UniProt: A0A0D2A9X1

Database: UniProt
Entry: A0A0D2A9X1_9PEZI

LinkDB:  A0A0D2A9X1_9PEZI 
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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (20)   
   InterPro (11)   
   Pfam (4)   
   PROSITE (4)   
   SMART (1)   
All databases (32)   

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ID   A0A0D2A9X1_9PEZI        Unreviewed;      1005 AA.
AC   A0A0D2A9X1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=PV09_05274 {ECO:0000313|EMBL:KIW03508.1};
OS   Verruconis gallopava.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX   NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW03508.1, ECO:0000313|Proteomes:UP000053259};
RN   [1] {ECO:0000313|EMBL:KIW03508.1, ECO:0000313|Proteomes:UP000053259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW03508.1,
RC   ECO:0000313|Proteomes:UP000053259};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA ligase involved in DNA non-homologous end joining (NHEJ);
CC       required for double-strand break (DSB) repair.
CC       {ECO:0000256|ARBA:ARBA00043870}.
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; KN847544; KIW03508.1; -; Genomic_DNA.
DR   RefSeq; XP_016213377.1; XM_016358758.1.
DR   AlphaFoldDB; A0A0D2A9X1; -.
DR   STRING; 253628.A0A0D2A9X1; -.
DR   GeneID; 27313247; -.
DR   VEuPathDB; FungiDB:PV09_05274; -.
DR   HOGENOM; CLU_004844_1_1_1; -.
DR   InParanoid; A0A0D2A9X1; -.
DR   OrthoDB; 8251at2759; -.
DR   Proteomes; UP000053259; Unassembled WGS sequence.
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; cd17722; BRCT_DNA_ligase_IV_rpt1; 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; 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; 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; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SMART; SM00292; BRCT; 2.
DR   SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 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:UP000053259};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          430..555
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          729..813
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          895..1005
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
SQ   SEQUENCE   1005 AA;  115861 MW;  EE55AE456A102F31 CRC64;
     MAHDRVVADS DAVEEEEMMY GHGALTSAEL DEKYPHRPHN VHKTLPFHEL FTTLFNPLNE
     QRKKSNTSLV SRKKQGPQGR VLMTPHEARR NIIERFISRW RKQVGNDIYP ALRLIVPEKD
     RDRAMYGLKE KTIGKLLVKV IGIDKNSEDA YNLTNWKLPG FKAAASAGDF AARCFEVLQK
     RPMLTKPGDM TIAEVNERLD RLAASSKESE QIPIFEEFYR RMNPEELMWL VRMMLRQMKI
     GATEKTFFDI WHPDAENLFN VSSSLRRVCW ELYDPEIRLD SDQSSVTLMQ CFQPQLANFQ
     ARSFEYMVRS MRPTEDDDEF WIEEKLDGER IQLHMMEDSL VPGGKRFSFW SRKGKDYTYL
     YGNGYQDEES SLTQHLKGAF SDNVRNIILD GEMITWDMEE DAIVPFGTLK TAALSEGRNP
     YGGGGQRPMF KVFDCLYLND TPITQYTLRD RRRALESAVK SVPRRMEIHE YTVAHRAEEI
     EPLLRKVVAD SSEGLVLKNP RSSYKLSERN DDWWKVKPEY MTEFGEALDC VIIGGYWGSG
     HRGGMLSSFL CGLRVDDETV RGQNANPQKC WSFFKVGGGM TATDYKEIRE ATDGKWRRWD
     PKRPPTEYIE LGGGDRQYER PDMWIKPEDS VVVEVKAASV HNTDQFRTGF TLRFPRFTRL
     RRDKTWREAL TQTEFHTLKN EAEQRHKERE FQIDDERKRR RAAASVRKRK KPLTVHGADE
     VIDTPYAGPS TKIFEGLSFF IISESLKPVK KSKAELEQLV KAHGGNVVQS QSAAEKVICI
     ADKELVKVRS IKNEGKLNIV RPIWLFDCIE QNQADIGQER FLLPIEPVHV FHTIEADQDM
     IFQNVDEFGD SYCRDVSVED LRRILASMPL NSKIALSKDQ LLEQFMDHGV DFGETKGSMF
     RNVIAYMGSA EDAVMANSDA EQEHEDLDML FIQQKLAFGG GQWVHSLSAD GVTHVVVTKD
     LNRSKLNDLR EAVASQTTLP RIVTLEWIQE SWKEGTLLDE ERFKP
//

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