ID A0A0F2L2U6_9PROT Unreviewed; 526 AA.
AC A0A0F2L2U6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN ORFNames=VY88_09870 {ECO:0000313|EMBL:KJR67268.1};
OS Azospirillum thiophilum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=528244 {ECO:0000313|EMBL:KJR67268.1, ECO:0000313|Proteomes:UP000033623};
RN [1] {ECO:0000313|EMBL:KJR67268.1, ECO:0000313|Proteomes:UP000033623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21654 {ECO:0000313|EMBL:KJR67268.1,
RC ECO:0000313|Proteomes:UP000033623};
RA Kwak Y., Shin J.-H.;
RT "Genome sequence of Azospirillum thiophilum strain DSM 21654T.";
RL Submitted (MAR-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJR67268.1}.
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; LAEL01000001; KJR67268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2L2U6; -.
DR STRING; 528244.AL072_02840; -.
DR KEGG; ati:AL072_02840; -.
DR PATRIC; fig|528244.3.peg.2057; -.
DR Proteomes; UP000033623; Unassembled WGS sequence.
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; cd07897; Adenylation_DNA_ligase_Bac1; 1.
DR CDD; cd07972; OBF_DNA_ligase_Arch_LigB; 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; 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 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 Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KJR67268.1}.
FT DOMAIN 313..432
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 526 AA; 58649 MW; 308D0E95B0BA8442 CRC64;
MPSRTGKIRL LVEHFATAPD PDRGWALAAL TGALSFREAK PAAIRELAAT RVDPELLALS
YDYVGDLAET VALIWPERPA SWAERANSLP PGLDEVVDAL RSAKRGQVMG LVEGWLDTLD
SSGRFALLKL ITGALRIGVS ARLAKTALAE WGKAARPEVG IDDEIGVDDV EEVWHGLSPP
YVELFAWLEG RAERPAAGHG AGFRPMMLSH PLEEEERAAL DPAAYAAEWK WDGIRVQLAA
RDGQRRLYSR TGDDVSGAFP DITDHMGFDA VLDGELLVAR DGVVAPFNDL QQRLNRKTVT
AQMLRDGPAW VRLYDILFDG AEDLRGLPFV ERRARLERWY DAVRPRRMDV SPLVPFAAWD
ELAALREGAR ENGIEGLMLK RRDSAYLAGR PKGPWFKWKR GALTLDTVMM YAQRGHGKRS
SYYSDYTFGV WRGEELVPVG KAYSGFTDAE LVELDRWVRT HTTKRYGPVR EVAAGLVLEV
AFDSVHPSTR HKSGLAMRFP RIHRIRWDKP AHEADRLETL AAMVAG
//