ID A0A239V534_9MICO Unreviewed; 526 AA.
AC A0A239V534;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN ORFNames=SAMEA4475696_00183 {ECO:0000313|EMBL:SNV17327.1};
OS Dermatophilus congolensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Dermatophilus.
OX NCBI_TaxID=1863 {ECO:0000313|EMBL:SNV17327.1, ECO:0000313|Proteomes:UP000242637};
RN [1] {ECO:0000313|EMBL:SNV17327.1, ECO:0000313|Proteomes:UP000242637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13039 {ECO:0000313|EMBL:SNV17327.1,
RC ECO:0000313|Proteomes:UP000242637};
RG Pathogen Informatics;
RL Submitted (JUN-2017) 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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|RuleBase:RU004196}.
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DR EMBL; LT906453; SNV17327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239V534; -.
DR STRING; 1121387.GCA_000429885_01531; -.
DR KEGG; dco:SAMEA4475696_0183; -.
DR Proteomes; UP000242637; Chromosome 1.
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; 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: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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:SNV17327.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000242637}.
FT DOMAIN 298..422
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 526 AA; 56550 MW; 90890C3BE14F8B19 CRC64;
MAAAMLKGMK FSQVVATSQQ ISATRSRTAK VQAVAHTLRL AAPREARLVA HYLSGSLPQR
RTGVGARSLS NLPAPAATDT LHVADVDAII ADIAALSGSG SGTRRKEKLI DLFARATDNE
QRLLRDLFTG QVRHGALDGV LQTAIAVAAD VPVDAVRRAV MLAGSSAAVV EDALTGGVQA
LERVGLVVGR PLMPMLAASA PDVAEAVQQA GEGKKVAVER KLNGIRLQAH KNRDEVRLFT
RSLDDITDRL PEVVEVIAAI PAQKAVIDAE AIALRPDGRP HPFQVTAART ASRNDPAALA
ANTPVSTFVF DMLHRDGHDL LDLPAKERID QLNALIDEAH LVPRVITDRA EKTAEFFAAQ
IAAGHEGVVV KSLEAPYAAG RRGAGWIKVK PRHTLELVVL AVEWGSGRRS GKLSNIHLGA
SDGAGGFVML GKTFKGMTGE MLDWQTTRFL ELETHREGYV VHLRPEQVVE IAFDGLQQST
RYPAGLALRF ARVLRYRHDK TANHIDTIDT IRALAGSPSA ETDQRH
//
