UniProt: A0A1F5LWX4

Database: UniProt
Entry: A0A1F5LWX4_9EURO

LinkDB:  A0A1F5LWX4_9EURO 
Original site:  A0A1F5LWX4_9EURO

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (21)   
   InterPro (12)   
   Pfam (5)   
   PROSITE (3)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (32)   

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ID   A0A1F5LWX4_9EURO        Unreviewed;       990 AA.
AC   A0A1F5LWX4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=PENARI_c001G10400 {ECO:0000313|EMBL:OGE57642.1};
OS   Penicillium arizonense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE57642.1, ECO:0000313|Proteomes:UP000177622};
RN   [1] {ECO:0000313|EMBL:OGE57642.1, ECO:0000313|Proteomes:UP000177622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE57642.1,
RC   ECO:0000313|Proteomes:UP000177622};
RX   PubMed=27739446; DOI=10.1038/srep35112;
RA   Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA   Workman M., Frisvad J.C.;
RT   "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT   high chemical diversity in secreted metabolites.";
RL   Sci. Rep. 6:35112-35112(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGE57642.1}.
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DR   EMBL; LXJU01000001; OGE57642.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5LWX4; -.
DR   STRING; 1835702.A0A1F5LWX4; -.
DR   OrthoDB; 8251at2759; -.
DR   Proteomes; UP000177622; 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; IPR021536; DNA_ligase_IV_dom.
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   Pfam; PF11411; DNA_ligase_IV; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 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:UP000177622};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          422..547
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          716..800
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          677..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   990 AA;  113489 MW;  ABEB370FADAFDE9B CRC64;
     MDSDEIMGSG PHQPDIPEDL DEKYPNRPHN RGPTLPFHDL YINLFNPLNE VKKKPAGPAP
     VRRKLGPHGK SAAGLNPYER RRDVIERFIS RWRKDVGDDI YPAFRLILPD KDRDRPMYGI
     KEKIIGKMLV KIMKINKESE DGYNLMHWKL PGQGATARMA GDFAGRCFDV LSKRPMRTDP
     GDMTIDEVNE KLDKLSAASK EDEQLPIMKE FYMRMNPEEL LWLIRIILRQ MKVGATERTL
     FNVWHPDAES LYSISSSLRR VCWELHDPNI RLEGEERGIT VMQCFQPQLA QFQMHSFEKI
     ISRMKPTEDD NVFWIEEKLD GERMQLHMTP DDSVEGGRRF GFWSRKAKEY TYLYGNGIYD
     ENGALTRHLK DAFVDGVQSI ILDGEMITWN PEQDAIVPFG TLKTAALSEQ RNPFSNGPRP
     VFRIFDILYL NGRDLTKYTL RDRRNALQKT IRSVHRRFEI HPYQEATTTA EIETALRTVV
     AEASEGLVLK NPRSPYRLNE RHDDWMKVKP EYMTEFGESL DLVIIGGYYG SGHRGGHLSS
     FLCGLRVDET SRGSEPESMK CWSFCKVGGG FTAADYQEIR HNTDSKWKEW DIKKPPTEYI
     ELAGGDAQIE RPDMWIKPSD SVVLCVKAAS VAASPTFRMG LTLRFPRFKK LRKDKDWKSA
     LSVQGFLDLK SNAEQEHKEK EFSVDNSRKK RAKRTTKKPM AVAGYDQNVN LQDLGPSGHV
     FDGLNFFIMS ESTVPEKKTK PQLEHLVKTN GGKVFQTKAA AADMICVSER RTVKVASLQK
     SGDQNIIRPS WLLDCLKQNE KDAGLPDFLL PFEPKHMFFT MEDKEEEIAA NVDKYMDSYA
     RDINVDELKE IFNQMNKNQD QPNSPLDPTT IQRIESQIQD KVNAGYTAPR GWLFRDLTFF
     FYTRPDESNG DEQTRKHIRL RLAQNTARFA GAQSAASLKD SGITHIVIDT ESSFSVDLPS
     VRKSLAENLG KKLPHIMKKD SKFGDDKKLS
//

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