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Database: UniProt
Entry: F3PMU4_9BACE
LinkDB: F3PMU4_9BACE
Original site: F3PMU4_9BACE 
ID   F3PMU4_9BACE            Unreviewed;       665 AA.
AC   F3PMU4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=DNA ligase {ECO:0000256|HAMAP-Rule:MF_01588};
DE            EC=6.5.1.2 {ECO:0000256|HAMAP-Rule:MF_01588};
DE   AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] {ECO:0000256|HAMAP-Rule:MF_01588};
GN   Name=ligA {ECO:0000256|HAMAP-Rule:MF_01588};
GN   ORFNames=HMPREF9446_00030 {ECO:0000313|EMBL:EGF59882.1};
OS   Bacteroides fluxus YIT 12057.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=763034 {ECO:0000313|EMBL:EGF59882.1, ECO:0000313|Proteomes:UP000003416};
RN   [1] {ECO:0000313|EMBL:EGF59882.1, ECO:0000313|Proteomes:UP000003416}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 12057 {ECO:0000313|EMBL:EGF59882.1,
RC   ECO:0000313|Proteomes:UP000003416};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA ligase that catalyzes the formation of phosphodiester
CC       linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-
CC       stranded DNA using NAD as a coenzyme and as the energy source for the
CC       reaction. It is essential for DNA replication and repair of damaged
CC       DNA. {ECO:0000256|ARBA:ARBA00004067, ECO:0000256|HAMAP-Rule:MF_01588}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-
CC         nicotinamide D-nucleotide.; EC=6.5.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00034005, ECO:0000256|HAMAP-
CC         Rule:MF_01588};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01588};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01588};
CC   -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01588}.
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:EGF59882.1}.
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DR   EMBL; AFBN01000003; EGF59882.1; -; Genomic_DNA.
DR   RefSeq; WP_009123413.1; NZ_GL882604.1.
DR   AlphaFoldDB; F3PMU4; -.
DR   STRING; 763034.HMPREF9446_00030; -.
DR   eggNOG; COG0272; Bacteria.
DR   HOGENOM; CLU_007764_2_0_10; -.
DR   Proteomes; UP000003416; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd00114; LIGANc; 1.
DR   Gene3D; 6.20.10.30; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 1.10.287.610; Helix hairpin bin; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_01588; DNA_ligase_A; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR041663; DisA/LigA_HHH.
DR   InterPro; IPR001679; DNA_ligase.
DR   InterPro; IPR033136; DNA_ligase_CS.
DR   InterPro; IPR013839; DNAligase_adenylation.
DR   InterPro; IPR013840; DNAligase_N.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004150; NAD_DNA_ligase_OB.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR004149; Znf_DNAligase_C4.
DR   NCBIfam; TIGR00575; dnlj; 1.
DR   PANTHER; PTHR23389; CHROMOSOME TRANSMISSION FIDELITY FACTOR 18; 1.
DR   PANTHER; PTHR23389:SF9; DNA LIGASE; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF01653; DNA_ligase_aden; 1.
DR   Pfam; PF03120; DNA_ligase_OB; 1.
DR   Pfam; PF03119; DNA_ligase_ZBD; 1.
DR   Pfam; PF12826; HHH_2; 1.
DR   Pfam; PF14520; HHH_5; 1.
DR   PIRSF; PIRSF001604; LigA; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM00278; HhH1; 4.
DR   SMART; SM00532; LIGANc; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_01588};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_01588};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_01588};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01588};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01588};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01588};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01588};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01588};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003416};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01588}.
FT   DOMAIN          587..665
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   ACT_SITE        112
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         31..35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         80..81
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         110
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         133
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         169
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         284
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         308
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         403
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         406
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         421
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         427
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
SQ   SEQUENCE   665 AA;  75058 MW;  7ED0EEFDADD53D6A CRC64;
     MTAKEKIDRL RAELHQHNYN YYVLNAPEIS DKEFDDKMHE LQNLEKEHPE YQDENSPTMR
     VGSDLNKNFT QVAHKYPMLS LGNTYSENEV TDFYDRVKKT LNEDFEICCE LKYDGTSISL
     TYEDGKLIRA VTRGDGEKGD DVTDNVKTIR TIPLVLHGNY PRSFEIRGEI LMPWESFEML
     NREREAREEP LFANPRNAAS GTLKSQNSAV VASRKLDAYL YYLLGEELPC DGHYENLQMA
     GSWGFKISEH TKKASSLEEV FEYINYWDTE RKNLPVATDG IVLKVNSLRQ QKNLGFTAKS
     PRWAIAYKFQ AERALTRLNK VSYQVGRTGA VTPVANLDPV QLSGTVVKRA SLHNADIIEG
     LDLHIGDMVY VEKGGEIIPK ITGVDKNARG MLLGEKVRFI THCPECGNRL IRYEGEAAHY
     CPNETACPPQ IKGRIEHFIS RKAMNIDGLG PETVDMFYRL GLIKDTADLY DLKADDIKNL
     DRMGEKSAEN IINGIAASKE VPFERVLFAL GIRFVGETVA KKIAKSFTDI EELINTDLEN
     LKNIDEIGEK IAQSIITYFS NPFNRELVGR LKAAGLQLFR KEEDLSGYTD KLTGQSIVIS
     GVFTHHSRDE YKELIEKNGG KNVGSISAKT SFILAGENMG PAKLEKAQKL GVKIMSEDEF
     LTLIS
//
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