ID A0A0Q4RSY2_9FLAO Unreviewed; 533 AA.
AC A0A0Q4RSY2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN ORFNames=ASF10_15870 {ECO:0000313|EMBL:KQO20553.1};
OS Flavobacterium sp. Leaf82.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1736238 {ECO:0000313|EMBL:KQO20553.1, ECO:0000313|Proteomes:UP000051828};
RN [1] {ECO:0000313|EMBL:KQO20553.1, ECO:0000313|Proteomes:UP000051828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf82 {ECO:0000313|EMBL:KQO20553.1,
RC ECO:0000313|Proteomes:UP000051828};
RX PubMed=26633631; DOI=.1038/nature16192;
RA Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL Nature 528:364-369(2015).
RN [2] {ECO:0000313|Proteomes:UP000051828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf82 {ECO:0000313|Proteomes:UP000051828};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf82 {ECO:0000313|Proteomes:UP000051828};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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 -!- 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:KQO20553.1}.
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DR EMBL; LMMA01000036; KQO20553.1; -; Genomic_DNA.
DR RefSeq; WP_056254439.1; NZ_LMMA01000036.1.
DR AlphaFoldDB; A0A0Q4RSY2; -.
DR OrthoDB; 9767858at2; -.
DR Proteomes; UP000051828; Unassembled WGS sequence.
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: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; cd07897; Adenylation_DNA_ligase_Bac1; 1.
DR CDD; cd07972; OBF_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; IPR026333; ATP_dep_DNA_lig_pp_1105_fam.
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; TIGR04120; DNA_lig_bact; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KQO20553.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 303..435
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 533 AA; 62103 MW; ADC5B968A08E52EE CRC64;
MKNFAELIKA LDSSNKTSVK VDALTNYFIN ASNEDKVWTI AILSHRRPPR PVNTTLLRLW
ANELANIPLW LFEESYHIVG DLAETIALVI PTTHEHSDKS LTEYLQEIIA LKKKTDIEKK
EYLQENWLAL NYYERFVFTK LITGSFRIGV SQKLMTRALS KAENIDEDSL AHKLMGDWNP
NTISFQELIL DEKNSDYLSK PFPFYLAYPI EGEPSNLGNA EDWSAEHKWD GIRSQTIIRD
NEIFIWSRGE ELVTDKYPEF AAFIGIIPDG TVIDGEILPF IENEIGTFND LQTRIGRKTV
SAAVLKKSPV IIKAYDLLEW KGQDIRNLPF EERRILLEQL FEDIKHNDIP LQLSERVKFS
TWEELTEERL RSREMRSEGL MIKRKDSPYL VGRKKGDWWK WKIEPLVIDA VLTYAMRGHG
RRSNLFTDYT FALWHNNENN ERELVTFAKA YSGLTDAEFR MVDDWIKKNT LERFGPVRSV
TPQLVFEIGF EGIALSKRHK SGIATRFPRI LRWRHDKKIK EANSIEDLKS MIL
//
