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Database: UniProt
Entry: A0A101URD2_9ACTN
LinkDB: A0A101URD2_9ACTN
Original site: A0A101URD2_9ACTN 
ID   A0A101URD2_9ACTN        Unreviewed;       238 AA.
AC   A0A101URD2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=AQJ91_41140 {ECO:0000313|EMBL:KUO15493.1};
OS   Streptomyces dysideae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO15493.1, ECO:0000313|Proteomes:UP000053260};
RN   [1] {ECO:0000313|EMBL:KUO15493.1, ECO:0000313|Proteomes:UP000053260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RV15 {ECO:0000313|EMBL:KUO15493.1,
RC   ECO:0000313|Proteomes:UP000053260};
RA   Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J.,
RA   Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces sp. RV15, isolated from a marine
RT   sponge.";
RL   Submitted (OCT-2015) 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   -!- 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:KUO15493.1}.
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DR   EMBL; LMXB01000111; KUO15493.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101URD2; -.
DR   STRING; 909626.AQJ91_41140; -.
DR   OrthoDB; 3733803at2; -.
DR   Proteomes; UP000053260; Unassembled WGS sequence.
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; 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; 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.
PE   4: Predicted;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053260}.
FT   DOMAIN          32..159
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|Pfam:PF01068"
FT   DOMAIN          158..222
FT                   /note="DNA ligase ATP-dependent C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04679"
FT   REGION          216..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..230
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   238 AA;  26916 MW;  78E88923CD0DDE25 CRC64;
     MLDTLDAEQR RLLDKARPGE RTGRAAVPDR RRLSDTYPEI VDALADQPCG DFTVDGEIVA
     FSRGRTDFAR LQQRMALTRR RDVEASGVAV TYYVFDLLRL DGRDTTGLPL WARRSLLRRA
     PAIRSPLRTT PHRNAGGAEL LAESCERGWE GLIAKRADRR TLLALRERLD ELRTSGSPFD
     GPVREAGARW VEPELVAQID FTEWTRDGML RHPRYLGLRD DKKPTDVARE RPSGRAAA
//
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