ID A0A0D9QTF6_PLAFR Unreviewed; 913 AA.
AC A0A0D9QTF6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 08-NOV-2023, entry version 38.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=AK88_00281 {ECO:0000313|EMBL:KJP90112.1};
OS Plasmodium fragile.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5857 {ECO:0000313|EMBL:KJP90112.1, ECO:0000313|Proteomes:UP000054561};
RN [1] {ECO:0000313|EMBL:KJP90112.1, ECO:0000313|Proteomes:UP000054561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=nilgiri {ECO:0000313|Proteomes:UP000054561};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Duraisingh M., Young S.K., Zeng Q., Gargeya S., Abouelleil A.,
RA Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium fragile nilgiri.";
RL Submitted (MAR-2014) 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; KQ001646; KJP90112.1; -; Genomic_DNA.
DR RefSeq; XP_012333355.1; XM_012477932.1.
DR AlphaFoldDB; A0A0D9QTF6; -.
DR EnsemblProtists; KJP90112; KJP90112; AK88_00281.
DR GeneID; 24265595; -.
DR VEuPathDB; PlasmoDB:AK88_00281; -.
DR OMA; CYATHSE; -.
DR OrthoDB; 162082at2759; -.
DR Proteomes; UP000054561; Unassembled WGS sequence.
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 ECO:0000256|RuleBase:RU000617};
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..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..913
FT /note="DNA ligase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012791295"
FT DOMAIN 644..780
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 78..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 913 AA; 103672 MW; 0AC9102E1A961041 CRC64;
MKLLVLLLIA RMLLCKINSC MRREYAYIIP FMQKNKFYKR KTVFNVKVFT NFTNIASNRH
SDFLKCFSFP KKTMDEQKDE TDVKEESKMK KEEKETTKRK ITSDGNTKAK KAKGKSENDI
KKGSLFNCSV TEDDKVSDLT SPKFNPVHFD VSNLYLSPKD KEKHKFKDSL LFTFLTNTFN
QIEELKGSGT GSKKNVAIIL SNVFRVLIYY SPNDLIPAVY ITLNKVAPDY LNVEAGVGEA
LILKTMSEAY SRTESSIKKD LQQIEDLGII AESCSCKMRT IFPLPRLTIQ SVFNELKSIP
NLSGSNSQQK KREVIKKLLV SAKTSEAKYI VRFLQQRLRI GVNSATVLQA LSYAFIITRP
SIPEEIVQKG KLMNEQLLSG KGSGIGQDST VSGTTTEDDM NKLKGEKEGV VKVEKTNEES
PSNIKKEKEN QSVPDHFDFE ALVQSIKIRN EKISKPNLFY DIGKEGDTRL LPIFKELKKS
YCGANDDSDI FECMEKSVKS ALCELPNIEI IIQNLLSGDD MNTLSKKCTV KAGLPVQPML
AKPTKGIQEV LDRFNNVTFT CEYKYDGERA QIHYIDKDNI KIFSRNLETM TEKYPDVIQI
VRDQIISGAK ECIIDSEVVA YDIENKKILP FQVLTTRKRK DVDIENIKVK ICLFPFDLIC
CNGVPVIKEP LEIRRKLLYS LLKCKDGVLC YATHSEMNNI EDIDIFLQDA IENNCEGLMV
KTLLDNASYE PSRRSLNWLK VKKDYIEGLS DSVDLVPIAG YYGKGKRSGV YGAFVLATYN
SETENFQTVC KAGTGFSDEI LGSLYETLSD KIIPNKKSYY EVSDKLNPDV WFDAHYVWEV
KAADLSLSPV HTAAIGVYSD DKGIGLRFPR FLRLREDKNA EQATTSQQIV DLYEAQFTYN
KNKNDFNEES ESE
//