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Database: UniProt
Entry: A0A0F0LZQ8_9MICO
LinkDB: A0A0F0LZQ8_9MICO
Original site: A0A0F0LZQ8_9MICO 
ID   A0A0F0LZQ8_9MICO        Unreviewed;       343 AA.
AC   A0A0F0LZQ8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=RR49_00654 {ECO:0000313|EMBL:KJL38853.1};
OS   Microbacterium ginsengisoli.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=400772 {ECO:0000313|EMBL:KJL38853.1, ECO:0000313|Proteomes:UP000033451};
RN   [1] {ECO:0000313|EMBL:KJL38853.1, ECO:0000313|Proteomes:UP000033451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18659 {ECO:0000313|EMBL:KJL38853.1,
RC   ECO:0000313|Proteomes:UP000033451};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) 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:KJL38853.1}.
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DR   EMBL; JYIY01000060; KJL38853.1; -; Genomic_DNA.
DR   RefSeq; WP_045246636.1; NZ_JYIY01000060.1.
DR   AlphaFoldDB; A0A0F0LZQ8; -.
DR   STRING; 400772.RR49_00654; -.
DR   PATRIC; fig|400772.4.peg.688; -.
DR   OrthoDB; 9770771at2; -.
DR   Proteomes; UP000033451; 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   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; 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:KJL38853.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033451}.
FT   DOMAIN          117..230
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   343 AA;  37315 MW;  2111EFC3403E76E6 CRC64;
     MRYDVPAPML AKGVDAIPDA AGLSFEPKWD GFRVLAAWDG TEVELASRGA KPLTRYFPEI
     VDALPRVLPG PCVIDGELVV ATGEPGAQRL DWEALSARIH PAASRVTRLA TETPAMLIAF
     DLIAEGDDPL VDAPFRERRA RLERMLAGVG HPVHLTRTTL DADVAGRWLA EFEGAGLDGV
     VAKRLDEPYA PGKRTMLKIK HARTADVVAL GYRVHASGAG VGSLLVGLYG DDGELRQVGG
     VSAFTAARRL ELVDELAPLV ERDADGEVVT GAGERSRFTG SKDVSFVRLR PERVLEVRYD
     QLEGARFRHT VQFERWRPDR DAASCTFAQL EQIAAYDLAA VLD
//
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