ID E3S3V7_PYRTT Unreviewed; 909 AA. AC E3S3V7; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAR-2024, entry version 53. DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617}; DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617}; GN ORFNames=PTT_17200 {ECO:0000313|EMBL:EFQ87336.1}; OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus) OS (Drechslera teres f. teres). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes; OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; OC Pyrenophora. OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067}; RN [1] {ECO:0000313|EMBL:EFQ87336.1, ECO:0000313|Proteomes:UP000001067} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ87336.1, RC ECO:0000313|Proteomes:UP000001067}; RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109; RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S., RA Oliver R.P., Friesen T.L.; RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f. RT teres."; RL Genome Biol. 11:R109.1-R109.14(2010). 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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family. CC {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GL537060; EFQ87336.1; -; Genomic_DNA. DR RefSeq; XP_003304562.1; XM_003304514.1. DR AlphaFoldDB; E3S3V7; -. DR STRING; 861557.E3S3V7; -. DR EnsemblFungi; EFQ87336; EFQ87336; PTT_17200. DR KEGG; pte:PTT_17200; -. DR eggNOG; KOG0967; Eukaryota. DR HOGENOM; CLU_005138_0_1_1; -. DR OrthoDB; 961at2759; -. DR Proteomes; UP000001067; Unassembled WGS sequence. 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:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR CDD; cd07900; Adenylation_DNA_ligase_I_Euk; 1. DR CDD; cd07969; OBF_DNA_ligase_I; 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; 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; IPR012340; NA-bd_OB-fold. DR NCBIfam; TIGR00574; dnl1; 1. DR PANTHER; PTHR45674:SF4; DNA LIGASE 1; 1. DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1. DR Pfam; PF04679; DNA_ligase_A_C; 1. DR Pfam; PF01068; DNA_ligase_A_M; 2. DR Pfam; PF04675; DNA_ligase_A_N; 1. DR SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1. DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. 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|RuleBase:RU000617}; KW DNA repair {ECO:0000256|RuleBase:RU000617}; KW DNA replication {ECO:0000256|ARBA:ARBA00022705}; 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:UP000001067}. FT DOMAIN 636..773 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT REGION 1..248 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 867..909 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 38..71 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 83..161 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 169..206 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 867..881 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 909 AA; 100499 MW; 31D80B2A2CF41DFA CRC64; MPPKQATLGK FFGKANGDGA KQQSKLSFST KPRPVKKEVP QSSPEDVKKE HKDEVDSDAD VKAPVKEEVE ADADADAMEV DSTTSETGKK RQIKEGEEAE SEEEPPSKRQ RRKPSEEKEK PKKKTAVKPK AEKSPAKSKK ATAKSSSPEP EDEDVSAPTK VAKGKKKAAA KPKAAEVDDG EAAAPAKVAK GKKKEIEKSP APAEDEVDSN KEEEDVLSSE EEEVKVKARK QVQTTLASNT KDPYPDWKPG EPVPYAALCT TFSKIEMTTK RLEILAHCSL FLRQVLRLTP KDMLPTVMLM VNKLAADYAG IELGIGESLI MKAVSESTGR NLQQIKTDQN EIGDLGLVAA KSRSKQPTMF KPKALTVEGV RKGLMGIATV EGQGAQGRKV DGIKKLLSAA DAHNSGKAID IDKDKGGPSE AKFIVRTLEG KLRLGLAEKT VVVAVAQAMI FHEMSLEGKT PSTTDLGKAE AMLKTVYSEL PSYEVIIPAM LEHGIMNLRE NCRLQPGVPL KPMLAKPTKS ITEVLDRFEG KDFTCEYKYD GERAQIHFVA HDADMELATA APTAGRSDRG VSNIFSRNSE DLSKKYPDIL AKLPTWVKEG TKSFVLDCET VAWDMVEKKV LPFQQLMTRK RKDVKVEDVK VKVCVFAFDL LYLNGEALVT KSFRERREHL NEAFIPVEGE FALAKFGNTN ELEEIQTLLE DSVKEGCEGL MVKMLDGPES FYEPSKRSQN WLKVKKDYLA GVGDSLDLVV LGAYYGKGKR TSWYGAFLLA CYNPKTEKYE TVCNIGTGFS EVILESLHKT LSEIVIDRPK PFYTHSTGNK DQPDVWFEPR HVWEVKTADL TLSPRYKAAA DEVGGGGKGV SLRFPRFIKE RDDKKPDEAS SSRMIAEMYQ RQESVGKNKG PSVDDDFEY //