ID   F4CD67_SPHS2            Unreviewed;       532 AA.
AC   F4CD67;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   OrderedLocusNames=Sph21_1108 {ECO:0000313|EMBL:ADZ77678.1};
OS   Sphingobacterium sp. (strain 21).
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ77678.1};
RN   [1] {ECO:0000313|EMBL:ADZ77678.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=21 {ECO:0000313|EMBL:ADZ77678.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA   Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT   "Complete sequence of Sphingobacterium sp. 21.";
RL   Submitted (MAR-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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002584; ADZ77678.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4CD67; -.
DR   STRING; 743722.Sph21_1108; -.
DR   KEGG; shg:Sph21_1108; -.
DR   PATRIC; fig|743722.3.peg.1188; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_005138_6_2_10; -.
DR   OrthoDB; 9767858at2; -.
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:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07897; Adenylation_DNA_ligase_Bac1; 1.
DR   CDD; cd07972; OBF_DNA_ligase_Arch_LigB; 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; IPR026333; ATP_dep_DNA_lig_pp_1105_fam.
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; TIGR04120; DNA_lig_bact; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF13; DNA LIGASE-RELATED; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ADZ77678.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          304..435
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   532 AA;  61379 MW;  87F64E02459F3D58 CRC64;
     MRAFNELFEE IDRTTSTNAK VEALVRYFRS AHNQDLLWCV YLLMGKSTGR FVKTAILRQA
     AIQLSQLPAW LFEESYHVVG DLAETIALCL PPPLEPKAYT LNETMAFLHD LKNLSDEEME
     AALSSRWMHT PNNHRFVFNK LITGNFRMGA SKQLVIKALS ITFDKPESEM AHRLMGNWHP
     TTADVQQLLL TEMPKDERSF EPYPFYLAYQ LDKDPESLGN VDEWFIERKY DGIRGQIIVR
     NGSLYIWSRG EDLLTDKFPE FHPLADLLPN GTVIDGEILP FKDEKVLPFS VMQTRTGRKQ
     LSKKILADAP LIMICYDLLE YDGEDIRARP LETRRNLLVT LLEKLPRDIP LLISGIIPCD
     TWHDVARARE EARAYQCEGV MLKRKQSIYE TGRRRGNWWK WKVEPYTIDG VLIYGQRGHG
     RRANLYTDYT FAVWDNGELV PFAKAYSGLT DKEILEVDAW IKRHTIDKFG PVRSVTPTLV
     FELAFEGISS SPRHKSGIAL RFPRIVRWRK DKPAKEANTK ADLLALLKQQ KA
//