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Database: UniProt
Entry: A0A255G8P8_9ACTN
LinkDB: A0A255G8P8_9ACTN
Original site: A0A255G8P8_9ACTN 
ID   A0A255G8P8_9ACTN        Unreviewed;       360 AA.
AC   A0A255G8P8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=CGZ94_17170 {ECO:0000313|EMBL:OYO10786.1};
OS   Enemella evansiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Enemella.
OX   NCBI_TaxID=2016499 {ECO:0000313|EMBL:OYO10786.1, ECO:0000313|Proteomes:UP000215896};
RN   [1] {ECO:0000313|EMBL:OYO10786.1, ECO:0000313|Proteomes:UP000215896}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML 030167 {ECO:0000313|EMBL:OYO10786.1,
RC   ECO:0000313|Proteomes:UP000215896};
RA   Bernier A.-M., Bernard K., Domingo M.-C.;
RT   "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL   Submitted (JUL-2017) 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   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572}.
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:OYO10786.1}.
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DR   EMBL; NMVO01000016; OYO10786.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255G8P8; -.
DR   OrthoDB; 9770771at2; -.
DR   Proteomes; UP000215896; 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; cd07905; Adenylation_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; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
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; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OYO10786.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215896}.
FT   DOMAIN          109..192
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   360 AA;  40195 MW;  976B73584782A3B1 CRC64;
     MDLPLTPMLA RVAEHIPAGM AYEPKWDGWR CVLARDGGEV RLWSRHGTEL TAHFPELVAA
     AAEQLPERCV VDGEIIIIAG DRLDYTRLAG RLAEVSRAAT LARESPGTLL IFDLLALDEH
     QLLDLPWEVR RELLEQIGDG LQAPLLLSPV TRDEELAHDW FDRFEGAGLD GVVAKPLGGR
     YAPGQRGWLK IKHRRTADVV VAGYRLDRTS TPERPQLGSL LLGLFDEQDQ LHAVGVCAGF
     PGAIRGELAE MFAALEQHPG DPAYEGHPWS PRSAARTGVR VPDHVTRWSR PRDQAHLIWP
     PLVAEVGFDQ LHDEVRFRSN TSFLRWRVDK DPVECRFDQL EPPVRFDLAA ILADATPDES
//
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