ID   Q24FD9_TETTS            Unreviewed;       648 AA.
AC   Q24FD9;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 2.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=TTHERM_00865240 {ECO:0000313|EMBL:EAS06519.2};
OS   Tetrahymena thermophila (strain SB210).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=312017 {ECO:0000313|EMBL:EAS06519.2, ECO:0000313|Proteomes:UP000009168};
RN   [1] {ECO:0000313|Proteomes:UP000009168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX   PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA   Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA   Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA   Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA   Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA   Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA   Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA   Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA   Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA   Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA   Hamilton E.P., Orias E.;
RT   "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT   model eukaryote.";
RL   PLoS Biol. 4:1620-1642(2006).
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; GG662285; EAS06519.2; -; Genomic_DNA.
DR   RefSeq; XP_001026764.2; XM_001026764.2.
DR   AlphaFoldDB; Q24FD9; -.
DR   SMR; Q24FD9; -.
DR   STRING; 312017.Q24FD9; -.
DR   EnsemblProtists; EAS06519; EAS06519; TTHERM_00865240.
DR   GeneID; 7839837; -.
DR   KEGG; tet:TTHERM_00865240; -.
DR   eggNOG; KOG0967; Eukaryota.
DR   HOGENOM; CLU_005138_1_2_1; -.
DR   InParanoid; Q24FD9; -.
DR   OrthoDB; 162082at2759; -.
DR   Proteomes; UP000009168; 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; 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; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF9; DNA LIGASE 3; 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   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:UP000009168}.
FT   DOMAIN          374..505
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          618..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..648
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   648 AA;  75028 MW;  89DC8E41AF9C629B CRC64;
     MIKKLLYLPK QSLLSSLIFS KFCTQFNSKS IQSFYFLAKQ FDDISKISSR NSGIEAIETL
     MNDYIQGGDN ELFIQMVRLL TCKVDSEEIQ IANSSLVEIL KVVYPQEDIT KFLFEKGDIG
     LYAKEMLEKK LEKEGNNRTE KNHLSILEVT SFFEKLKNLQ GDRSRLEKQE LIIDFLKKIQ
     DPLEIQYFIR ILSKSLRIGV SEKSIIKALT NINKKKKNSL DSLLKNVQDK IFGYNTALHT
     DIQIGTPVPP MLAKPVSDFD ELLKFLKKYE SKKVSLELKY DGERCQVHYG KKKGIKLFSR
     NLEIQNEKYP QLVQQLEKYF QKNNSVEDCI LDGEIVVTDS KGNIKSFQEQ QQNRKRKQDS
     NKVVAFDEDN IEKIYLFDIL FLNACEQNTK EQLYRKSLIK ENFPIEGPVN HAESKIFDLS
     IQKDFDELKK LVKQYIDQKE EGAMVKSLDS NTFYDNNGRT QWAKLKKQVL SGGLADTFDV
     IPIAAYYGKG KRSGVYGSYL LACYDDKKKE YVALCKIGTG FSDQFLQDST DRLKQKVCSQ
     KPKEYSVHRT FKPDVWFQKD AEVWEVESDS LSSSPIYTIG KMNYSDNGIS LRFPRFLRVR
     DDKTTEQSTK TYQIIEFYNK QQAKPNNNSK DQKGDHGDKG EEEEEGDK
//