ID A0A0D2GPN4_9BACT Unreviewed; 592 AA.
AC A0A0D2GPN4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, 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=J120_03475 {ECO:0000313|EMBL:KIX85334.1};
OS candidate division TM6 bacterium JCVI TM6SC1.
OC Bacteria; Candidatus Dependentiae; Vermiphilus.
OX NCBI_TaxID=1306947 {ECO:0000313|EMBL:KIX85334.1, ECO:0000313|Proteomes:UP000032214};
RN [1] {ECO:0000313|EMBL:KIX85334.1, ECO:0000313|Proteomes:UP000032214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM6SC1 {ECO:0000313|EMBL:KIX85334.1,
RC ECO:0000313|Proteomes:UP000032214};
RX PubMed=23754396; DOI=10.1073/pnas.1219809110;
RA McLean J.S., Lombardo M.J., Badger J.H., Edlund A., Novotny M.,
RA Yee-Greenbaum J., Vyahhi N., Hall A.P., Yang Y., Dupont C.L., Ziegler M.G.,
RA Chitsaz H., Allen A.E., Yooseph S., Tesler G., Pevzner P.A., Friedman R.M.,
RA Nealson K.H., Venter J.C., Lasken R.S.;
RT "Candidate phylum TM6 genome recovered from a hospital sink biofilm
RT provides genomic insights into this uncultivated phylum.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E2390-E2399(2013).
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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
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:KIX85334.1}.
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DR EMBL; ARQD01000002; KIX85334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2GPN4; -.
DR STRING; 1306947.J120_03475; -.
DR eggNOG; COG1793; Bacteria.
DR Proteomes; UP000032214; 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:0071897; P:DNA biosynthetic process; IEA:InterPro.
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; cd07901; Adenylation_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; IPR000977; DNA_ligase_ATP-dep.
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; TIGR00574; dnl1; 1.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45674:SF9; DNA LIGASE 3; 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; PS00333; DNA_LIGASE_A2; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000032214}.
FT DOMAIN 328..464
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 592 AA; 66317 MW; 0978BCF419340430 CRC64;
MKFKALADAF AQIEQESGRI KITHILAQTL SNANGHEAQI ICNLSLGQLH PPYIGTQFAL
AEKSIIKVLA VILSLSAENV LKERARLGDL GLVFKEYASI EHMKHDLDVV AVYEFLVRIE
NLGGAGSQEA KQHALLELLR QVDGLSGCYI IRIILAKLRL GFSDMTLIDA LSFMVTGDKS
LRSALEHAYN ICVDLGLIAQ TLKDHGIDAI KHMEIQLGIP IRPAAAERLP NAKQIIEKIG
PCIVEPKIDG FRLQIHIEQQ GSNKKIHFFS RNLTDMSDSF PDLYKACEQW PIHSLIAEGE
AIVFDPANGR FVPFQETVKR KRKHDIVSVM QQLPLQLFLF DALYINGTSM LDKPYTVRRA
ELEKISQLNQ SSSIQLIQDR TCTTAQEMQG YFDQALAHGL EGLMAKRPDS LYQPGKRNFN
WIKLKKHQES SVEDTIDCVI LGYYLGSGKR TSFGIGAFLV GVYDKPNDRF ETIAKVGTGL
SDQDWKILKT ECDKYKASEK PMNVVCVPEL YPSVWVDPVI VCEIFADEIT LSPLHTAGKG
TGAGQGFALR FPRFLGYRPD KTATESTQVT EIKRMYHDQK KQELPENDNK DS
//
