ID   Q23RI5_TETTS            Unreviewed;      1026 AA.
AC   Q23RI5;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=TTHERM_00387050 {ECO:0000313|EMBL:EAR99063.1};
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:EAR99063.1, 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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; GG662644; EAR99063.1; -; Genomic_DNA.
DR   RefSeq; XP_001019308.1; XM_001019308.1.
DR   AlphaFoldDB; Q23RI5; -.
DR   STRING; 312017.Q23RI5; -.
DR   EnsemblProtists; EAR99063; EAR99063; TTHERM_00387050.
DR   GeneID; 7825974; -.
DR   KEGG; tet:TTHERM_00387050; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   HOGENOM; CLU_004844_0_0_1; -.
DR   InParanoid; Q23RI5; -.
DR   OMA; EGIMIKH; -.
DR   OrthoDB; 209192at2759; -.
DR   Proteomes; UP000009168; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07903; Adenylation_DNA_ligase_IV; 1.
DR   CDD; cd07968; OBF_DNA_ligase_IV; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 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; IPR044125; Adenylation_DNA_ligase_IV.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
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; IPR021536; DNA_ligase_IV_dom.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45997; DNA LIGASE 4; 1.
DR   PANTHER; PTHR45997:SF1; DNA LIGASE 4; 1.
DR   Pfam; PF16589; BRCT_2; 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   Pfam; PF11411; DNA_ligase_IV; 1.
DR   SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50172; BRCT; 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|ARBA:ARBA00023172,
KW   ECO:0000256|RuleBase:RU000617}; 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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          430..577
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          770..868
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          702..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        721..747
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1026 AA;  120320 MW;  C110753492BAE3B9 CRC64;
     MQNYYKWHKI KQEQNQELSV NIKPISSSKM KQSDISTRKK KAQEYNMDFD EFQQEDSKIN
     QNSDNFHFGD SADEYGIDSP KMKREKAVKE EDNTFRLEIK KSPILEKTLF SFLVKFYNQV
     QQSKKGQRKK FVQRFIDSTF KTNRCPSYTF TILRLIMPHH DKQRLNYGLN YKNLAKVLSE
     VFALSEDKRQ QLLNYKRPLK DNQQVVGDFG EVVQNVLQAF TQKATLTIND VDRCLDELAQ
     PQNRDLASKE KVLRNCLKNA TSEEIKWISR LILKDLNLGI NHEIILALFH PDAVVLFNST
     SSLWEVCKEF VDPNHKLSNV LRLFHPIKPM LAGRKTLKSI EAILKGKNYL VETKFDGERI
     QCHVSPESLM FFTRNSNNYT NIYERMIEHV RRSLKDAVHS CILDGEMVVV NKITGQRVQF
     GLNKTVAMER EDDELCICYK IFDILYLKTK DNKEYALTEY TLQYRKKILE NLIDNQQDRV
     EVIFGREYSD INDILTEFNE AIHRNDEGIV IKQLDTLYYP DDRSDKWIKM KGDYYEGIID
     TLDLIVIGGY FGEKSYKING IGDWTDHITH YLVAVAKKID LQNPSNSILV PFAKVGAGFT
     ARDYADIKAR MRDQWVRTNH SNKTPSFIIQ NWKPGEKDKP DAYILSPQNS LILEIRATEI
     IQSSQYPTNY TLRFPRFEKF RRDKDWFDCM KFNEIIEMTQ NLKKKEQKES DKEDNASDEE
     QDENGGKLKK KRKGQNGEEI EVNRQGRKPN WKTNKVMAQY LDIDVSDVKV ESNIFNNFVF
     NIINLPHEVS LSEEKILLEK AQIEKGIVAN GGKKVQNDSN LVTHYIASHY DFKVQVIGDH
     YKVNVLSLQW VKDCIKKKTL LDYSPRYIIY GQDQLLERNK LLYDQYGDSY YKDVDEDELL
     DILKSMKIDQ IEEEFQENEE FEEAVKDIIS MKNQLFKECF PQGQTYCFYN ANDKLNSDID
     LRYLVDLIQF SGNQVVFDLQ DEIDYIVALD YSEAENEKII TFREKNRSME VITPKNLLNN
     FGIALE
//