ID G3T2A3_LOXAF Unreviewed; 915 AA.
AC G3T2A3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN Name=LIG1 {ECO:0000313|Ensembl:ENSLAFP00000007286.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000007286.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000007286.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000007286.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000007286.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000007286.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; G3T2A3; -.
DR STRING; 9785.ENSLAFP00000007286; -.
DR Ensembl; ENSLAFT00000008675.3; ENSLAFP00000007286.3; ENSLAFG00000008673.3.
DR eggNOG; KOG0967; Eukaryota.
DR GeneTree; ENSGT00940000157783; -.
DR HOGENOM; CLU_005138_0_2_1; -.
DR InParanoid; G3T2A3; -.
DR OMA; WIKYKRD; -.
DR TreeFam; TF300342; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0006284; P:base-excision repair; IEA:Ensembl.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; 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; 3.30.1490.70; -; 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; PS00333; DNA_LIGASE_A2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646}.
FT DOMAIN 645..781
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 915 AA; 100799 MW; AF42721E415C6B95 CRC64;
LPCSCRSFFQ PKKEGKAKKP EKETSNSSRE TEPPPKVALK ERNGVVPESE SPVKRLVRKA
ARVLSSEEEE EDSALTSLKG QKPAPGSPKA SPPSPAASLE SIPSPSEASP VEVSPSGIPK
RRTARKQLPK RKIQDVLEEQ SGKHLSSSKK KKSPEAETPA ESVTEPEVAK KKEAEDEDQP
RMSPKPCKTS EAETPAESTS EPAVGVKKEP QEGDQTKPSP RPSKRISSFF TPRKPATKKE
VKEEGSGAPG EEETKGPLDP ADYNPAKNNY HPIEDACWKS GQKVPYLAVA RTFEKVEEVS
ARLRMVETLS NLLRSVVALS PPDLLPVLYL SLNRLGPPQQ GLELGVGDGV LLKAVAQATG
RQLESVRAEA AEKGDVGLVA ESSRTTQRIM LPPPPLTASG VFAKFRDIAR LAGSASTAKK
IDIIKGLFVA CRHSEARFIA RSLSGRLRLG LAEQSVLAAL AQAVSLTPPG QEFPPAVVDA
GKGRTAEARK MWLDEQGMVL KQTFCEVPDL DCIVPVLLEH GLEHLPEHCR LSPGIPLKPM
LAHPTRGVSE VLKRFEEAAF TCEYKYDGQR AQIHVLEGGE VKIFSRNQED NTGKYPDIID
RIPKIKLPSV TSFILDTEAV AWDREKKQIQ PFQVLTTRKR KDVDASEIQV QVCLYAFDLI
YLNGESLVRE PLSRRRQLLR ENFVETEGEF VFATSLDTKD TDQIAEFLEQ SVRDSCEGLM
VKTLDVDATY EIAKRSHNWL KLKKDYLEGV GDTLDLVVIG AYLGRGKRAG RYGGFLLATY
DKESEELQAI CKLGTGFSDE ELEKHHQSLQ ALVLPSPRSY VRADGAVAPD HWLEPSTVWE
VKCADLSLSP IYPAARGLVD REKGISLRFP RFIRIRDDKK PEEATTSAQV AQLYQAQSQI
QNQKGASSES DLEDF
//