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Database: UniProt/TrEMBL
Entry: F6BHW1_THEXL
LinkDB: F6BHW1_THEXL
Original site: F6BHW1_THEXL 
ID   F6BHW1_THEXL            Unreviewed;       307 AA.
AC   F6BHW1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   OrderedLocusNames=Thexy_0579 {ECO:0000313|EMBL:AEF16630.1};
OS   Thermoanaerobacterium xylanolyticum (strain ATCC 49914 / DSM 7097 / LX-11).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacterium.
OX   NCBI_TaxID=858215 {ECO:0000313|EMBL:AEF16630.1, ECO:0000313|Proteomes:UP000007239};
RN   [1] {ECO:0000313|Proteomes:UP000007239}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Hemme C., Woyke T.;
RT   "Complete sequence of Thermoanaerobacterium xylanolyticum LX-11.";
RL   Submitted (MAY-2011) 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; CP002739; AEF16630.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6BHW1; -.
DR   STRING; 858215.Thexy_0579; -.
DR   KEGG; txy:Thexy_0579; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_008325_4_0_9; -.
DR   OMA; AGFRWHK; -.
DR   Proteomes; UP000007239; 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; IPR012340; NA-bd_OB-fold.
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:AEF16630.1}.
FT   DOMAIN          114..250
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   307 AA;  35477 MW;  747381AA61B829DF CRC64;
     MSLMDEKISP MLAISGNVFD DPSWVYEIKW DGSRTIAFLS STTKLQDRRL VDISHQFPEL
     MEVNKCLKSN EAILDGELIV LKDNKPSYRN IMMRKHQQNK LKIELLSKYN PAIFITWDVI
     YVDGKELLNY PLIKRKEILS KIVSEGNLIR ISDYIFGQGK TLFAETGKKQ LEGVMAKKAD
     SKYYLGKRSS LWQKFKHHII LNAVILGYKI DKTALVLGLY NEDDKLVHIG NVESGISQKE
     LSSFLEVAND LKVNPEFYGL AINNVQWIMP FIVCKVKFME WSENFKMRAP SFLEFALDVK
     PTECRFM
//
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