ID   I3X6V0_SINF2            Unreviewed;       364 AA.
AC   I3X6V0;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=USDA257_c30360 {ECO:0000313|EMBL:AFL51606.1};
OS   Sinorhizobium fredii (strain USDA 257).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=1185652 {ECO:0000313|EMBL:AFL51606.1, ECO:0000313|Proteomes:UP000006180};
RN   [1] {ECO:0000313|EMBL:AFL51606.1, ECO:0000313|Proteomes:UP000006180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USDA 257 {ECO:0000313|EMBL:AFL51606.1,
RC   ECO:0000313|Proteomes:UP000006180};
RX   PubMed=22843606; DOI=10.1128/JB.00966-12;
RA   Schuldes J., Rodriguez Orbegoso M., Schmeisser C., Krishnan H.B.,
RA   Daniel R., Streit W.R.;
RT   "Complete genome sequence of the broad-host-range strain Sinorhizobium
RT   fredii USDA257.";
RL   J. Bacteriol. 194:4483-4483(2012).
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; CP003563; AFL51606.1; -; Genomic_DNA.
DR   RefSeq; WP_014763768.1; NC_018000.1.
DR   AlphaFoldDB; I3X6V0; -.
DR   STRING; 1185652.USDA257_c30360; -.
DR   KEGG; sfd:USDA257_c30360; -.
DR   PATRIC; fig|1185652.3.peg.3152; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_008325_4_1_5; -.
DR   Proteomes; UP000006180; 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; 3.30.1490.70; -; 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; 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; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AFL51606.1}.
FT   DOMAIN          138..266
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   364 AA;  40400 MW;  331A628908C02525 CRC64;
     MPSPAHRKST KEAGSLRPTA TAKAARGMGS PAAFPLPVST APMEARSATE LPSDVVWQYE
     PKWDGFRCLA FKSGEEVDLR AKSGKPLGRF FPEIIALMRQ LDAAQFVVDG ELVIEVDGRL
     SFDALQMRLH PAASRVQKLS QQTPARLILF DMLVDTDGAI LTGRPLVARR AALEAFAAEN
     SGAAQLELSP FTLDRHEAER WLTSWEAGAT DGVVAKRRDG PYECGERAML KVKRLKTADC
     VVGGFRYESD SEEVGSLLLG LYDTDGTLNH VGFTATISDK ERPALTRRLE ALREPPGFTG
     KAPGGPSRWS TERSGEWEPV RPELVVEVRF DHVSSRRFRH GTKLMRWRPD KDPRQCTYEQ
     IEPR
//