ID A0A0M4QPJ3_9PSEU Unreviewed; 354 AA.
AC A0A0M4QPJ3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN Name=ligC {ECO:0000313|EMBL:ALE80968.1};
GN ORFNames=WY02_24160 {ECO:0000313|EMBL:ALE80968.1};
OS Pseudonocardia sp. AL041005-10.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=445576 {ECO:0000313|EMBL:ALE80968.1, ECO:0000313|Proteomes:UP000067245};
RN [1] {ECO:0000313|EMBL:ALE80968.1, ECO:0000313|Proteomes:UP000067245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL041005-10 {ECO:0000313|EMBL:ALE80968.1,
RC ECO:0000313|Proteomes:UP000067245};
RX PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT "Variable genetic architectures produce virtually identical molecules in
RT bacterial symbionts of fungus-growing ants.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
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; CP011862; ALE80968.1; -; Genomic_DNA.
DR RefSeq; WP_062401048.1; NZ_CP011862.1.
DR AlphaFoldDB; A0A0M4QPJ3; -.
DR STRING; 445576.WY02_24160; -.
DR KEGG; psea:WY02_24160; -.
DR PATRIC; fig|445576.3.peg.5294; -.
DR OrthoDB; 9770771at2; -.
DR Proteomes; UP000067245; 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; 3.30.470.30; 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:SF4; DNA LIGASE 1; 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 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ALE80968.1}.
FT DOMAIN 105..248
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 354 AA; 39495 MW; 81357800A01F9A3E CRC64;
MDLPVMPPVK PMLAKPAPSI PEGRLYEPKW DGFRSIVFRD GDEVEIGSRN EKPMTRYFPE
VVEAVKAHFP PRAVVDGEIV VASGNALDFE ALQQRIHPAA SRVTLLSTET PASFVAFDLL
GLGDDDLTAR PFAERRALLE EAFAGVAPPV HLTPVTDDTA TARRWFEKFE GAGLDGLIAK
DPAGTYQPDK RVMTKVKHER TADCVVAGYR VHKSGPDAVG SLLLGLHDAR GVLVSVGVVG
AFPMARRREL MTELQPLVSD FDDHPWAWAK QLEGERTPRK SETSRWNAGK DLSFVPLRPE
RVVEVRYDYM EGARFRHTTQ FVRWRPDREP ASCTYEQLER PVNFDLAEVL AGRG
//