ID A0A3Q7TIX1_VULVU Unreviewed; 912 AA.
AC A0A3Q7TIX1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN Name=LIG1 {ECO:0000313|RefSeq:XP_025869643.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025869643.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025869643.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025869643.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025869643.1};
RG RefSeq;
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 RefSeq; XP_025869643.1; XM_026013858.1.
DR AlphaFoldDB; A0A3Q7TIX1; -.
DR Proteomes; UP000286640; Unplaced.
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; 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:UP000286640}.
FT DOMAIN 642..778
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 912 AA; 100917 MW; F5AF85982420B7FC CRC64;
MQRSIMSFFY PKKEGKVKKP EKETSNSIRE TEPPPKVALK ERNGEVPESD SPVKRPGRKV
ARVLGSEGEE EDEALTPSKA QKPAPGSPQG SPPSPVTYPE SSPSLSTTSP VDISAGIPKR
RTARKQLPKR TIQDVLEEQS KDEDREAKKK KEEEAETPPE SLSESEVTQE KEAEGEDQPV
TSPEHRETSQ PPVDSTLEPA VSGKQEAQKE DSAKLPTRAP KTVSSFFAPR KPATKKEGKE
EDPGTPRQEE TKGPLDPPSY NPAKNNYHPI DDACWKPGQK VPYLAVARTF EKIEEVSARL
RMVETLSNLL RSVVALSPPD LLPILYLSLN RLGPPQQGLE LGVGDGVLLK AVAQATGRQL
DSVKAEAAEK GDVGLVAENS RSTQRLMLPP PALTAAGVFA KFRDIARLAG SASTAKKIDV
IKGLFVACRH SEARFIARAL SGRLRLGLAE QSVLAALAQA VSLTPPGQEF PPAIVDAGKG
RTAEARKTWL EEQGMILKQT FCEVPDLDRI IPVLLEHGLE HLPEHCRLSP GVPLKPMLAH
PTRGVSEVLK RFEEAAFTCE YKYDGQRAQI HVLEGGEVKI FSRNQEDNTG KYPDIISRIP
KIKLPSVTSF ILDTEAVAWD REKKQIQPFQ VLTTRKRKEV DAAEIQVQVC LYAFDLIYLN
GESLVREPLS RRRQLLRENF VETEGEFVFA TSLDTKDTDQ IAEFLEQSVK DSCEGLMVKT
LDVDATYEIA KRSHNWLKLK KDYLDGVGDT LDLVVIGAYL GRGKRAGRYG GFLLAAYDEE
SEELQAICKL GTGFSDEELE EHYQRLQTLV LPTPRSYVRV DGAVAPDHWL DPSAVWEVKC
ADLSLSPIYP AARGLVDGEK GISLRFPRFI RVREDKKPEE ATTSGQVACL YMKQSQIQNQ
QGADLDSDSD FY
//