UniProt: I2H6P9

Database: UniProt
Entry: I2H6P9_TETBL

LinkDB:  I2H6P9_TETBL 
Original site:  I2H6P9_TETBL

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (18)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (4)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (32)   

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ID   I2H6P9_TETBL            Unreviewed;       972 AA.
AC   I2H6P9;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   Name=TBLA0G01040 {ECO:0000313|EMBL:CCH62051.1};
GN   ORFNames=TBLA_0G01040 {ECO:0000313|EMBL:CCH62051.1};
OS   Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS   10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH62051.1, ECO:0000313|Proteomes:UP000002866};
RN   [1] {ECO:0000313|EMBL:CCH62051.1, ECO:0000313|Proteomes:UP000002866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC   UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
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}.
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DR   EMBL; HE806322; CCH62051.1; -; Genomic_DNA.
DR   RefSeq; XP_004181570.1; XM_004181522.1.
DR   AlphaFoldDB; I2H6P9; -.
DR   STRING; 1071380.I2H6P9; -.
DR   GeneID; 14497183; -.
DR   KEGG; tbl:TBLA_0G01040; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   HOGENOM; CLU_004844_1_1_1; -.
DR   InParanoid; I2H6P9; -.
DR   OMA; IMLQHRT; -.
DR   OrthoDB; 8251at2759; -.
DR   Proteomes; UP000002866; 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; 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; 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:UP000002866};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          391..523
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          706..805
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          870..971
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   972 AA;  111977 MW;  8E9984F9905F8756 CRC64;
     MNSSNEVIIP VSTTTKESPA TTPKNFAPSP DFKWLCDELF VKIDKIREQI KNKTANTISN
     KPISTRYFDT ITHFIKLWRT TIGDDIFPAL RLILPYRDRR VYNIKDLTLI RAICSYLKLP
     KNSVVERRLI RWKYKADRYE TLATFCIHEI SKRKNEPQVT QVERISIDKL NEILDDLVVN
     RQNWNNKKRS NLLQVETFKF CLENMTFIEL KYFFDIIVKN KILGSLENMF LKIWHPDSKE
     YLSVVSDLRT LSNKLWNPSI KINNSDLSIK VGYIFAPQLA KRLMLSYDTI SNRLNNDFFI
     EEKMDGERIQ LHYMNYGETV KFFSRHGTDY TYLYGNDKSA GTIAKFLRLH KNVKECVLDG
     EMVTFDSTSK KVLPFGLVKS SASSQLNKKD IDNDSFHPLF MVFDILYLNG SSLIDLPLFK
     RKEFLNTVLT PYKDYVEILS SIRCTDSIQI KKGLDAAISV GSEGIVLKQY ISKYIPNARH
     NNWIKVKPEY LEEFGENMDL IVIGRDSGKK DCLICGILVT EEKQELSENM KRESEIEIIS
     DSGDDDLDTK PSQGIKKVIS FCTIANGLSQ NELKEINRIT RGAWKNYNNE TPPIDVLEFG
     TKKPVEWIYP QDSVVLEIKA RSLDRTDQTQ YKYATGCTLY GGYCRQIRQD KDWTSCYTLH
     DLTYNEIKRH EKKNKNKQTL IRSYSRKKSK IISPAGMLPN GTDLRLISDL FHGLYFYIIS
     DYIPDSDAQR IDREDICSLI IKNGGRVIYN VIAKTYTISK LRILSSKSTI ECTDLVRRGY
     DVINLSWLFD CLQAGVILPL EPAHCLFVSN ELLAIATDRI DKFGDSYEAT LIDSKLLKLL
     DSNINKVNRS NSNLLLINKD EGVDSIPIFL FTNRKFFLIK EDILLGDRDT LIFQIKLYGG
     SLVTKLEDCN IIVGVCGSQL VNKKLGDLRC KLVKQYVDAN FPQPIPRAVN VSWITESIKA
     GYQLSPEDYP IL
//

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