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Database: UniProt
Entry: X1FKD3_9ZZZZ
LinkDB: X1FKD3_9ZZZZ
Original site: X1FKD3_9ZZZZ 
ID   X1FKD3_9ZZZZ            Unreviewed;       369 AA.
AC   X1FKD3;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=DNA ligase (NAD(+)) {ECO:0000256|ARBA:ARBA00012722};
DE            EC=6.5.1.2 {ECO:0000256|ARBA:ARBA00012722};
DE   Flags: Fragment;
GN   ORFNames=S03H2_06032 {ECO:0000313|EMBL:GAH29844.1};
OS   marine sediment metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=412755 {ECO:0000313|EMBL:GAH29844.1};
RN   [1] {ECO:0000313|EMBL:GAH29844.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Expedition CK06-06 {ECO:0000313|EMBL:GAH29844.1};
RX   PubMed=24624126; DOI=10.3389/fmicb.2014.00080;
RA   Kawai M., Futagami T., Toyoda A., Takaki Y., Nishi S., Hori S., Arai W.,
RA   Tsubouchi T., Morono Y., Uchiyama I., Ito T., Fujiyama A., Inagaki F.,
RA   Takami H.;
RT   "High frequency of phylogenetically diverse reductive dehalogenase-
RT   homologous genes in deep subseafloor sedimentary metagenomes.";
RL   Front. Microbiol. 5:80-80(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-
CC         nicotinamide D-nucleotide.; EC=6.5.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00034005};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAH29844.1}.
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DR   EMBL; BARU01002583; GAH29844.1; -; Genomic_DNA.
DR   AlphaFoldDB; X1FKD3; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.70; -; 1.
DR   Gene3D; 6.20.10.30; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR041663; DisA/LigA_HHH.
DR   InterPro; IPR001679; DNA_ligase.
DR   InterPro; IPR033136; DNA_ligase_CS.
DR   InterPro; IPR013839; DNAligase_adenylation.
DR   InterPro; IPR013840; DNAligase_N.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004150; NAD_DNA_ligase_OB.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR004149; Znf_DNAligase_C4.
DR   NCBIfam; TIGR00575; dnlj; 1.
DR   Pfam; PF01653; DNA_ligase_aden; 1.
DR   Pfam; PF03120; DNA_ligase_OB; 1.
DR   Pfam; PF03119; DNA_ligase_ZBD; 1.
DR   Pfam; PF12826; HHH_2; 1.
DR   Pfam; PF14520; HHH_5; 1.
DR   SMART; SM00278; HhH1; 4.
DR   SMART; SM00532; LIGANc; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR   PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE   4: Predicted;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1..212
FT                   /note="NAD-dependent DNA ligase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00532"
FT   DOMAIN          210..229
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          244..263
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          276..295
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          308..327
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:GAH29844.1"
FT   NON_TER         369
FT                   /evidence="ECO:0000313|EMBL:GAH29844.1"
SQ   SEQUENCE   369 AA;  40978 MW;  0D64CBA9C7A54735 CRC64;
     PDTHWEIMEY LKSLGFKVNP SIALYHTVDE VEKCHQNWVE KRDDLPYEAD GMVVKVDLIA
     FQRELGTVAH EPRWAIAYKF PAIQGTTRLV DIGVNVGRTG SLNPYAILEP VRVGGVVISR
     AALHNEEDIH RKDIRIGDWV TVQRAGEVIP EIVGPIVSRR TGEEKTFFMP GRCPVCGSEV
     IKPEDEAMHK CTNAACPSQA LERIKHFVSR GAMDIDGVGE KLCQALFEAG LVKDVADLYY
     LTKEQLLGLE RMADKSVSNV LNSIEGSKNR PLSRIIFALG ILHVGEEYAE LLAENFNSID
     ELAKANQEEL LSLPSIGNKI ADSIVAFFRQ EGNKRIIEKL GKAGVKLERG KAEEAKPEEL
     PLAGLEFVL
//
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