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Database: UniProt
Entry: A0A0N4T5Q9_BRUPA
LinkDB: A0A0N4T5Q9_BRUPA
Original site: A0A0N4T5Q9_BRUPA 
ID   A0A0N4T5Q9_BRUPA        Unreviewed;       639 AA.
AC   A0A0N4T5Q9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=BPAG_LOCUS3510 {ECO:0000313|EMBL:VDN84696.1};
OS   Brugia pahangi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0000354001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BPAG_0000354001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN84696.1, ECO:0000313|Proteomes:UP000278627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-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   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; UZAD01001059; VDN84696.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N4T5Q9; -.
DR   STRING; 6280.A0A0N4T5Q9; -.
DR   WBParaSite; BPAG_0000354001-mRNA-1; BPAG_0000354001-mRNA-1; BPAG_0000354001.
DR   Proteomes; UP000038020; Unplaced.
DR   Proteomes; UP000278627; Unassembled WGS sequence.
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; 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:UP000278627}.
FT   DOMAIN          367..503
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   639 AA;  72493 MW;  9713DF89189DF3C4 CRC64;
     MKFEENMGKK LFFRIPYLCL AKTFEGIEAT SSRLEIVKIL ASFFMKVIER TPSELATCVY
     LCVNKLGPTY EGMELGIAEG ALMKAIAQAT GRKIDKLKED LNQKGDLGLV AQMSRSNQRI
     LFTPAPLTVT AVFHKLQDMA KTSGHMAMNK KVDMIKSLLV SCRDCEARYL IRCLSGKLRI
     GLAEQSILAA LANAFTDFEI KKTGEKLSCE KMKERQAEDI LLLRSTYSEC PDYEKVVAAV
     LNGGLSKLPE KCKITPGIPV KPMLAHPTKG IAEVLKRFGG SVFACEFKYD GERAQIHYDS
     SGIKIFSRNQ ENNTDKYPDL KELLKQIMDE ETTSFIIDSE IVAFDPIHET ILPFQILSTR
     KRKNVGDSEI KVKVHVFMFD LLFWNDQSLT KSPYRKRREM LQRHFKEVGG VCGFVASKDT
     EDTEQISEFL DDAIKGNCEG LMIKTLDVDA TYEIAKRSHS WLKLKKDYLD TIGDTVDLTV
     IGAFFGTGKR TGVYGGYLLA CYNPINEEYE SICKIGTGLT DDDLRQQHQY FEELRIEKAR
     PYYSYDSSLK PDVWFDPKIV WEVKAADLSI SPKHFAARGI VDLEKGISLR FPRYIRRRTD
     KTPEEATTSQ QIADMYNNQE QIKNKVASSA NDDNIDDYY
//
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