UniProt: A0A452QGR2

Database: UniProt
Entry: A0A452QGR2_URSAM

LinkDB:  A0A452QGR2_URSAM 
Original site:  A0A452QGR2_URSAM

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Ontology (18)   
   GO (18)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (22)   
   InterPro (12)   
   Pfam (5)   
   PROSITE (4)   
   SMART (1)   
All databases (44)   

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ID   A0A452QGR2_URSAM        Unreviewed;       911 AA.
AC   A0A452QGR2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   Name=LIG4 {ECO:0000313|Ensembl:ENSUAMP00000004110.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000004110.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000004110.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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; A0A452QGR2; -.
DR   STRING; 9643.ENSUAMP00000004110; -.
DR   Ensembl; ENSUAMT00000004683.1; ENSUAMP00000004110.1; ENSUAMG00000003773.1.
DR   GeneTree; ENSGT00860000133881; -.
DR   OMA; EGIMIKH; -.
DR   OrthoDB; 8251at2759; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
DR   GO; GO:0000793; C:condensed chromosome; IEA:Ensembl.
DR   GO; GO:0032807; C:DNA ligase IV complex; IEA:Ensembl.
DR   GO; GO:0005958; C:DNA-dependent protein kinase-DNA ligase 4 complex; IEA:Ensembl.
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:Ensembl.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR   GO; GO:0071479; P:cellular response to ionizing radiation; IEA:Ensembl.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:Ensembl.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; IEA:Ensembl.
DR   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IEA:Ensembl.
DR   GO; GO:2001252; P:positive regulation of chromosome organization; IEA:Ensembl.
DR   GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
DR   GO; GO:0000012; P:single strand break repair; IEA:Ensembl.
DR   GO; GO:0033151; P:V(D)J recombination; IEA:Ensembl.
DR   CDD; cd07903; Adenylation_DNA_ligase_IV; 1.
DR   CDD; cd17722; BRCT_DNA_ligase_IV_rpt1; 1.
DR   CDD; cd17717; BRCT_DNA_ligase_IV_rpt2; 1.
DR   CDD; cd07968; OBF_DNA_ligase_IV; 1.
DR   Gene3D; 6.10.250.520; -; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 2.
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; IPR044125; Adenylation_DNA_ligase_IV.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
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; IPR021536; DNA_ligase_IV_dom.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45997; DNA LIGASE 4; 1.
DR   PANTHER; PTHR45997:SF1; DNA LIGASE 4; 1.
DR   Pfam; PF00533; BRCT; 2.
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; PF11411; DNA_ligase_IV; 1.
DR   SMART; SM00292; BRCT; 2.
DR   SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR   SUPFAM; SSF52113; BRCT domain; 2.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50172; BRCT; 2.
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|ARBA:ARBA00023172,
KW   ECO:0000256|RuleBase:RU000617}; DNA repair {ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000617}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          355..489
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          654..743
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          845..911
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
SQ   SEQUENCE   911 AA;  104144 MW;  2791AD22043439B2 CRC64;
     MAASHTSPTV ASHVPFADLC STLERIQRSR GRAEKIRHFR EFLDSWRRFH DALHKNQRDV
     SDSFYPAMRL ILPQLERERM AYGIKETMLA KLYIELLNLP RGGKDALKLL NYRTPTGTRA
     DAGDFATIAY FVLKPRCLQK GSLTIQQVND ILDSIASNNS ARRKDLIKKS LLQLISQSSA
     LEQKWLIRMI VKDLKLGFSE QSVFSVFHND AAELHNVTTD LEKVCRQLHD PSIGLSDISI
     TLFSAFKPML AAIADIERIE KDMKHQSFYI ETKLDGERMQ MHRQGDVYQY FSRNGYNYTD
     QFGNSPQEGS LTPFIHSAFK TDVQICILDG EMMAFNPNTQ TFMQKGNKFD IKRMVEESDL
     QTCYCVFDVL MVNNKKLGRE TLKKRHEILT SVFTPIPGRI EIVQKTQAHT QKEVIDALNE
     AIDKREEGIM IKHPLSIYKP DKRGEGWLKI KPEYVDGLMD ELDILIVGGY WGKGSRGGMM
     SHFLCAIAEK PPPGEKPSVF HTLCRVGSGY TMKELYDLGL KLAKHWKPFH KKAPPSGILC
     GTEKPEVYIE PCHSVIVQVK ATEIVSSDMY KAGCTLRFPR IERIREDKEW HECTTVDDLE
     QLRGKASGKL ASKHLYVGDD DEPQEKKRKA APKVKKVIGI IEHLKAPNLS NVNKVSNIFE
     DVEFCVMSGM DSHPKPDLEN RIAEFGGYIV QNPGPDTYCV IAGSENIRVK NIISSNKHDV
     VKPEWLLECF KTKSCVPWQP RFMIHMCPST KEHFAREYDR YGDSYFVDTD LNQLKEVFSG
     IKNSGEQTPG EMASVIAHLE FRYSWDRCPL SMFRQHVIYV DVYAVINDLS TKIEGTRLAV
     MGLELRFHGA KVVSHLARGV SHVVVGEDRS RVADLKAFRR TLKRKFKILQ QDWVTDSIDK
     CELQEENRYL V
//

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