ID A0A1B1E4N7_9APIC Unreviewed; 918 AA.
AC A0A1B1E4N7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=PCOAH_00037630 {ECO:0000313|EMBL:ANQ09992.1};
OS Plasmodium coatneyi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium.
OX NCBI_TaxID=208452 {ECO:0000313|EMBL:ANQ09992.1, ECO:0000313|Proteomes:UP000092716};
RN [1] {ECO:0000313|Proteomes:UP000092716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hackeri {ECO:0000313|Proteomes:UP000092716};
RA Chien J.-T., Pakala S.B., Geraldo J.A., Lapp S.A., Barnwell J.W.,
RA Kissinger J.C., Galinski M.R., Humphrey J.C.;
RT "First high quality genome sequence of Plasmodium coatneyi using continuous
RT long reads from single molecule, real-time sequencing.";
RL Submitted (JUN-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 ECO:0000256|RuleBase:RU000617};
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
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DR EMBL; CP016250; ANQ09992.1; -; Genomic_DNA.
DR RefSeq; XP_019916687.1; XM_020060554.1.
DR AlphaFoldDB; A0A1B1E4N7; -.
DR EnsemblProtists; ANQ09992; ANQ09992; PCOAH_00037630.
DR GeneID; 30910494; -.
DR VEuPathDB; PlasmoDB:PCOAH_00037630; -.
DR OrthoDB; 162082at2759; -.
DR Proteomes; UP000092716; Chromosome 12.
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:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd07900; Adenylation_DNA_ligase_I_Euk; 1.
DR CDD; cd07969; OBF_DNA_ligase_I; 1.
DR Gene3D; 3.30.1490.70; -; 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; IPR016059; DNA_ligase_ATP-dep_CS.
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:SF4; DNA LIGASE 1; 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 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; PS00697; DNA_LIGASE_A1; 1.
DR PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000617};
KW DNA damage {ECO:0000256|RuleBase:RU000617};
KW DNA recombination {ECO:0000256|RuleBase:RU000617};
KW DNA repair {ECO:0000256|RuleBase:RU000617};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000617}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..918
FT /note="DNA ligase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008521615"
FT DOMAIN 649..785
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 99..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 918 AA; 104402 MW; 1B801CFC2FB3A16B CRC64;
MKLVVLLLIA RMLLCKVNSC MRREYAYIIP FMQKNKFYRR KTNFNVKVFT NFRDSASNRR
SDFLYGHIKK CLSFPKKTMD GQNEETDVKE ECKVKGEEKE SSKRKIASDG NTKTKKAKAK
SENDVKKGSL FNCAVREDDK VSDLTSPKFN PVHFDVSNLY LSQKDKEKHK FKDSLLFTFL
TNTFNQIEEL KGSGTGSKKN VAIILSNVFR VLIYYSPNDL IPAVYITLNK VAPDYLNVEA
GVGEALILKT MSEAYSRTES SIKKDLQQIE DLGIIAESCS CKMRTIFPLP RLTIQSVFNE
LKSIPNLSGS NSQQKKREVI KKLLVSAKTS EAKYIVRFLQ QRLRIGVNSA TVLQALSYAF
ILTRPSIPEE IVQKGKLMNE QLLSGKGNGS GEDDTVSDST TENEMNKVKT KKAGVLKVEK
QIGESPSHVK RENENQSVLD QFDFDALIQS IKMRNEKISK PNLFYDIGKE GDTRLLPIFK
ELKKSYCEVN NDSDIFECME KSVKSALCEL PNIEIIIQNL LNGDDMNTLS KKCTVKAGLP
VQPMLAKPTK GIQEVLDRFN NVTFTCEYKY DGERAQIHYI DKDNIKIFSR NLETMTEKYP
DVIQIVRDQI ISGAKECIID SEVVAYDIEN KKILPFQVLT TRKRKDVDIE NIKVKICLFP
FDLICCNGVP VIKEPLEIRR KLLYSLLKCK EGVLCYATHS EMNNIEDMDI FLQDAIENNC
EGLMVKTLLD NASYEPSRRS LNWLKVKKDY IEGLSDSVDL VPIAGYYGKG KRSGVYGAFV
LATYNSETEN FQTVCKAGTG FSDEILGSLY ETLSDKIIPN KKSYYEVSDK LNPDVWFDAH
YVWEVKAADL SLSPVHTAAI GVYSDDKGIG LRFPRFLRLR DDKNAEQATT SQQIVDLYEA
QFTYNKNKND FNEESESE
//
