ID   C4M5H3_ENTH1            Unreviewed;       685 AA.
AC   C4M5H3; A0A175JSN5;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=EHI_111060 {ECO:0000313|EMBL:EAL52210.1};
OS   Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM).
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=294381 {ECO:0000313|EMBL:EAL52210.1, ECO:0000313|Proteomes:UP000001926};
RN   [1] {ECO:0000313|EMBL:EAL52210.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HM-1:IMSS {ECO:0000313|EMBL:EAL52210.1};
RX   PubMed=15729342; DOI=10.1038/nature03291;
RA   Loftus B.J., Anderson I., Davies R., Alsmark U.C., Samuelson J., Amedeo P.,
RA   Roncaglia P., Berriman M., Hirt R.P., Mann B.J., Nozaki T., Suh B., Pop M.,
RA   Duchene M., Ackers J., Tannich E., Leippe M., Hofer M., Bruchhaus I.,
RA   Willhoeft U., Bhattacharya A., Chillingworth T., Churcher C.M., Hance Z.,
RA   Harris B., Harris D., Jagels K., Moule S., Mungall K.L., Ormond D.,
RA   Squares R., Whitehead S., Quail M.A., Rabbinowitsch E., Norbertczak H.,
RA   Price C., Wang Z., Guillen N., Gilchrist C., Stroup S.E., Bhattacharya S.,
RA   Lohia A., Foster P.G., Sicheritz-Ponten T., Weber C., Singh U.,
RA   Mukherjee C., El-Sayed N.M.A., Petri W.A., Clark C.G., Embley T.M.,
RA   Barrell B.G., Fraser C.M., Hall N.;
RT   "The genome of the protist parasite Entamoeba histolytica.";
RL   Nature 433:865-868(2005).
RN   [2] {ECO:0000313|EMBL:EAL52210.1}
RP   GENOME REANNOTATION.
RC   STRAIN=HM-1:IMSS {ECO:0000313|EMBL:EAL52210.1};
RA   Lorenzi H., Amedeo P., Inman J., Schobel S., Caler E.;
RL   Submitted (MAR-2007) 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; DS571279; EAL52210.1; -; Genomic_DNA.
DR   RefSeq; XP_657595.1; XM_652503.2.
DR   AlphaFoldDB; C4M5H3; -.
DR   SMR; C4M5H3; -.
DR   STRING; 5759.C4M5H3; -.
DR   EnsemblProtists; GAT96687; GAT96687; CL6EHI_111060.
DR   EnsemblProtists; rna_EHI_111060-1; rna_EHI_111060-1; EHI_111060.
DR   GeneID; 3411902; -.
DR   KEGG; ehi:EHI_111060; -.
DR   VEuPathDB; AmoebaDB:EHI5A_198730; -.
DR   VEuPathDB; AmoebaDB:EHI7A_158980; -.
DR   VEuPathDB; AmoebaDB:EHI8A_180540; -.
DR   VEuPathDB; AmoebaDB:EHI_111060; -.
DR   VEuPathDB; AmoebaDB:KM1_253780; -.
DR   HOGENOM; CLU_005138_4_2_1; -.
DR   InParanoid; C4M5H3; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; 961at2759; -.
DR   BRENDA; 6.5.1.1; 2080.
DR   Proteomes; UP000001926; Partially assembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006266; P:DNA ligation; IBA:GO_Central.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR   GO; GO:1903461; P:Okazaki fragment processing involved in mitotic DNA replication; IBA:GO_Central.
DR   CDD; cd07900; Adenylation_DNA_ligase_I_Euk; 1.
DR   CDD; cd07969; OBF_DNA_ligase_I; 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; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000617};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001926}.
FT   DOMAIN          405..541
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          655..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          240..267
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        29..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        655..675
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   685 AA;  78164 MW;  594BA9A4207F93B7 CRC64;
     MSKRQSSLSR FFKPAKRATV GGQNNGENKS DEKGNEKKKQ ESIEEKNQSL QIKEEGNSFP
     EQKVKTLPFK GLADCFDALE NESGKLKKRE IYANYLKTVI TICPNDLTDV LNLTTGQIAP
     TWEGKELGIG DAILKDVVKS VTGLKLSQLN DKIKELGDIG IVAQNSKKNQ KLLVQPKPLT
     IQGVVLRMKE ILEADNSDIK KNKITALLVA AIGNEIRFIL RILKGVFRIG FTDRSLPPAI
     AQAVCSIRKE NNRIEELTEL ITNAVARVPS FQYLSEHITA NDPFEEFAKT NSVQLFIPFR
     PMLAKPKKSI TDITSRFKFP FTAEYKYDGE RGQIHFNKNK IMVFTRNLEN YTEKYPDVIE
     AVKDAVNPNI QSFIIDCEIV AFNRETNEFQ EFQILGRRAK KGVSVHSIAI NVCVNVFDIV
     YLNGKDLMDK PLKERRDILH STFHEVSQRF LFARFKNIEN EEDILPFFEE AINHRTEGLM
     CKTLIYDAEY IPDKRTDTWY KLKKDYLNGL ADTVDLVPVG AWMGEGKRAG VYGAFLLACR
     DEDSGDFETV TKVGTGFSDE ALQKLYEHLK TLECKEKKNV KHGDNLPDVW FEPKDVWEIK
     GADLSLSLQY KAGTKLVNTE GRGVCLRFPR YIRSRDDKEV NDITTNKQIY DLYKDQPSVR
     ETKDGQMKII NNDNEEESQE SEEKE
//