ID   F6EK69_HOYSD            Unreviewed;       352 AA.
AC   F6EK69;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   OrderedLocusNames=AS9A_4177 {ECO:0000313|EMBL:AEF42610.1};
OS   Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS   (Amycolicicoccus subflavus).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC   Hoyosella.
OX   NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF42610.1, ECO:0000313|Proteomes:UP000009235};
RN   [1] {ECO:0000313|EMBL:AEF42610.1, ECO:0000313|Proteomes:UP000009235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX   PubMed=21725023; DOI=10.1128/JB.05388-11;
RA   Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA   Wu X.L.;
RT   "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT   actinomycete isolated from crude oil-polluted soil.";
RL   J. Bacteriol. 193:4538-4539(2011).
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}.
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DR   EMBL; CP002786; AEF42610.1; -; Genomic_DNA.
DR   RefSeq; WP_013808959.1; NC_015564.1.
DR   AlphaFoldDB; F6EK69; -.
DR   STRING; 443218.AS9A_4177; -.
DR   KEGG; asd:AS9A_4177; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_008325_4_1_11; -.
DR   OrthoDB; 9770771at2; -.
DR   Proteomes; UP000009235; 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; cd07905; Adenylation_DNA_ligase_LigC; 1.
DR   CDD; cd07970; OBF_DNA_ligase_LigC; 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; IPR044119; Adenylation_LigC-like.
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   InterPro; IPR044117; OBF_LigC-like.
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   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   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AEF42610.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009235}.
FT   DOMAIN          118..255
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   352 AA;  39044 MW;  8DA503B3F3D21B5D CRC64;
     MQLPVMPPLA PMLAKAAATV PEQAPDASAE PTWLYEPKWD GFRAIVFRDG DDVVIGSRGG
     KDLSRYFPEV VTAVRDELPG RCVVDGEIVV PQSTEEGTRL DWEALSARIH PAERRVRQLS
     VDTPALFVGF DLLAHHDRSL LDAPFGERRG MLTELAAAEI GPARCHVTRA TNDAAVAQHW
     FETFEGAGLD GVIAKRLASR YLPNKRELVK VKHSRTAEAV VIGYRPHKSQ PGVGSVLLGL
     YDGDELKMVG GMSAFTNAKR IKIQEDLDGI RSGDRAEGEV SRWRTSADAG FVPVRPERVA
     EVAYDQMEGD RFRHAVRLLR WRPDRDPRSC TYDQLEVPVR YDLADVLEGS AR
//