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Database: UniProt
Entry: A0A089KRA0_9BACL
LinkDB: A0A089KRA0_9BACL
Original site: A0A089KRA0_9BACL 
ID   A0A089KRA0_9BACL        Unreviewed;       315 AA.
AC   A0A089KRA0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=R70331_04855 {ECO:0000313|EMBL:AIQ50922.1};
OS   Paenibacillus sp. FSL R7-0331.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1536773 {ECO:0000313|EMBL:AIQ50922.1, ECO:0000313|Proteomes:UP000029487};
RN   [1] {ECO:0000313|EMBL:AIQ50922.1, ECO:0000313|Proteomes:UP000029487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R7-0331 {ECO:0000313|EMBL:AIQ50922.1,
RC   ECO:0000313|Proteomes:UP000029487};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-2014) 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; CP009284; AIQ50922.1; -; Genomic_DNA.
DR   RefSeq; WP_042173292.1; NZ_CP009284.1.
DR   AlphaFoldDB; A0A089KRA0; -.
DR   STRING; 1536773.R70331_04855; -.
DR   KEGG; paee:R70331_04855; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_008325_4_0_9; -.
DR   Proteomes; UP000029487; Chromosome.
DR   GO; GO:0005524; F:ATP 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   CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR   CDD; cd07971; OBF_DNA_ligase_LigD; 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; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR45674:SF15; DNA LIGASE (ATP); 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 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   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AIQ50922.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029487}.
FT   DOMAIN          105..223
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   315 AA;  35134 MW;  563E385CB62B149D CRC64;
     MEVKPVKPFE PVLAAQLPSG SQWIAQIKWD GVRMLSCYDG SSIELVNRRG NRRTLQYPEL
     TVQGRYCRAD SYILDGEVIA LSGGKPSFHE VMRRDGLRSE AAVRAVKPQV PVLYMVFDIL
     YCNGEWLLDR PLSVRQQLLQ DVLLPHPHVQ NVPSYTDPAQ LFAAACKGGL EGIICKDIRS
     TYAPGGKDAR WQKRKNILDV TAVAGGVTFR DGMVNALLLG LYDDEGRLHY IGHAGAGRLT
     ATDWRNLTAQ AHNLEVPVMP FTGVPQRSKD AVWIRPSLVF KLHFLEWNAS GTLRQPVIQA
     QVDLPPDACR LEQRG
//
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