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Database: UniProt
Entry: A0A1T5CMN7_9GAMM
LinkDB: A0A1T5CMN7_9GAMM
Original site: A0A1T5CMN7_9GAMM 
ID   A0A1T5CMN7_9GAMM        Unreviewed;       531 AA.
AC   A0A1T5CMN7;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=SAMN05660880_01813 {ECO:0000313|EMBL:SKB60606.1};
OS   Luteibacter sp. 22Crub2.1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Luteibacter.
OX   NCBI_TaxID=1283288 {ECO:0000313|EMBL:SKB60606.1, ECO:0000313|Proteomes:UP000191150};
RN   [1] {ECO:0000313|EMBL:SKB60606.1, ECO:0000313|Proteomes:UP000191150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22Crub2.1 {ECO:0000313|EMBL:SKB60606.1,
RC   ECO:0000313|Proteomes:UP000191150};
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};
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DR   EMBL; FUYT01000007; SKB60606.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5CMN7; -.
DR   Proteomes; UP000191150; 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: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:SKB60606.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          308..437
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   531 AA;  59455 MW;  28FA91DED129C317 CRC64;
     MRRFAQLFEA LDRTASTSAK RDAMAAYFAV APAEDAAWAV YVLGGGKLRR TASSTELRTA
     LAEETGYADW LIDDSYQHVG DLAETIALML PAIDDDGEDT PLHVWMEARL PSIGKLEPGE
     RIALLREWWR STPREQIFLV NKLLTGSLRV GVSQRLVVQA LAQWSNLATD LIAHRLSGTW
     KPGAEAFRAL AGPERDDEHA GERPYPFFLA SPLEQGVENL GDIHQWLAEW KWDGIRAQLM
     RRADGALIWS RGEERMDGRF PELEQAAADL PDGCVIDGEI LAWLPDEAHP LLFAALQKRI
     GKLKPGPKLL ADTPVRLMAY DLLELGGKDL REHPLAERRA LLTSLLEGRG PTLTVSPAVS
     APDWASLAEV RAESRERRTE GLMLKRTDSP YRVGRKRGDW WKWKVDPYTV DAVLLYAQPG
     HGRRSGLFTD YTFGVWDGET LVPVAKAYSG LDDSEIGKLD RWIRAHTIDR FGPVRSVEPT
     HVFELAFEAI QASGRHKAGV AVRFPRILRW RTDLAIRDAD KLDDLRRLAS G
//
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