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Database: UniProt/TrEMBL
Entry: A0A1B1NCN7_9MICO
LinkDB: A0A1B1NCN7_9MICO
Original site: A0A1B1NCN7_9MICO 
ID   A0A1B1NCN7_9MICO        Unreviewed;       560 AA.
AC   A0A1B1NCN7;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=SGUI_1778 {ECO:0000313|EMBL:ANS79174.1};
OS   Serinicoccus hydrothermalis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Ornithinimicrobiaceae; Serinicoccus.
OX   NCBI_TaxID=1758689 {ECO:0000313|EMBL:ANS79174.1, ECO:0000313|Proteomes:UP000092482};
RN   [1] {ECO:0000313|EMBL:ANS79174.1, ECO:0000313|Proteomes:UP000092482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLT9 {ECO:0000313|EMBL:ANS79174.1,
RC   ECO:0000313|Proteomes:UP000092482};
RA   Tang K.;
RT   "Shallow-sea hydrothermal system.";
RL   Submitted (MAR-2016) 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|RuleBase:RU004196}.
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DR   EMBL; CP014989; ANS79174.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B1NCN7; -.
DR   STRING; 1758689.SGUI_1778; -.
DR   KEGG; serj:SGUI_1778; -.
DR   PATRIC; fig|1758689.4.peg.1842; -.
DR   Proteomes; UP000092482; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07901; Adenylation_DNA_ligase_Arch_LigB; 1.
DR   Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 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; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF13; DNA LIGASE-RELATED; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ANS79174.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092482}.
FT   DOMAIN          347..470
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   560 AA;  59560 MW;  8B074FE041F4261E CRC64;
     MSNGPASIDV SHARRGSAKG GYADGKKLVK FGPGARTLDR TSVTGVRHTA GMQLAQVTET
     SAAVAGTRSR TAKTGLLAEA LELAARGGDD REVEVVADYL AGTLPQRTVG VGWRSLRERP
     GPAGEATLSV LEVDAALSEL KALSGAGSTA ARARALSDLL GRATAQEQDW LVGLLTGELR
     QGAGDGVLLP AVAQAAQVPE ALVRRAVMLA GFPGPVARAA LGDGAPALEQ VRLEVGRPLR
     PMLAGSEPDV ASAVDGTREV ALDLKLDGIR LQAHLDRDAD PADPVRLFTR SLEEITDRLP
     EVVAAVAALP ARTAVLDGEV IALDAEGRPE PFQVTGARTA SRTDPVELAR TTPVTTYLFD
     VLHLDGRDLV DEPAHERWRV LGELAPELVV ERLTTDDPGA AQAFFDRVVG QGHEGVVVKD
     PQAPYAAGRR GAGWVKVKPR RTADLVVTGV EWGSGRRQGW LSNIHLAARG ADGELVMVGK
     TFKGMTDELL TWQTERFLGL ETSREGHVVQ VRPEQVVEVA YDAVQTSRRY AGGVALRFAR
     VLRYRDDKGV EEIDTVESLR
//
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