ID F0ZI28_DICPU Unreviewed; 1076 AA.
AC F0ZI28;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=DICPUDRAFT_97591 {ECO:0000313|EMBL:EGC36387.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC36387.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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; GL871028; EGC36387.1; -; Genomic_DNA.
DR RefSeq; XP_003287084.1; XM_003287036.1.
DR AlphaFoldDB; F0ZI28; -.
DR STRING; 5786.F0ZI28; -.
DR EnsemblProtists; EGC36387; EGC36387; DICPUDRAFT_97591.
DR GeneID; 10500716; -.
DR KEGG; dpp:DICPUDRAFT_97591; -.
DR eggNOG; KOG0966; Eukaryota.
DR InParanoid; F0ZI28; -.
DR OMA; EGIMIKH; -.
DR OrthoDB; 8251at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0032807; C:DNA ligase IV complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IBA:GO_Central.
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 GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
DR CDD; cd07903; Adenylation_DNA_ligase_IV; 1.
DR CDD; cd17722; BRCT_DNA_ligase_IV_rpt1; 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; 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; 2.
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; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
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:UP000001064};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 481..617
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 801..891
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 983..1076
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1076 AA; 123925 MW; 19D9BC3FC2315D4B CRC64;
MDRLSLFLSE DEEENEETKN NTQNINDNSK NNLYNAFINN NYNNNNISDQ QPIISTPQQQ
QLQQQQQQQK INSPIKNSKK DIDDNDIIKA FKDNKINVRN QNQNQINDYK YQKTVPFTTF
CNLLDKIIND TKISNKKKYL SIFFSKYKEE PNNYFQLLRL LLPHMDRDRN TYGIKEKTLA
RLYVELLNIS VESQDATRLL NWRKSTNADE IGGDFGSAIY LSLKNRCLEK GILSMGDINE
ALDRLNQVDD NKSKALILKK VLRSSTAQEQ KWFVRLILKE MKMGLNEKTA LKFFHPSAMD
HLSITSNLRL VCSNLFYMSP EEQKKLKDEQ KPVTSNATVL DIHNLKIETF NAIRPMLADR
KPIDYLFSIL DNNPYHVPSS NGLGPSTTSY IIEKKYDGER TQIHKDGNDI RFYSRNTNDT
TFIYGSLLLP IVKECVLADK CILDGELIVW DTVTQRFEDF GKLKTLALNK DGISGSGDPL
GANYGKQLCY IAFDILFVKD KSVMPLPLAQ RTMLLKRCIN VKDKQFEISE QTPVSTVQEV
LGQLDAAIMN REEGLMLKDL NSFYVPAERK EKWIKIKPEY LDGMGDDFDL VIIGGYYGSG
INRRGGTISH FMLGVAYCPD DVVDEESLQE KVVFYSFCKV GSGYTDEQLK ILQKELDPHW
SPFNTNKPPS CIQLAEPFKE KPDVWIDPRK FSKVVQIKAA QLNPTEKYKA GYTLRFPRVL
KIRDDKSWQD CSTFSDILEL YKNFQNNDFK FKTLLNNNSI KTTTQKKRKL EINGISEAGS
GPGKLKVLSI FQDTDTSNIV PIQNIFQGLE FCVIKGNQQY TKSKLEIMIV ELGGTKVQNP
SKNNTHYVIG SKEVVKIQNL ISSGFFDIVL FQWVVDCYNE QKLIPLGPKY MIFTTESTKK
KFLLESDPFG DSYFNETNFS ELKDCFNQVD KENCNHSNST NINNNKQIIK GNKNQKLLNN
EQFSIDKSII ELKYFSKNCW WTLFKPNVFY LDRYQVIGEP STLIENNNLE LSSLYIEFYG
GTVSLQLNDT VTHVVIDQSD QSRIPFINNK INSIKKLNQI EIINPNWIKN LIDNIK
//
