ID A0A1H8XU16_9PSEU Unreviewed; 359 AA.
AC A0A1H8XU16;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-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=SAMN04489732_10920 {ECO:0000313|EMBL:SEP43307.1};
OS Amycolatopsis saalfeldensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=394193 {ECO:0000313|EMBL:SEP43307.1, ECO:0000313|Proteomes:UP000198582};
RN [1] {ECO:0000313|EMBL:SEP43307.1, ECO:0000313|Proteomes:UP000198582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44993 {ECO:0000313|EMBL:SEP43307.1,
RC ECO:0000313|Proteomes:UP000198582};
RA de Groot N.N.;
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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOEF01000009; SEP43307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8XU16; -.
DR STRING; 394193.SAMN04489732_10920; -.
DR OrthoDB; 9770771at2; -.
DR Proteomes; UP000198582; 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; 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.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:SEP43307.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198582}.
FT DOMAIN 11..196
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|Pfam:PF01068"
FT DOMAIN 218..329
FT /note="DNA ligase ATP-dependent C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04679"
SQ SEQUENCE 359 AA; 39771 MW; 21691510C9784CA5 CRC64;
MALPVLAPIK PMLAKPAKAI PDSGGLLFEP KWDGFRCLVF RDGDELTLQS RAEKPLNRYF
PEVVERLLET LPDQVVLDGE LVVARDGKLD FDALTERIHP ADSRVQLLAK ESPAEFVAFD
VLALGSESFV DEPTSARRAR LEQLAGDGFH LTPATTDPDT ARHWFELFEG AGLDGVIGKP
LGEPYTPGKR VLFKYKHSRT ADCVLAGLRW HVDGAPGEAV GSFLLGLHDG DGLLHHVGVV
GSFPAARRRE LATELAPLVT DGEGHPWLGD AVREGQRIPG GITRWRSKEQ PWVPLRLERV
VEVSYEHTEG GDPARFRHTA QFARWRPDRE PSSCGYAQLE EPARYDLSAV FRGEVVRTR
//