ID F0ZSY6_DICPU Unreviewed; 1144 AA.
AC F0ZSY6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=DICPUDRAFT_81260 {ECO:0000313|EMBL:EGC32964.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC32964.1, 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 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; GL871165; EGC32964.1; -; Genomic_DNA.
DR RefSeq; XP_003290530.1; XM_003290482.1.
DR AlphaFoldDB; F0ZSY6; -.
DR STRING; 5786.F0ZSY6; -.
DR EnsemblProtists; EGC32964; EGC32964; DICPUDRAFT_81260.
DR GeneID; 10507925; -.
DR KEGG; dpp:DICPUDRAFT_81260; -.
DR eggNOG; KOG4437; Eukaryota.
DR InParanoid; F0ZSY6; -.
DR OMA; DKRVFRI; -.
DR OrthoDB; 162082at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR GO; GO:0006266; P:DNA ligation; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR CDD; cd00027; BRCT; 1.
DR Gene3D; 3.30.1490.70; -; 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; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
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; IPR031916; LIG3_BRCT.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00574; dnl1; 1.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45674:SF9; DNA LIGASE 3; 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; PF16759; LIG3_BRCT; 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; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50172; BRCT; 2.
DR PROSITE; PS00697; DNA_LIGASE_A1; 1.
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, 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 DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064}.
FT DOMAIN 355..490
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 890..986
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 1045..1143
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 196..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1144 AA; 129457 MW; 9E6CFEC950E9ECED CRC64;
MSEDKSGSLY SLSKLCEKLK EESTHSGKTQ IISSFCKVFN GDLYLLAKLL LCKEDKRVFR
MRDKVMLKIC AHIWDADLDD MIADLDNGDF TETCKKFYIE YGKYPEKSTL TLKQVDDFLD
SLTLSGKFDE QVKIISSLLK KCTPQDFRLI CRIIDSDLKI NTGAKFFLDA LHPNAYDAYK
KANNLHGVIE KIQKHSFESD EESDDERSSS SSSNKKKSKK SIDSDDSDNE KSSSKKKSKS
KSKSFDVAIK LMTPIKPMLP KAVKDVDDVA KSSSCFYSEI KYDGERIQIH KDGNKFSCFS
RNLKPLMPWK VDEVKQYIPK ATKANQMILD GEVLLMDTKT GIPLPFGTLG AHKKKGFIDA
TVCVFLFDIL YLDGKSLIHL PLEERREILE KNVTVVKHRV EFSEVTIVKG IQEKYKLTNL
LNRAFKEKLE GLVIKNADSI YEPGARHWIK VKKDYIKGMA DSADLIAIGG YYGSGSFGGL
VTVFLMACYD KVSKRYKTVV KASGGLDDKT IDKLQPKIKE TMKKISKDHT KVPDWIDINK
PYTPDFIVEH PRDAMILEIE SAELTKTNYH TSGYSMRFPR IVRFREDKDY KTATNLQELM
ELGKDAKIIP TDDIEGEFDD ENLIAKRNKK KSLSITATTS TTTTTTTSSK SKDKDQQQSD
NEEEDSKTKD KLFYVGGDLT QPFSGSGDTS PNIFVLNYVD NTDKWNNKGI SGAISKRFPK
VVESFEKIKS GESKSEKVLE ENIDKEKKKI FVCNLSCIVP PKSKDESYSF SLKHFKSAIK
ESKGVIKNKN GSVHIAKPSF SKPSWSEIEE VLIDELYDSG IKVFVHSIKS PPSVSKTSTL
SSKTTTIDVS VNNNNNNNKN ENENEKTSLK RDRDQMLEHE ILKELEEKEL EAPVFGNVNV
VFDQSVLDNQ KLAKKCERLI KILGGRVSEK WCAIKGLDKT THLICDDGES DLYHHVSRLG
GAIAKTQWVE DCFNNDLLLP IDEIYCYVSK NGSSTSQNHS SKSLDTNTTK NSNAMQIDKL
GESTSTSKKE EKQCKSSPSP TKKQHLLNIF SDCSIYLHEN VNDRDTLKRY IVAFGGDVVD
QINEKTTHLI ASLPPNFSTV KPKDLFKQFL QQNKTHNKKI GNSLWLWDSI NMGEVLDIKS
YKLF
//