ID   A0A1A8WSR0_9APIC        Unreviewed;       911 AA.
AC   A0A1A8WSR0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
DE   Flags: Fragment;
GN   ORFNames=POVCU2_0091430 {ECO:0000313|EMBL:SBS94891.1};
OS   Plasmodium ovale curtisi.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=864141 {ECO:0000313|EMBL:SBS94891.1, ECO:0000313|Proteomes:UP000078560};
RN   [1] {ECO:0000313|Proteomes:UP000078560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Naeem Raeece;
RL   Submitted (MAY-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; FLQU01001900; SBS94891.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A8WSR0; -.
DR   Proteomes; UP000078560; 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   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   InterPro; IPR000977; DNA_ligase_ATP-dep.
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   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45674:SF4; DNA LIGASE 1; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 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   PROSITE; PS00697; DNA_LIGASE_A1; 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   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078560}.
FT   DOMAIN          841..911
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:SBS94891.1"
FT   NON_TER         911
FT                   /evidence="ECO:0000313|EMBL:SBS94891.1"
SQ   SEQUENCE   911 AA;  105274 MW;  B5912D2267854681 CRC64;
     KIKSSKMDKI YFNILFENTW LYEFSYYNDE HFILLENDNK TFDNDKNKCI TFLNPSTIII
     YSYSVNRFNK KYWKSNKNNN IIPKRLCPNE QNNCLNLKKN EKINSDIIMG SRQKLSACGS
     INRGKIYSME EKNTFSKYGN MKTSSFSTKD ISSHKGKIFY DSNNLISYNN KASEFHQNDK
     VKNIDLKNSL KLKRGNINFI ADRTSYNEHD EKKKKKNYTK YKTLRNIIQK RKNIELCNYK
     NIIYEKSCKD KQILNSIYRN NYYKENKTKD LFFVLDKNGE QKQKKEELPY QFNQSEKKEN
     FVTCNNEGNI FTKEIGCTNG DTKSKGKNEN EIKKGSLFNC KVYEDEKISD LASPKFNPAN
     FDISNLCLPE KDKAKHKFKD SLLFTFLTNT FNQIEELKGS GAGSKKNVAI ILSNVFRVLI
     YYSPNDLIPA VYITLNKVAP DYQNVEAGVG EALILKTMSE AYSRTEASIK KDLQQIEDLG
     IIAESCSCKM RTIFPLPRLT IQSVFNELKS IPNISGSNSQ QKKREVIKKL LVSAKTSEAK
     YIVRFLQQRL RIGVNSATVL QALAYAFVLT RPELPENIIK EGKMMNEKLL NESVAVKGDK
     DNCNDNATEI KNENNIKLEK KNDADNKTNA LDTDQFNDLV KSIKMRNERM SKPNLFYNIG
     KEGDTRLLPI FKELKNAYCD VNNDSDIFEC MEKSVKSALC ELPNIEMIIQ NLLNGDDMNV
     LMKKCTVKTG VPVQPMLAKP TKGIQEVLDR FNNVTFTCEY KYDGERAQIH YIDKDNIKIF
     SRNLETMTEK YPDVIQIVKD QIMPGVTESI IDSEVVAYDI ENKKILPFQI LTTRKRKDVD
     IENIKVKICL FPFDLICCNG VPVIKEPLEI RRKLLYSLLK CKEGVLEYAT HSEMNNIEDI
     DIFLQDAIEN N
//