UniProt: A0A3M0K176

Database: UniProt
Entry: A0A3M0K176_HIRRU

LinkDB:  A0A3M0K176_HIRRU 
Original site:  A0A3M0K176_HIRRU

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (22)   
   InterPro (12)   
   Pfam (5)   
   PROSITE (4)   
   SMART (1)   
All databases (32)   

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ID   A0A3M0K176_HIRRU        Unreviewed;       912 AA.
AC   A0A3M0K176;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=DUI87_16184 {ECO:0000313|EMBL:RMC06738.1};
OS   Hirundo rustica rustica.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC   Hirundo.
OX   NCBI_TaxID=333673 {ECO:0000313|EMBL:RMC06738.1, ECO:0000313|Proteomes:UP000269221};
RN   [1] {ECO:0000313|EMBL:RMC06738.1, ECO:0000313|Proteomes:UP000269221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Chelidonia {ECO:0000313|EMBL:RMC06738.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:RMC06738.1};
RA   Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA   Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT   "A high quality draft genome assembly of the barn swallow (H. rustica
RT   rustica).";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RMC06738.1}.
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DR   EMBL; QRBI01000120; RMC06738.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0K176; -.
DR   STRING; 333673.A0A3M0K176; -.
DR   Proteomes; UP000269221; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; 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; 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:UP000269221};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          360..494
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          659..748
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          809..912
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
SQ   SEQUENCE   912 AA;  104067 MW;  BFBD54850E709A1E CRC64;
     MASAPVSQPP PKKTVASHVP FADLCSTLER IQKCKSRPEK SKYFKDFLDS WRKFHDALHQ
     KEKDVTDSFY PAMRLILPQL ERERMAYGIK ETMLAKLYIE LLNLPKDGKD AAKLLNYRTP
     TGSRGDAGDF AMIAYFVLKP RSPKQGRLTI EQVNEHLDVI ANNNAAKNKG QLKKSLLQLI
     TQSTALEQKW LIRMIIKDLK LGVSQQTIFS IFHPDAAELH NVTTDLEKVC RQLHDPSVSL
     SDVSIMLFSA FKPMLAAIAD VQQIEKQMSN QTFYIETKLD GERMQMHKDG DVYKYFSRNG
     FDYTQQFGAS PLEGSLTPFI HNVFKSNIQN CILDGEMMAY NPETQTFMQK GNKFDIKRMV
     EDSDLQTCFC VFDVLMVNDQ KLGHEVLSKR YEILSSVFTP VKGRLHVVHK RSGRTRKEVI
     DALNEAIDNR EEGIMVKDPM STYKPDKRGE GWLKIKPEYV NGLMDELDLL IVGGYWGKGS
     RGGMMSHFLC AIAETPPPNE KPTIFHSICR VGSGYTMKEL YDLGLKLAKH WKPYHRKDPP
     GNILCGTEKP EMYIEPCNSV IVQIKAAEIV DSDMYKTGCT LRFPRIEKIR EDKEWYECMT
     SDMLEDLRSK AQGKLASKHL HVDEYDEPHE KKRKTVSKVR KIIGIAEQFK APDLSSVSKV
     SNVFEDVEFC VMTGMGKYSK SELESKIAEC GGSVVQNPGP ETYCVIVGAE NVRVKNIIAS
     NKYDVVRAEW LLQCFQTKML VPWQPAFMIH MSPDTKEHFA REYDCYGDSY TANTDVAPLK
     EVFSRMKDNK PMPLDVIAEL EERYWWNSCR LSIFRGSTIY VDCYAVVSEP ESKIPGTTLS
     IRALELRFYG AKVVSHLEEG VSHVVVGEDH SRVEQMKALR RTFGKKFKIV SELWVTHSVE
     EGVAKNENQY LV
//

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