ID F6FVH2_ISOV2 Unreviewed; 385 AA.
AC F6FVH2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN OrderedLocusNames=Isova_1647 {ECO:0000313|EMBL:AEG44399.1};
OS Isoptericola variabilis (strain 225).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Isoptericola.
OX NCBI_TaxID=743718 {ECO:0000313|Proteomes:UP000009236};
RN [1] {ECO:0000313|EMBL:AEG44399.1, ECO:0000313|Proteomes:UP000009236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=225 {ECO:0000313|Proteomes:UP000009236};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Zeytun A., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Siebers A., Allgaier M., Thelen M.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Isoptericola variabilis 225.";
RL Submitted (MAY-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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572}.
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DR EMBL; CP002810; AEG44399.1; -; Genomic_DNA.
DR RefSeq; WP_013838791.1; NC_015588.1.
DR AlphaFoldDB; F6FVH2; -.
DR STRING; 743718.Isova_1647; -.
DR KEGG; iva:Isova_1647; -.
DR eggNOG; COG1793; Bacteria.
DR HOGENOM; CLU_008325_4_1_11; -.
DR Proteomes; UP000009236; 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; cd07905; Adenylation_DNA_ligase_LigC; 1.
DR CDD; cd07970; OBF_DNA_ligase_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; IPR044119; Adenylation_LigC-like.
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 InterPro; IPR044117; OBF_LigC-like.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45674:SF9; DNA LIGASE 3; 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; PS00697; DNA_LIGASE_A1; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AEG44399.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009236}.
FT DOMAIN 117..242
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 385 AA; 42262 MW; AB4DC7C3B82183F9 CRC64;
MSLPLQPPIL PMLAKSVPEV PEQPDGDAQW VYEPKWDGFR AIVYRDGDDV RIDSRNARPM
QRYFPEVVAA VLDALPERCV VDGEIVVARP DPGPGPARLD FDALSQRIHP AESRVRLLAE
QTPASLVVFD VLALGDDDLS RRPLAERLDA LDGLGLSGPH VFATPRTHDT AVAREWFEAF
EGAGLDGVVA KRLDGRYEPN KRTLLKIKHA RTADVVLAGY RLHKTSTPAE PLIGSLLLGL
YDGDEDGDPG QLQFVGVAAS FPAARRAALH AELAPLVVEP GTPEHEAHPW ADWQDPAVAD
GTAGERRPGA QSRWSAGKDL SFTPLRVERV LEVGYDHMEG TRFRHTAQFK RWRPDRDPTS
CTYAQLEEPV RYDLGSLLPG APGTA
//
