:0000313|Proteomes:UP000002209};
RA   Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A.,
RA   Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H.,
RA   Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT   "Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a
RT   novel phylum Gemmatimonadetes.";
RL   Submitted (MAR-2006) 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; AP009153; BAH40445.1; -; Genomic_DNA.
DR   RefSeq; WP_015895214.1; NC_012489.1.
DR   AlphaFoldDB; C1AD68; -.
DR   STRING; 379066.GAU_3403; -.
DR   KEGG; gau:GAU_3403; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_005138_6_2_0; -.
DR   OrthoDB; 9767858at2; -.
DR   Proteomes; UP000002209; 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:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07897; Adenylation_DNA_ligase_Bac1; 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; IPR026333; ATP_dep_DNA_lig_pp_1105_fam.
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; TIGR04120; DNA_lig_bact; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:BAH40445.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002209}.
FT   DOMAIN          304..435
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   529 AA;  59053 MW;  86C9FC04037954E9 CRC64;
     MKQFAALYDA IDATTATSEK VAALVAYFRI ANPADAAWAV SFLVGRRPKR LVKAPDLRLW
     AAEAADIPAW LFEESYAQAG DLAEAISLLV PEPAATTDES LAWWVEQRLL PLATMEPIEQ
     RTALRAAWSE LGGTARFLFN KLITGGFRVG VAEGLVVRAL SQASGVPVDT IAHRLMGQWE
     PSGAWYEQLV HAHTSDADWS KPYPFFLAYP LEAAPESLGE VRDWQCEWKW DGIRCQLVRR
     NGRTMLWSRG EELLAGRFPE VEAVAEWLPD GTVLDGEMLA WRDGQPLPFS ELQRRINRKT
     VGKALLADVP CHMLVYDCLE VRGNDIRSEP LRARRTQAEH IVGALPSGGS MGLSPIVDAR
     TWADVTEARD AARERQSEGL MLKRLESPYG VGRKVGDWWK WKVNPMTVDA VLVYAQAGHG
     RRAGLYTDYT FAIWDGTTLV PFAKAYSGLT DAEIRDVDRF VRANTLEKFG PVRTVKPELV
     FELAFEGIQR STRHKSGLAV RFPRMARWRK DKPAAEADTV ETVRALLPA
//
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