ID A0A0C1JWR2_9BACT Unreviewed; 530 AA.
AC A0A0C1JWR2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN Name=lig {ECO:0000313|EMBL:KIC74876.1};
GN ORFNames=DB41_IB00090 {ECO:0000313|EMBL:KIC74876.1};
OS Neochlamydia sp. TUME1.
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Neochlamydia.
OX NCBI_TaxID=1478174 {ECO:0000313|EMBL:KIC74876.1, ECO:0000313|Proteomes:UP000031320};
RN [1] {ECO:0000313|EMBL:KIC74876.1, ECO:0000313|Proteomes:UP000031320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUME1 {ECO:0000313|EMBL:KIC74876.1,
RC ECO:0000313|Proteomes:UP000031320};
RX PubMed=25069652; DOI=10.1093/molbev/msu227;
RA Domman D., Collingro A., Lagkouvardos I., Gehre L., Weinmaier T.,
RA Rattei T., Subtil A., Horn M.;
RT "Massive expansion of Ubiquitination-related gene families within the
RT Chlamydiae.";
RL Mol. Biol. Evol. 31:2890-2904(2014).
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:KIC74876.1}.
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DR EMBL; JRXI01000136; KIC74876.1; -; Genomic_DNA.
DR RefSeq; WP_039385609.1; NZ_JRXI01000136.1.
DR AlphaFoldDB; A0A0C1JWR2; -.
DR PATRIC; fig|1478174.3.peg.1441; -.
DR Proteomes; UP000031320; 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; 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; 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; 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:KIC74876.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 306..434
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 530 AA; 61330 MW; BC36032DC79FE553 CRC64;
MKNFTELFDL IDQTSSTNEK LRYMEEYFKK VPSEDGAWAL FFLSGHRLKR LIGSKTLLSW
CGEITQLPAW LIEESYASVG DTAETISLLL EQSCSKNHLI DLPLSAWMEN LILPLKSKKE
EEQKSAVVEI WKSLSKKEIF IFNKILTGGF RIGVSQLSAI KAVSQALQVP KEVLSQRVMG
HWQPTANFFD SLRVVEEKNN YLNPYPFYLA SPLEGNLEAL IHPHEWQAEW KWDGIRAQVV
FREKAAAIWS RGNELISDQF PEILEGIQKF PHGTVLDGEI LAYENENPLS FGVLQKRLGR
KAPSKAIQKE APVVFMIYDL LEYNSVDLRK EALINRRKIL EELAEIHPKF LISPLIAFNA
WEQIHEKRLM AKHTLTEGIM LKRLNSPYGT GRQRGNWWKY KIDPMTIDAV LLYAQAGTGR
RANLYTDYTF GVWHQQELIP ITKAYSGLSQ QEIDKLDRWI RRNTEEKFGP VRKVKAEQVF
EIAFEGIQSS KRHKSGIALR FPRIARWRTD KPFTECDTLQ QIKLEFLNEQ
//
