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Database: UniProt/TrEMBL
Entry: A0A1D7QJY0_9SPHI
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Original site: A0A1D7QJY0_9SPHI 
ID   A0A1D7QJY0_9SPHI        Unreviewed;       530 AA.
AC   A0A1D7QJY0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=BFS30_18490 {ECO:0000313|EMBL:AOM78981.1};
OS   Pedobacter steynii.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=430522 {ECO:0000313|EMBL:AOM78981.1, ECO:0000313|Proteomes:UP000094313};
RN   [1] {ECO:0000313|EMBL:AOM78981.1, ECO:0000313|Proteomes:UP000094313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DX4 {ECO:0000313|EMBL:AOM78981.1,
RC   ECO:0000313|Proteomes:UP000094313};
RA   Seilhamer J.J.;
RL   Submitted (AUG-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};
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DR   EMBL; CP017141; AOM78981.1; -; Genomic_DNA.
DR   RefSeq; WP_069380644.1; NZ_CP017141.1.
DR   AlphaFoldDB; A0A1D7QJY0; -.
DR   KEGG; psty:BFS30_18490; -.
DR   OrthoDB; 9767858at2; -.
DR   Proteomes; UP000094313; 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: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; IPR016059; DNA_ligase_ATP-dep_CS.
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; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 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:AOM78981.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094313}.
FT   DOMAIN          303..434
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   530 AA;  60518 MW;  BDFE73C417788A00 CRC64;
     MKRFTALIAQ LELSNKTNDK IAALVRYFNE AEDLDKPYVI AMFTGKRPRR PVSTALMKEW
     AINLSGIPAW LFAESYHSVG DLSETIALIL PPPTSTTDLP LHQWINALAA LNGQDDESKK
     RFIERAWDSL DMQERFVFNK LISGNFRIGV SNKMLVNALA KQSDLESNQI MHSIMGKWKP
     DEISYQELIA GAHVDTDRSW PYPFCLAYAL DTEPQSLGNI KEWQAEWKWD GIRGQIVKRG
     GELFIWSRGE ELVTDQFPEL HFLIDHLEDG TVLDGEILSV KEGKIQPFSL LQQRLNRKTI
     SKAQLLAAPI AFYVYDLLEY QGADQRGKTL QVRRDQLTTV IKNTGNQEAI VISPVINVES
     WEALALLRAD SRLQNSEGLM LKKLDSLYHS GRKRGDWWKW KINPYTVDAV MIYAQKGSGR
     RANFFTDYTF AVRDGEQLIT IAKAYSGLTD QEIKEVDAFV RKNAIEKFGP VRTVKPELVF
     EIAFEGIAES KRHKAGLALR FPRIARWRKD KKAAEINTLE DLRQLLQSTL
//
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