ID A0A0R3W726_TAEAS Unreviewed; 1065 AA.
AC A0A0R3W726;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=TASK_LOCUS6042 {ECO:0000313|EMBL:VDK36036.1};
OS Taenia asiatica (Asian tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000604101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TASK_0000604101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK36036.1, ECO:0000313|Proteomes:UP000282613}
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 -!- 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 EMBL; UYRS01018464; VDK36036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3W726; -.
DR STRING; 60517.A0A0R3W726; -.
DR WBParaSite; TASK_0000604101-mRNA-1; TASK_0000604101-mRNA-1; TASK_0000604101.
DR Proteomes; UP000046400; Unplaced.
DR Proteomes; UP000282613; 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 Gene3D; 3.40.50.10190; BRCT domain; 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; 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; 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; PF04679; DNA_ligase_A_C; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF04675; DNA_ligase_A_N; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS00697; DNA_LIGASE_A1; 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:UP000282613};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 386..568
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 775..881
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 706..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1065 AA; 118029 MW; 5EC212DBDCF3A4E9 CRC64;
MAFSPSEEGN KIADIFPFGI LCKFLEQVSS IDGAKKKRDC ISLFIQKWAD KYRGSGGNVG
PIAGSLGSFF PVLRLLIPSA DRTRPAYGVG ESTMARMLIK AFGLAPKGSD AARMLKKSRT
LSKRAAREDL ADIVQCVLRG HCATESSYTI SVQKIHDILD ALASSPSYDQ KLEIISRFVR
NVTILELKWF VRIVSRRDLS LGVVDKAWLR CLHPAAPSIW DVTQDLCVVC QRIAYINPKL
ALPDVNSKLK SVELFTAFKP MLCSRANSVD EICMAYQQEF SGSVDAGLCL EVKYDGERVQ
LHKSDANYRF WSRAGREWSW SYGERGDSSK GSLTYRLHAN GTTFANHVID CILDGEMLAF
NRLTGRFVTK ATGYDVKRAG FDCQSDSSKD VMPCFIVFDV LYLNGQLLTE MPLSQRKRTL
LTIFPSVKST CEEISSEVET CFRSTNNHAD DDNLEDYPSQ QDQILSLFAV KKGALYLGGF
LLTQPDKTRL ARCFDTWVQH GAEGMVAKAL CTPYTPNGRT GAGWWKLKPD YVLGLCADLD
CLLVGAYADT SAATCMTMFS AFLCAVVNDG DSAKIENKRR RLQSDHPSPP SFLTFCQVSC
GLKHNQLESL NRRLAPHWRQ YDRRKINCNE TEWLRVSGER PDFWIPPRHS LVLQIHAAEM
IPSASYSAGL TLRFPRIVAI REGKTWEDVA SISEIRKLYH DTKGKMVKGK TVQSSEDEDN
KSDADSDEDK KPSSYTTPET ASTIGVSTRR VKTPSKSSTS LLTRYCHPLR DPVEIESSTF
ADVEFCLYIS SRFSGPSAGL ETKSDLENAI LKRSGKVVQN AGSDTTYIVA DRITAKISNF
IEATRKGTGR GKEGGYDIVS TGWLIQCIQA NRLLPLRKDQ VFATRPSTTL QLDGACEGTH
NDFADLDTSG PSSDHHARSI SPSRLRAGLF AQTPVRRLPT DEYIQLFKGC DFSDLALPLC
GVSIVLYGSV DTSPQLKLMI ADLRSLQAIV HGPLTDISSL LSERTGTVTH VVMMNEKVHG
FEIEPALEEI RKKLGQASLP IAVTLEWAMG CASHKTLLPV SGFHL
//