ID   A2DFX6_TRIV3            Unreviewed;       679 AA.
AC   A2DFX6;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=TVAG_162990 {ECO:0000313|EMBL:EAY20603.1};
OS   Trichomonas vaginalis (strain ATCC PRA-98 / G3).
OC   Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC   Trichomonas.
OX   NCBI_TaxID=412133 {ECO:0000313|EMBL:EAY20603.1, ECO:0000313|Proteomes:UP000001542};
RN   [1] {ECO:0000313|EMBL:EAY20603.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=G3 {ECO:0000313|EMBL:EAY20603.1};
RA   Amadeo P., Zhao Q., Wortman J., Fraser-Liggett C., Carlton J.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAY20603.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G3 {ECO:0000313|EMBL:EAY20603.1};
RX   PubMed=17218520; DOI=10.1126/science.1132894;
RA   Carlton J.M., Hirt R.P., Silva J.C., Delcher A.L., Schatz M., Zhao Q.,
RA   Wortman J.R., Bidwell S.L., Alsmark U.C.M., Besteiro S.,
RA   Sicheritz-Ponten T., Noel C.J., Dacks J.B., Foster P.G., Simillion C.,
RA   Van de Peer Y., Miranda-Saavedra D., Barton G.J., Westrop G.D., Mueller S.,
RA   Dessi D., Fiori P.L., Ren Q., Paulsen I., Zhang H., Bastida-Corcuera F.D.,
RA   Simoes-Barbosa A., Brown M.T., Hayes R.D., Mukherjee M., Okumura C.Y.,
RA   Schneider R., Smith A.J., Vanacova S., Villalvazo M., Haas B.J., Pertea M.,
RA   Feldblyum T.V., Utterback T.R., Shu C.L., Osoegawa K., de Jong P.J.,
RA   Hrdy I., Horvathova L., Zubacova Z., Dolezal P., Malik S.B.,
RA   Logsdon J.M. Jr., Henze K., Gupta A., Wang C.C., Dunne R.L., Upcroft J.A.,
RA   Upcroft P., White O., Salzberg S.L., Tang P., Chiu C.-H., Lee Y.-S.,
RA   Embley T.M., Coombs G.H., Mottram J.C., Tachezy J., Fraser-Liggett C.M.,
RA   Johnson P.J.;
RT   "Draft genome sequence of the sexually transmitted pathogen Trichomonas
RT   vaginalis.";
RL   Science 315:207-212(2007).
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; DS113196; EAY20603.1; -; Genomic_DNA.
DR   RefSeq; XP_001581589.1; XM_001581539.1.
DR   AlphaFoldDB; A2DFX6; -.
DR   STRING; 5722.A2DFX6; -.
DR   GeneID; 5466150; -.
DR   KEGG; tva:TVAG_2v0950900; -.
DR   VEuPathDB; TrichDB:TVAG_162990; -.
DR   VEuPathDB; TrichDB:TVAGG3_0950900; -.
DR   eggNOG; KOG0967; Eukaryota.
DR   InParanoid; A2DFX6; -.
DR   OMA; WIKYKRD; -.
DR   Proteomes; UP000001542; Unassembled 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   CDD; cd07900; Adenylation_DNA_ligase_I_Euk; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001542}.
FT   DOMAIN          416..561
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   679 AA;  77200 MW;  D0BDA8ADE832366C CRC64;
     MTQQGIAKFF GGKDIESTKK NAIVRKQVNV NISDFDNVFK DVEIPTVEGY NIPRDVVGYV
     AWNRGDPIPF TFITKMVDEL EPLTGKLEIN DLLCKYFLAI LMTTPKDIVP FVFLCLGQLR
     PNHEGVKINI GQESIISALG DKKVVKEKLK KEGDLSKVAQ QIRSTQKSMT SMFGKVNEAY
     TITGVYKEFL KMAGFQGANS DRNRTQTIQK LLTNCKPEEV KCIVRMLECK LRVGAAHESF
     LFALGMAFRR REYIMGMIKN NPDEEDLKDH GHLFREIYYR YPIIDEILVE FLRGSFKGAE
     KNINIKVGIP AMPMLAKPAK KLDEIKRRLG DGRITGEYKY DGERAQIHKN KEGKVRIFSR
     SAEDSTAKFA DVADIITDNV KGEQYILDSE IVAYDPEKHV ILPFQTLMNR PKKGTDTPSA
     IHVCVCAFDL LSYNGVSMLD EPLEKRRDKL HEIVTVVPTK LQLATYKNAS KIEDLGDFFE
     EAVSNRTEGL MVKTLNGRYE CGKRAMSWAK LKKDYISKEV FKGGVAEEIP PDTIDVVVIG
     ATYGKGKRTS VYGAFLVGVY NNVTGKVESL CFVGTGFKED DLKEFYEKLH PLEMEKCPDN
     VDCRPLDQDP VFFKPELVWE IQVADIQTTP TYSACWGELG EKGLTIRFGR YYRTRTDKTW
     EQSTSTEQLL ELYHQQFEK
//