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Database: UniProt
Entry: A0A1S2KFR0_9ACTN
LinkDB: A0A1S2KFR0_9ACTN
Original site: A0A1S2KFR0_9ACTN 
ID   A0A1S2KFR0_9ACTN        Unreviewed;       326 AA.
AC   A0A1S2KFR0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=BJP40_13950 {ECO:0000313|EMBL:OII66223.1};
OS   Streptomyces sp. CC53.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1906740 {ECO:0000313|EMBL:OII66223.1, ECO:0000313|Proteomes:UP000179639};
RN   [1] {ECO:0000313|EMBL:OII66223.1, ECO:0000313|Proteomes:UP000179639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC53 {ECO:0000313|EMBL:OII66223.1,
RC   ECO:0000313|Proteomes:UP000179639};
RA   Cruz-Morales P., Ramos-Aboites H.E., Barona-Gomez F.;
RT   "Functional and evolutionary genomics of ferrioxamines biosynthesis and
RT   transport.";
RL   Submitted (OCT-2016) 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:OII66223.1}.
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DR   EMBL; MKXB01000005; OII66223.1; -; Genomic_DNA.
DR   RefSeq; WP_071277534.1; NZ_MKXB01000005.1.
DR   AlphaFoldDB; A0A1S2KFR0; -.
DR   STRING; 1906740.BJP40_13950; -.
DR   Proteomes; UP000179639; 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; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR   CDD; cd07971; OBF_DNA_ligase_LigD; 1.
DR   Gene3D; 3.30.1490.70; -; 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.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OII66223.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000179639}.
FT   DOMAIN          115..234
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   326 AA;  35020 MW;  E8AA2DBF7AAB2C45 CRC64;
     MDLPLIAPML ATAGTLPPPA QDAAWAYETK QDGQRAVFYL PGDGTLALRS RSGEDITPAY
     PELRPLADAL PPGLAAVLDG EIVMPDERGR SDFARLQPRM GLAASPERAR RLAARAPVHA
     VLFDVLHLRG RLLTGLPWSE RRQELEALAL AGPTWSTPAA LVGHGAQALR ATEEHGLEGL
     LCKRIASRYA PGARSRDWIK IRNMRTADVV VCGWLPGAGR LTGLPGSVLM GQFEASGGGL
     RYVGAVGTGW SERERAELAR LLHASEAAAH PFVQAPPVAA AARWVVPRLV GEVRYATRTG
     GGLLRQPSWL RLRPDLSPEE SSAYLD
//
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