ID A0A1I7VUJ2_LOALO Unreviewed; 885 AA.
AC A0A1I7VUJ2; A0A1S0TZB4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DNA ligase IV {ECO:0000256|ARBA:ARBA00031942};
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4 {ECO:0000256|ARBA:ARBA00030676};
GN ORFNames=LOAG_05773 {ECO:0000313|EMBL:EFO22713.2,
GN ECO:0000313|WBParaSite:EN70_6369};
OS Loa loa (Eye worm) (Filaria loa).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Loa.
OX NCBI_TaxID=7209 {ECO:0000313|Proteomes:UP000095285, ECO:0000313|WBParaSite:EN70_6369};
RN [1] {ECO:0000313|EMBL:EFO22713.2, ECO:0000313|Proteomes:UP000095285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Henn M.R.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Loa loa.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:EN70_6369}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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; JH712454; EFO22713.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7VUJ2; -.
DR STRING; 7209.A0A1I7VUJ2; -.
DR EnsemblMetazoa; EFO22713.2; EFO22713.2; LOAG_05773.
DR WBParaSite; EN70_6369; EN70_6369; EN70_6369.
DR eggNOG; KOG0966; Eukaryota.
DR InParanoid; A0A1I7VUJ2; -.
DR OMA; MAQPSND; -.
DR OrthoDB; 8251at2759; -.
DR Proteomes; UP000095285; 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; 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; 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 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 PROSITE; PS50172; BRCT; 2.
DR PROSITE; PS50160; DNA_LIGASE_A3; 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:UP000095285};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 377..501
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 653..743
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 808..885
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 885 AA; 100560 MW; B0D8860272F41142 CRC64;
MSGSDETGEE AVENSDVSSG KEDEQEVETA AASSLEEEIS RNFKYSTLCK YLDRIQQIHF
KNKFGKERVL KALVTKWTAD ASKFTNGAVS FYPVLRIMAN SLDRRKFRMR SKRIISKVCQ
VLCLPPKTKK ELLQIDSKSA DQSILKLAEE ISMRNPAVTK RELSLFDVND SLCKITEQEI
SSAELEKLLK ACATIREVYW LLQVLVRKIE RSLKVTSANL VSWIHPNGAA LYQSGVSLRK
ICDLIVEGKM TDNSSMLFRR FEPMLLSRIR HGSGDVYDKL VRFCGQEFYV ELKYDGEHFL
LHRGPSCEMR YYSRVQNDFT NSIAPVLDHR INPYFAPSLE SCILDTELLL WDTIDEVFVG
HNAQASDGRI YDVKALRTDG AVEPSVAVFD ILFLNGKSLM DIPLSERIAL LQSGNVLEKQ
DKTKIFVSNF TIVKTREEFA SLYQEAVISG QEGVVAKKMD SVYKTGMRQM ANGWFKIKPF
HLGNETLDLA IVGVDLGRND KISNYCLATL RDNKFFIVGK VGTGLDDTTR TFLKNRLTRD
HGFFKSDRIP SWIHQDYISS DLPSHFVNQN NMQVVEIRAK GLRNDRLYAP TLKTYRDDKY
VKDIDQYQAF LDFDKNLRLD SIKNAQSVTN LKKRTTVVHV LEEYQTKKAR IEEINQDLKG
KQICILRGTS DVNTQELQEI VISFGGIHVA NPGPKTLFVV TGEPKHVKSK SIIKSNKYNV
VSADWLIACK NVSKILPVTR KEAIHVVDDS LYTLFGNDGT LENSTVPTSS TAYTIASVSV
LLDSIKVPKR KKPLAAEETL RKQLFMDEKF NRFCGQTFYL HDDLTKIQKM YAQILLQMHG
ADLSTKQSSA VTHIVVPDRK IAYDNLLKKT TVVDICWLEN TLDML
//
