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Database: UniProt/TrEMBL
Entry: A0A0F2L2U6_9PROT
LinkDB: A0A0F2L2U6_9PROT
Original site: A0A0F2L2U6_9PROT 
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}.
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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
//
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