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Database: UniProt
Entry: G8BS16_TETPH
LinkDB: G8BS16_TETPH
Original site: G8BS16_TETPH 
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
//
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