ID   B4F6N5_XENTR            Unreviewed;       893 AA.
AC   B4F6N5;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   Name=lig3 {ECO:0000313|RefSeq:NP_001016351.2,
GN   ECO:0000313|Xenbase:XB-GENE-5788004};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI67946.1};
RN   [1] {ECO:0000313|RefSeq:NP_001016351.2}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAI67946.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=N6 {ECO:0000313|EMBL:AAI67946.1};
RC   TISSUE=Fat body {ECO:0000313|EMBL:AAI67946.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001016351.2}
RP   IDENTIFICATION.
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   EMBL; BC167946; AAI67946.1; -; mRNA.
DR   RefSeq; NP_001016351.2; NM_001016351.3.
DR   GeneID; 549105; -.
DR   KEGG; xtr:549105; -.
DR   AGR; Xenbase:XB-GENE-5788004; -.
DR   CTD; 3980; -.
DR   Xenbase; XB-GENE-5788004; lig3.
DR   OrthoDB; 162082at2759; -.
DR   Proteomes; UP000008143; Chromosome 10.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:0008270; F:zinc ion binding; IEA:InterPro.
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; cd07902; Adenylation_DNA_ligase_III; 1.
DR   CDD; cd07967; OBF_DNA_ligase_III; 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   Gene3D; 3.30.1740.10; Zinc finger, PARP-type; 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   InterPro; IPR001510; Znf_PARP.
DR   InterPro; IPR036957; Znf_PARP_sf.
DR   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF9; DNA LIGASE 3; 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   Pfam; PF00645; zf-PARP; 1.
DR   SMART; SM01336; zf-PARP; 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; SSF57716; Glucocorticoid receptor-like (DNA-binding 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.
DR   PROSITE; PS00347; ZF_PARP_1; 1.
DR   PROSITE; PS50064; ZF_PARP_2; 1.
PE   2: Evidence at transcript level;
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000617}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008143};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          61..153
FT                   /note="PARP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50064"
FT   DOMAIN          544..678
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          152..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          799..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..839
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        840..875
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   893 AA;  100464 MW;  797F437FB781E248 CRC64;
     MRAFLRLLAY QTKRTLGQSL TKVPLRVIFH ACWSQSPLHS ALHFQFFLRV THFSNMAEQR
     YCVEYAKRGT AGCKKCKEKI GKGLVRIGKI VPNPFSESAG DMKEWYHIKC MFEKLERARA
     TTKKIDDLTE LEGWQELQDC DKNLISQHVT ELATKTAATP RKKTPSKEKQ SPAVQGTTST
     TAPAASPSLK FSGFSAKPSQ SSSPPSSSTG SSLSTAKCDP KHKDCLLREF RKLCAMVAEQ
     PSYNSKTQII RDFLTKGTSG DGFHGDTYLT VKLLLPGVIK SVYNLNDKQI VKHFSRIFNC
     NQEEMVRDLE QGDVSETVRI FFEESKCFAP ASKSLLTIHE VDDLLTKLSK MTKEEDQQNV
     LEDIAHRCTS NDLKCIIRLI KHDLKMNSGA KHVLDALDPN AYDAFKASRN LGDVVERVLR
     NEQQAPGMKR TLSVQASLMT PVQPMLAEAC KSIEYAMKKC PNGMYAEIKY DGERVQVHKN
     GDHFSYFSRS LKPVLPHKVA HFKDFIPKAF PGGNSMILDA EVLLIDTNTG KPLPFGTLGV
     HKKAAFKDAN VCLFVFDCIY FNGVSLMDRP LSERRKFMRD NMVEIPNHIL FSEMKHVTKA
     SDLADMITRV IREGLEGLVL KDLKSNYEPG KRHWLKVKKD YLNEGAMADT ADLAVLGAYY
     GKGANGGIMS IFLMGCYDPE SQKWCTVTKC SSGYDDATLQ RLQKELNMVK ISKDPSKIPS
     WLKINKNYFP DFIIHDPKKA PIWEITGAEY SKAEAHTAAG LSIRFPRCTR FRDDKDWKTA
     TTLQQLKELY RLSKEKSDFN ITATSSQDED GSSESSSREN EGNSRQTASG SMVKKSKNAP
     SKSPGKDKTS ESTKLPPPQK KEELPKAEKR KSQTPKTVQS KKVRKQHIEK CIQ
//