ID I6DJS4_SHIBO Unreviewed; 373 AA.
AC I6DJS4;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=DNA ligase (NAD(+)) {ECO:0000256|ARBA:ARBA00012722};
DE EC=6.5.1.2 {ECO:0000256|ARBA:ARBA00012722};
GN ORFNames=SB444474_4278 {ECO:0000313|EMBL:EIQ32016.1};
OS Shigella boydii 4444-74.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=766140 {ECO:0000313|EMBL:EIQ32016.1, ECO:0000313|Proteomes:UP000004199};
RN [1] {ECO:0000313|EMBL:EIQ32016.1, ECO:0000313|Proteomes:UP000004199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4444-74 {ECO:0000313|EMBL:EIQ32016.1,
RC ECO:0000313|Proteomes:UP000004199};
RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., Jones K.,
RA Santana-Cruz I., Liu X.;
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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};
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:EIQ32016.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKNB01000283; EIQ32016.1; -; Genomic_DNA.
DR AlphaFoldDB; I6DJS4; -.
DR PATRIC; fig|766140.3.peg.4329; -.
DR Proteomes; UP000004199; Unassembled WGS sequence.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; IPR018239; DNA_ligase_AS.
DR InterPro; IPR033136; DNA_ligase_CS.
DR InterPro; IPR013839; DNAligase_adenylation.
DR InterPro; IPR013840; DNAligase_N.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004150; NAD_DNA_ligase_OB.
DR PANTHER; PTHR47810; DNA LIGASE; 1.
DR PANTHER; PTHR47810:SF1; DNA LIGASE B; 1.
DR Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS01055; DNA_LIGASE_N1; 1.
DR PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE 4: Predicted;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EIQ32016.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027}.
FT DOMAIN 1..367
FT /note="NAD-dependent DNA ligase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00532"
SQ SEQUENCE 373 AA; 41643 MW; 22C0551407F7E0CB CRC64;
MEDGVYDQLS ARLTQWQRCF VSEPRDVMMP PLNGAVMHPV AHTGVRKMAD KNALSLWMRE
RSDLWVQPKV DGVAVTLVYR DGKLNKAISR GNGLKGEDWT QKVSLISAVP QTVSGPLANS
TLQGEIFLQR EGHIQQQMGG INARAKVAGL MMRQDDSDTL NSLGVFVWAW PDGPQLMSDR
LKELATAGFT LTQTYTRAVK NADEVARVRN EWWKAELPFV TDGVVVRAAK EPESRHWLPG
QAEWLVAWKY QPVAQVAEVK AIQFAVGKSG KISVVASLAS VMLDDKKVQR VNIGSVRRWQ
EWDIAPGDQI LVSLAGQGIP RIDDVVWRGA ERTKPTPPEN RFNSLTCYFA SDVCQEQFIS
RLVWLNRPGN PGD
//
