ID A0A498S072_ACAVI Unreviewed; 1244 AA.
AC A0A498S072;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=DNA ligase IV {ECO:0000256|ARBA:ARBA00031942};
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4 {ECO:0000256|ARBA:ARBA00030676};
GN ORFNames=NAV_LOCUS1415 {ECO:0000313|EMBL:VBB26585.1};
OS Acanthocheilonema viteae (Filarial nematode worm) (Dipetalonema viteae).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Acanthocheilonema.
OX NCBI_TaxID=6277 {ECO:0000313|EMBL:VBB26585.1, ECO:0000313|Proteomes:UP000276991};
RN [1] {ECO:0000313|EMBL:VBB26585.1, ECO:0000313|Proteomes:UP000276991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; UPTC01000121; VBB26585.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498S072; -.
DR STRING; 6277.A0A498S072; -.
DR Proteomes; UP000276991; 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: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; 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 Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR InterPro; IPR044125; Adenylation_DNA_ligase_IV.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
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 InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
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 SMART; SM00292; BRCT; 2.
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 SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS50172; BRCT; 2.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
DR PROSITE; PS50012; RCC1_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000276991};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 185..237
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 736..860
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 1012..1102
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 1167..1244
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
SQ SEQUENCE 1244 AA; 140711 MW; A5DA2DFEADF8FDF2 CRC64;
MKSAATTIAK MKTKKSNFVY GCGFGKTGSL FTRVLRETGQ KEFKNPRQIQ YFNSRNIRHI
AAGFGFSILA SERKLYGGGV DIFSNNLDNR NYWSEGICLN PNAKDKQFST IIDVAAGRRH
FLVASKKAVY AFGDNAHGQC GQDPENMPFV RLENKPFQKI TIPSDSEIAR VHCTLDTSFI
LLDSGEVFSF GLGTDGQLGR GKCNCDWRCL PVEGDLKGMK VKTLKGSTDT LMAVTKSGEL
FMWGQNEYEQ MYPFVKDIQR SFPCEIRLSM EKITLADSTA TSCIALSNND QVYVWGFGIL
GMGPNVTSLR RPALLESNLF SSGPNDSGKV KKVFAGNSSM FAVSRTDNLF SWGLNRFSHL
DCAMSDSDET DEEAAEDIGI NSGKEDEQEV ESAAANSLEE EISRNFKYET LCKYLDRMQQ
IHFKNKFGKE RVLKALVTKW TTDASKFTSE AVSFYPVLRI MANSLDRRKF RMKSKRIISK
ICQVLFLPPK TKKELLQIDS KSADQSIMKL AEEVSMRNPT ITKRELSLFD VNDSLCKITE
GEISNEELEK LLKTCATVRE VYWLLQVLVR KIEVTSANLV SWIHPNGTAL YQSGISLREI
CDLAAEGKIA DNSSMLFRRF EPMLLSRIRH GTGDVYDKLV HFCGQEFYVE LKYDGEHFLL
HRGPNCEIRY YSRVQNDFTN TIAPILDHRI NPYFAPCIES CILDTELLLW DTVDKRFVGH
NAQASDGRIY DVKALRTDGA VEPSVAVFDV LFLNGKPLTD VPLSERLALL QSGNVLQKQD
TTKIFVSKFT VVKTREEFAS IYQEAITNGQ EGIVAKKINS IYKMGMRQMA NGWFKVKPFH
LGSETLDLAI VGVDLGRNDK ISNYCVATLR DGKFFMVGKV GTGLDETTRT FIKNRLTRDH
GFFKSDRIPS WIHEDHTSND LPTYFVKRNN IQVVEIRAKG LRNGRLYAPT LKAYRDDKYV
KDIDQYQAFL DFDKNLRLDS IKNAQNVTDS KRRMITAHVF EQYQTKKARI NEINQDLKGK
QICVLRGTSN VTIQDLQEII VSFGGIHVAN PGPKTLFVVT GEPKHVKSKS IIKSNKYNVV
SADWLITCKN MSKVIPITKK ETVHVVDDSL YSLFGDDREL GNSIISASST AYTVAGVSAL
LDKIKVHKRK KPLAAEEALR KQLLMDEKFD RFYGQTFYLH DDLTKIQKMY TQTLLRMHGA
DLSTKQSSAV THVVVPDRKI MYDNLPKKTT VVDVCWLENT LDIQ
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