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Database: UniProt/TrEMBL
Entry: D3T4F8_THEIA
LinkDB: D3T4F8_THEIA
Original site: D3T4F8_THEIA 
ID   D3T4F8_THEIA            Unreviewed;       307 AA.
AC   D3T4F8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   OrderedLocusNames=Thit_1868 {ECO:0000313|EMBL:ADD03110.1};
OS   Thermoanaerobacter italicus (strain DSM 9252 / Ab9).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=580331 {ECO:0000313|EMBL:ADD03110.1, ECO:0000313|Proteomes:UP000001552};
RN   [1] {ECO:0000313|EMBL:ADD03110.1, ECO:0000313|Proteomes:UP000001552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9252 / JCM 16815 / Ab9 {ECO:0000313|Proteomes:UP000001552};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Hemme C.L., Woyke T.;
RT   "Complete sequence of Thermoanaerobacter italicus Ab9.";
RL   Submitted (FEB-2010) 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   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572}.
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DR   EMBL; CP001936; ADD03110.1; -; Genomic_DNA.
DR   RefSeq; WP_012995821.1; NC_013921.1.
DR   AlphaFoldDB; D3T4F8; -.
DR   KEGG; tit:Thit_1868; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_008325_4_0_9; -.
DR   OMA; AGFRWHK; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000001552; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR   CDD; cd07971; OBF_DNA_ligase_LigD; 1.
DR   Gene3D; 3.30.1490.70; -; 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; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR014146; LigD_ligase_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR02779; NHEJ_ligase_lig; 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   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ADD03110.1}.
FT   DOMAIN          114..196
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   307 AA;  35913 MW;  420BA1920D3A5FD4 CRC64;
     MTMIEEKISP MLAFSSDPFD NPEWIYEIKW DGSRTIAFLS NKTRLQDRRL VDITHQFPDL
     ALLHKQIKAK EAILDGELVV LKNGKPSYKS IMSRKHQQNL VKINLLSKIM PVIFITWDIL
     YLNGKSLVEL PLIERKDILR KTVKESEVIK ISDFIFEHGK RLFEETGKRG LEGIVAKKVD
     SKYLIGKRSK LWLKSKHFIV INAVIIGYRT DKTALILGLY DEENNLINIG SCESGLSQKE
     LKAFYEVAKE IKAPDNYYNF KEKNVQWLKP LLTCKVRFME WSENMKMRAP SFIQFEYNVK
     PEECRFE
//
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