ID A0A067R3N3_ZOONE Unreviewed; 899 AA.
AC A0A067R3N3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA ligase 4 {ECO:0000256|ARBA:ARBA00022073};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
DE AltName: Full=DNA ligase IV {ECO:0000256|ARBA:ARBA00031942};
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4 {ECO:0000256|ARBA:ARBA00030676};
GN ORFNames=L798_08121 {ECO:0000313|EMBL:KDR17778.1};
OS Zootermopsis nevadensis (Dampwood termite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Termopsidae; Zootermopsis.
OX NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR17778.1, ECO:0000313|Proteomes:UP000027135};
RN [1] {ECO:0000313|EMBL:KDR17778.1, ECO:0000313|Proteomes:UP000027135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole organism {ECO:0000313|EMBL:KDR17778.1};
RX PubMed=24845553; DOI=10.1038/ncomms4636;
RA Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA Liebig J.;
RT "Molecular traces of alternative social organization in a termite genome.";
RL Nat. Commun. 5:3636-3636(2014).
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 -!- 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; KK852718; KDR17778.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067R3N3; -.
DR STRING; 136037.A0A067R3N3; -.
DR EnsemblMetazoa; KDR17778; KDR17778; L798_08121.
DR eggNOG; KOG0966; Eukaryota.
DR InParanoid; A0A067R3N3; -.
DR OMA; EGIMIKH; -.
DR Proteomes; UP000027135; 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; cd07968; OBF_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 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; 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; PS00333; DNA_LIGASE_A2; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KDR17778.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000027135};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 345..469
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 643..732
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 835..899
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
SQ SEQUENCE 899 AA; 102960 MW; A413617AA1276F0B CRC64;
MEYTVASKIH FKSLCRLCEI ISDCARNKKE EYLKKYINYF HEYSKNLKQE SPLLDDSFYP
FLRLLLPQLD RERGAYGIKE HNLAKVYIRV LGLPKEGHDA SKLLNFRTPK TAGSGAGDFA
EVAFWVLKSR CPEGGNLSVE QINVHLDNIA LKHAAHDPRG VDAELVAMLT SMSAAEQKWL
IRMLLKDMKL GLGQSRIFHI YHPDALELYD VSNSLLKVCQ LLRDPNIRLH EVEVSLFSPF
RPMLAERCNV QTIEESMKKS QFYYVETKYD GERFQLHMEN GVFKYFSRNG YEYTDVYVTL
LTSHVSKLLR ADTKNCILDG EMMGWNKNLK CYKYKGTNFD VKCLKEGDCI RPCLCVFDVL
LYNGQVLTNK PLSERLHYLK NLFTPSEGIF MHAERKEVTT GQEVIHELNL AIDNRLEGIV
LKDPTSIYKP NMRKGGWYKI KPEYTEGLMD HLDLIIMGGY FGEGRRKGIS HFLVGAAVPP
PIEDMEPVEF HSVARVGSGY SADELSELLQ KLSLHWQRVT PGQCPPALVW TKEKPDVWIA
PQNSYILEVK ASEIVQSSSY KVDYTLRFPR VETIRYDKKW SDCMTIIDFD SLRKEASGKL
YSRHVDASDQ LSESPKKKVR QLKKIPITLG EQFCGIDVSE VNVTSNSLEA KVFCVLTGCQ
DHTKQDIETK IIQNGGTVVQ NTGHNTFCAL AGDSTLRVRN IAKSGQCSVA RVDWLLRSIA
ANMLLPWTPA DLLYATPTVS EQLSVEFDKF GDSYTQPLTE ESLKYVLEQV EKSGCVMDLT
EEMLADLEIE LFRGPSPYGL FRLCRSYVDK YFTLNDPLSG ESKELDIVEL DFSFYGGQVF
SHIDEQTTHV IIHSQSKDRL DEIKRINRAR VCKFYIVTEQ WVQKTVEMKN RQKENDYSL
//
