ID C6LSR2_GIAIB Unreviewed; 790 AA.
AC C6LSR2;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=GL50581_1804 {ECO:0000313|EMBL:EET00951.1};
OS Giardia intestinalis (strain ATCC 50581 / GS clone H7) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=598745 {ECO:0000313|EMBL:EET00951.1, ECO:0000313|Proteomes:UP000002488};
RN [1] {ECO:0000313|EMBL:EET00951.1, ECO:0000313|Proteomes:UP000002488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50581 / GS clone H7 {ECO:0000313|Proteomes:UP000002488};
RX PubMed=19696920; DOI=10.1371/journal.ppat.1000560;
RA Franzen O., Jerlstrom-Hultqvist J., Castro E., Sherwood E., Ankarklev J.,
RA Reiner D.S., Palm D., Andersson J.O., Andersson B., Svard S.G.;
RT "Draft genome sequencing of giardia intestinalis assemblage B isolate GS:
RT is human giardiasis caused by two different species?";
RL PLoS Pathog. 5:E1000560-E1000560(2009).
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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
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:EET00951.1}.
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DR EMBL; ACGJ01002208; EET00951.1; -; Genomic_DNA.
DR AlphaFoldDB; C6LSR2; -.
DR EnsemblProtists; EET00951; EET00951; GL50581_1804.
DR VEuPathDB; GiardiaDB:GL50581_1804; -.
DR OMA; DERSHAW; -.
DR OrthoDB; 961at2759; -.
DR Proteomes; UP000002488; Unassembled WGS sequence.
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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd07900; Adenylation_DNA_ligase_I_Euk; 1.
DR CDD; cd07969; OBF_DNA_ligase_I; 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; 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; IPR036599; DNA_ligase_N_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00574; dnl1; 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 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 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|RuleBase:RU000617};
KW DNA repair {ECO:0000256|RuleBase:RU000617};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000617}.
FT DOMAIN 530..667
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 88169 MW; 734E55A663276EF6 CRC64;
MQLSIDAFLQ QKSPSNGEPP RKVKKAGSTT STTTKVNLDT HPPGATNVSA TGGGYEIGKD
SSFPFMSLST AWKRIEDTTK RLEKSREMVQ MLLQIYLEST KDIVPAVLLS TNQLREPWSD
LPSVLNFAEL SLRKVISRTF GSDISTIQKL IEKHGDIGVV AEKVKKSQSA TFAPRKPLNI
ADVYNKLLQI ADTSGASSMD DKSTIISDLL YNGTALDTRY ISRLIAGKFR LGIQKKSIIA
NLADLLCCII LCKIKGVTAK SRISDVYDML LSYGKVPMIK TTDSVVEPSG KRTTDGNSIH
DDSDAYACSD DSAFTDDSDI HLERSYSDLL SINSKKLRTH CHIVVSKAYS SCPSFEVILN
QIITHCGEGS ENDKKQTNVD GVLAALNSMT IRPGVPVLSM LARPTTSYDE IIQRVSCEQS
FSAEYKYDGF RAQVHYDARA STNKIQIFSR SLENMSKRFP DVSDSVLESF KSSALFAEMT
AEEKKCAGFV IDGEICPINT DTGLVLPFQY LSRREKDILK AQRDAKQEKE TKTRTSIVMY
AFDILFLNSN DYLSVDLADR KKALYHAFAS LPRRFEFARA VTCTQHTNLK ELLEEAVQNK
TEGLIVKILR SRDSWYRPDE RSHAWLKLKK DYLNDVGDSF DLVPVAAWMG TGKRTGVLGA
YLLASFNEEC DQWETVCQLG TGFSDADLAA FHESFVKCGM HDKPASIEAH LDKEPDMWFD
PETSQVWEVK CANLSLSMKH TLCFNAETGQ GISLRLPRLL RARPDKKPWD CTKASIIFEA
FMSQPERAQT
//
