ID G8ZY51_TORDE Unreviewed; 969 AA. AC G8ZY51; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAR-2024, entry version 58. DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617}; DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617}; GN Name=TDEL0G04510 {ECO:0000313|EMBL:CCE93818.1}; GN ORFNames=TDEL_0G04510 {ECO:0000313|EMBL:CCE93818.1}; OS Torulaspora delbrueckii (Yeast) (Candida colliculosa). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Torulaspora. OX NCBI_TaxID=4950 {ECO:0000313|EMBL:CCE93818.1, ECO:0000313|Proteomes:UP000005627}; RN [1] {ECO:0000313|EMBL:CCE93818.1, ECO:0000313|Proteomes:UP000005627} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10662 / CBS 1146 / NBRC 0425 / NCYC 2629 / NRRL Y-866 RC {ECO:0000313|Proteomes:UP000005627}; RX PubMed=22123960; DOI=10.1073/pnas.1112808108; RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P., RA Wolfe K.H.; RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching RT accidents."; RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(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}. 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; HE616748; CCE93818.1; -; Genomic_DNA. DR RefSeq; XP_003683029.1; XM_003682981.1. DR AlphaFoldDB; G8ZY51; -. DR STRING; 1076872.G8ZY51; -. DR GeneID; 11505191; -. DR KEGG; tdl:TDEL_0G04510; -. DR eggNOG; KOG0966; Eukaryota. DR HOGENOM; CLU_004844_1_1_1; -. DR InParanoid; G8ZY51; -. DR Proteomes; UP000005627; Chromosome 7. 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; 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; 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; PF16589; BRCT_2; 1. DR Pfam; PF01068; DNA_ligase_A_M; 1. DR Pfam; PF04675; DNA_ligase_A_N; 1. DR SMART; SM00292; BRCT; 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; 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 Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU000617}; Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Reference proteome {ECO:0000313|Proteomes:UP000005627}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}. FT DOMAIN 396..510 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT DOMAIN 704..803 FT /note="BRCT" FT /evidence="ECO:0000259|PROSITE:PS50172" FT DOMAIN 864..966 FT /note="BRCT" FT /evidence="ECO:0000259|PROSITE:PS50172" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..27 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 969 AA; 111242 MW; BE41935B409BD40B CRC64; MESAEILTST HEVSQELQES ESTEKAPPNF APSPDFIWLC EELFVKLEDV QRQGREHLGN KPLSVRYYEV ISHFIRLWRK TVGNNIFPAL VLSLPYRDRR IYNIKDYTLV KAICSYLALP KQSATEKRLL KWKRRATRGV RLSNFCVEEI RKRKSEPSPG RRITIDKLNE CLDHLVEERN AKGGFKGLSD SPTFNFCLQN MSFIELRFFF DIVLKNRVIG GQEHKLLNCW HPDALDYLSV VSDLETVASR LWDPEHRLRR DDLSINLGYA FVPQLAKKMT ISYEKICTKL NNDFLIEEKM DGERIQVHYM DYGAKIRFLS RRGVDYTQLY GENLQSGTVA NYLNFDSNVR DCVLDGEMIT FDTDRNVVLP FGMVKSSARQ ALSTEGICSQ GHRPMLMVLD LVYLNGVSLI KLPLYQRKEF LNRVLKPCPH AVEILPYVRC SEHTAIRKSL EKSISMGSEG IVLKSYKARY EIGARNDYWI KVKPEYLEQF GENLDLVIIG RTPGKKDSLM CGLAVYEGEE DLNEIEAKRE SAIVNLDSEG DELDDTDGKK IIKYFISFCV IANGISQQEF KEIDRKTRGA WVKSDQRLPS ADLLRFGSKI PEEWIDPKNS IMLEVKARSL DNTESSKKKF AAGCTLHGGY CRRIRDDKDW TGCYSFSELW QERLHKSSTG VGSFNKQYSK KMKSKKRKID PFSGQAAKKH DVFDSTNIFK GLQFYVLSDY IDVSRNVRIT KSEFDDLILQ NSGKLVRNLI SKHHSESQFR IISGKYTAEC RALIERGYDI LSPQWILDCI RNRMVVKLEP RHCFNVSSEL MTIVNGRVDE YGDSFVNPIT EQQLDNLIDT NMKQTEPNLM REANSELDVV PLFLFSTRAV YIPPQVFNAV DAYGLTSKFK LHGGSIASDI PSCNLIIMPN ENQRLGTQSL VEMRQSVLQA MGRNDSTPSI PYIVTPDWVE KSIEENCQVP EEDFTPVYA //