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Database: UniProt
Entry: A0A068YHI3_9BURK
LinkDB: A0A068YHI3_9BURK
Original site: A0A068YHI3_9BURK 
ID   A0A068YHI3_9BURK        Unreviewed;       297 AA.
AC   A0A068YHI3;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=DNA ligase (ATP) {ECO:0000313|EMBL:CDS49194.1};
DE            EC=6.5.1.1 {ECO:0000313|EMBL:CDS49194.1};
OS   Polaromonas sp. CG9_12.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1504672 {ECO:0000313|EMBL:CDS49194.1, ECO:0000313|Proteomes:UP000043372};
RN   [1] {ECO:0000313|EMBL:CDS49194.1, ECO:0000313|Proteomes:UP000043372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Smith H.J., Foreman C.M., Ramaraj T.;
RT   "Draft Genome Sequence of a Metabolically Diverse Antarctic Supraglacial
RT   Stream Organism, Polaromonas sp. Strain CG9_12, Determined Using Pacific
RT   Biosciences Single-Molecule Real-Time Sequencing Technology.";
RL   Genome Announc. 2:1-2(2014).
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   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|ARBA:ARBA00001968};
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DR   EMBL; CCJP01000005; CDS49194.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068YHI3; -.
DR   STRING; 1504672.gene:199030097; -.
DR   eggNOG; COG1793; Bacteria.
DR   Proteomes; UP000043372; 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:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07896; Adenylation_kDNA_ligase_like; 1.
DR   CDD; cd08041; OBF_kDNA_ligase_like; 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; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR029319; DNA_ligase_OB.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR47810; DNA LIGASE; 1.
DR   PANTHER; PTHR47810:SF1; DNA LIGASE B; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF14743; DNA_ligase_OB_2; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000313|EMBL:CDS49194.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000043372};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..297
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001660832"
FT   DOMAIN          118..211
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|Pfam:PF01068"
FT   DOMAIN          225..295
FT                   /note="DNA ligase OB-like"
FT                   /evidence="ECO:0000259|Pfam:PF14743"
SQ   SEQUENCE   297 AA;  32311 MW;  5AA92B203FBC202D CRC64;
     MMQRRFLLSM VSLALAASLL PAAAPAQASL PSSAHSPAPS LMLANVYRDG TILADYWVSE
     KYDGVRGYWD GQAFWTRGGE RIAAPAWFTA GWPKEPMDGE LWAGHGQFAK AVSTARQQTP
     SDAAWRTLRF MVFDLPAQGG TFTERIPALH GVVSRIDQLW VQAVAQSKVA SPQALRVLLT
     RTVKNGGEGL MLHRGASLYK GLRSDDLLKL KTHEDSEAQV VAHLPGQGKH AGRLGALLVE
     IPAAGDKPAQ RFKLGTGLSD AQRQNPPAIG ARVTYRFRGL NDSGIPRFAS FMRVRED
//
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