ID E3RRT9_PYRTT Unreviewed; 873 AA. AC E3RRT9; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAR-2024, entry version 54. DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617}; DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617}; GN ORFNames=PTT_11577 {ECO:0000313|EMBL:EFQ91558.1}; 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:EFQ91558.1, ECO:0000313|Proteomes:UP000001067} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ91558.1, 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; GL534730; EFQ91558.1; -; Genomic_DNA. DR RefSeq; XP_003300344.1; XM_003300296.1. DR AlphaFoldDB; E3RRT9; -. DR STRING; 861557.E3RRT9; -. DR EnsemblFungi; EFQ91558; EFQ91558; PTT_11577. DR KEGG; pte:PTT_11577; -. DR eggNOG; KOG0967; Eukaryota. DR HOGENOM; CLU_005138_1_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; DNA LIGASE 1/3 FAMILY MEMBER; 1. DR PANTHER; PTHR45674:SF9; DNA LIGASE 3; 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 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; 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 541..728 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT REGION 1..139 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 625..675 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..16 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 33..57 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 59..74 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 75..139 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 655..672 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 873 AA; 97054 MW; B005CFD75A9D5A0C CRC64; MNSPSKRRKK NDGSGKPVRS LDYFFAKQTA KATPKDAPTN TGASAEEDTT GLTDEQLARK LQEQFDKEDQ QRGQDAEPAS SNELYTDPGK SMTDVTAKND VDNVEPSNVP LPNRTIQEAP ESAPPKQKNT LSLQSTASEE DTITANIPFD QSPLEFDPQD YIPDLQKHWV ADGGHATYAL LTRCFILVNS TTSRIKIVDT LVNLLRTIIE SDPSSLLPAV WLATNAISPP YIDLELGLGG SAISKALKKV CGLDNAGLKV LNNKYGDAGD VAFEAKKKQS FTLRKPKPLT IKSVFESLVK IANSKGHGSV ENKQRIVERL VQDARGAEES RYIVRTLVQH LRIGAVKTTM LIALSRAFML SKPLGAEFEI RDRKDMAKLK KEELTEIYSR NEEIVKACFA RRPNYNDLIP VLLEIGVCEE LLVRCGLTLH IPLRPMLGSI TRDMGEMLTK LQGRDFACEY KYDGQRAQVH CDDKGKVTIF SRHLEVMTDK YPDLVALVPK IRGEGVSSFI LEGEVVAVDR ESGDLKTFQT LANRARKDVV IGAVTIDVCL FAFDLMYLNG EELLNRPFRE RRSLLKSLFV EIPHHFTWVK SLDATSADVE AVQSFFQSAL DIKCEGIMVK MLDNNPPIPD LVPDPDQPTT PKKPKKKAAK SSKSSAVKDD SSTTTTKPSR RKPLLSTYEP DKRLDAWLKV KKDYSTTSET LDLIPIAAFH GSGRKAAWWS PILLAVRNAE TGQLDAVTKC MSGFTDAFYR ANRKKYDPDD PECTVVLGQK PSFVRYNGGA GTPAVWFEPH EVWEVAFADL TLSPTYTAAI GLVSEERGLS TRFPRFLRVR EDKGVDEATE AGELAALYRK QEAKATLTKD EGEQQDIVEE EED //