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Database: UniProt
Entry: H0FYC6_RHIML
LinkDB: H0FYC6_RHIML
Original site: H0FYC6_RHIML 
ID   H0FYC6_RHIML            Unreviewed;       312 AA.
AC   H0FYC6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=SM0020_11020 {ECO:0000313|EMBL:EHK77980.1};
OS   Sinorhizobium meliloti CCNWSX0020.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=1107881 {ECO:0000313|EMBL:EHK77980.1, ECO:0000313|Proteomes:UP000004038};
RN   [1] {ECO:0000313|EMBL:EHK77980.1, ECO:0000313|Proteomes:UP000004038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCNWSX0020 {ECO:0000313|EMBL:EHK77980.1,
RC   ECO:0000313|Proteomes:UP000004038};
RX   PubMed=22328762; DOI=10.1128/JB.06682-11;
RA   Li Z., Ma Z., Hao X., Wei G.;
RT   "Draft Genome Sequence of Sinorhizobium meliloti CCNWSX0020, a Nitrogen-
RT   Fixing Symbiont with Copper Tolerance Capability Isolated from Lead-Zinc
RT   Mine Tailings.";
RL   J. Bacteriol. 194:1267-1268(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};
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DR   EMBL; AGVV01000016; EHK77980.1; -; Genomic_DNA.
DR   RefSeq; WP_003528445.1; NZ_AGVV01000016.1.
DR   AlphaFoldDB; H0FYC6; -.
DR   PATRIC; fig|1107881.3.peg.2227; -.
DR   Proteomes; UP000004038; 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; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR   CDD; cd07971; OBF_DNA_ligase_LigD; 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; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR014146; LigD_ligase_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR02779; NHEJ_ligase_lig; 1.
DR   PANTHER; PTHR45674:SF15; DNA LIGASE (ATP); 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 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   4: Predicted;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EHK77980.1}.
FT   DOMAIN          100..234
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   312 AA;  35127 MW;  77230FA68794888B CRC64;
     MPARVDPCLA TLVDRPPKGP DWACEVKWDG YRIAVHIEHG RVRILTRGGY DWTERFPTIV
     DDARRLAVKT AIVDGEAVVL DDKGRSDFGM LQRALGRLPS AVEAGAIVFF AFDLLYLDGR
     DLRRVPLRER RRLLEPLVAG REGAVRLSEK VQADGDEFFR VACEHGLEGI IAKHIEKPYR
     SGRGEWWQKI TCKRRDSFVI VGFEPSTVPG HLGRLLLAAC KNDDLVYVGG CGTGWSHDIS
     RELRNVLASI VTKRPAVSLR RKNAVFTEPV LVAEVEYRAW TDDGKLRHES FKGIRSREDE
     AAVFQLSKGI EE
//
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