ID G8BS16_TETPH Unreviewed; 736 AA.
AC G8BS16;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN Name=TPHA0D04570 {ECO:0000313|EMBL:CCE63091.1};
GN OrderedLocusNames=TPHA_0D04570 {ECO:0000313|EMBL:CCE63091.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE63091.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE63091.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
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DR EMBL; HE612859; CCE63091.1; -; Genomic_DNA.
DR RefSeq; XP_003685525.1; XM_003685477.1.
DR AlphaFoldDB; G8BS16; -.
DR STRING; 1071381.G8BS16; -.
DR GeneID; 11534581; -.
DR KEGG; tpf:TPHA_0D04570; -.
DR eggNOG; KOG0967; Eukaryota.
DR HOGENOM; CLU_005138_4_1_1; -.
DR OMA; WIKYKRD; -.
DR OrthoDB; 961at2759; -.
DR Proteomes; UP000005666; Chromosome 4.
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; 3.30.1490.70; -; 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; 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; 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 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:UP000005666}.
FT DOMAIN 480..617
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 62..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 736 AA; 83284 MW; FE72B5B1CDFCABAC CRC64;
MAIGRLQTTI FRQLSYCRPF VSSLRFGTAS LLYTRTMSNS LEPSKKQATL ARFFTSMGKK
TPPAVEVATK QESPENHVDK KRKVEVHPSQ SVGASEKAES PPDQTKSTVL YSEVCNLFQQ
IEETSSRLAI IKLCSEFFIR VIKNNPSDII IVAYLFINRL GPDYEPGLEL GLGENLLIKT
ISEAYGKSIK QIKLELKETG DLGTIARDAR NIQPTMFKPK PLTISDVFNN LKKIASATGK
DSQLRKIKLI KQMLSASKGL EAKFLIRSLE SKLRIGLAEK TVLISLSKAL LLHEHWKEKG
ESKFDEEDVE SMDLIEQAEA KLREAHCQVP NYEIVINLCL QDGILNIDKT CTLRPGIPLK
PMLAKPTKAI TEVLNAFQGK EFISEYKYDG ERAQVHLLEG GEMRIYSRNG ENMTERYPEL
DVKDFLCVVK AITNDQEGEN AIQPVKDIIL DCEVVAWDVE QKKILPFQVL TTRKRKNVDL
KDVKVRVCLF AFDLLYLNNE GMINKSLRER QEILRKVTVL VPGEFQYATS LITSDMDELQ
TFLDQAVKNS CEGLMVKMLD GEESHYEPSK RSRNWLKLKK DYLDGVGDSL DLVVMGAYFG
KGKRTGSYGG FLLGCYNEDT QEFETCCKIG TGFSDEMLGN LHTLLQPTEI DNPPMTYIYD
SSAEPDVWFQ AKVLFEVLTA DLSLSPVYKA GNSRYDKGIS LRFPRFLRIR EDKDVTDGTT
SEDIIEFYES QSHIQN
//