UniProt: F8MM01

Database: UniProt
Entry: F8MM01_NEUT8

LinkDB:  F8MM01_NEUT8 
Original site:  F8MM01_NEUT8

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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 (19)   
   InterPro (11)   
   Pfam (4)   
   PROSITE (3)   
   SMART (1)   
All databases (32)   

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ID   F8MM01_NEUT8            Unreviewed;      1046 AA.
AC   F8MM01;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=NEUTE1DRAFT_81451 {ECO:0000313|EMBL:EGO57675.1};
OS   Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO57675.1};
RN   [1] {ECO:0000313|EMBL:EGO57675.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO57675.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Submitted (APR-2011) 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; GL891304; EGO57675.1; -; Genomic_DNA.
DR   RefSeq; XP_009850774.1; XM_009852472.1.
DR   AlphaFoldDB; F8MM01; -.
DR   GeneID; 20830407; -.
DR   KEGG; nte:NEUTE1DRAFT81451; -.
DR   VEuPathDB; FungiDB:NEUTE1DRAFT_81451; -.
DR   HOGENOM; CLU_004844_1_1_1; -.
DR   OrthoDB; 8251at2759; -.
DR   Proteomes; UP000008065; 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; cd00027; BRCT; 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; 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   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          433..556
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          738..823
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          932..1045
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          61..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1046 AA;  119093 MW;  8996BBEA8AD66A45 CRC64;
     MNTNRRSRSP DEEALEEDQH QYGAGTLSLE ELDEQPRNHS KTFPFSDLFR TLFNPLIDCK
     PSTSGGTVRG PKPGRGGHFS KVSYHEQRRH IIERFMSRWR SEVGNDFYPA MRLILSDKDR
     DRGVYGLKEN TIGKLLVKVM KIDRNSEDGY NLMHWKLPGS QSGVSRSVGD FAGRCFEVVS
     KRAMRAQPGE LTIADVNVLL DRLAAASGEA EQLPIFEEFY RQMNAEEMMW LVRIILKDMR
     VGATERTFLN LWHPDAEALF SVSSSLRRVC WELFDPEFRL EQQETGIKLM QCFQPQLAQF
     QMTTTWEKLV KNLGVTEENP EFWIEEKLDG ERMQMHMIED DTVPGGFRFA FWSRKAKDYT
     YLYGESLEDE QSALTRHLHK AFDDGVRNLI LDGEMITWDI DIDKMVPFGT LKTAALEQQK
     NPSKAGPRPL YRVFDILLLN DKPLTEYTLN DRRRALERAV VGVHRRLEIL PFERATSPDA
     IEPLLRRVVA EASEGLVLKN PRSRYSLNSR NNDWIKVKPE YMSDFGESLD CVVVGGYFGS
     GRRGGTLSSF LCGVRVSQNF IKSGNASAEK CLSFVKVGGG FKAEDYAEIR HHTEGKWQDW
     DPSSPPTEYI ELGGGEKLQY EKPDVWIRPS DSVVISVKAA SITQSDQFAM GWTLRFPRFR
     KLRLDRAWDS ALDMDEFEVL RSKIKDQEQE RKKMEMENRK RKPATKRARK DLVIAGMSDP
     SSSSAATPVI APRETREASE RLFEGLDFCV LSDSLKPNKM AKPALEKLIK DHGGRIHQQV
     VDHSGQGKII IPIADKNVIK VASLRKANPE MDIVRPKWIF DCLVQPILFT KQKENKKGYL
     LLFEPTHLFH SGSEETSEEA EQAVDRYGDS YAGDLADINE LKAIMEGMES DDYVSDSDWD
     SDPGRGRGRG DGFDMDHFLD HLEEQGTSLD ELRSFMFRRC RVFFALPSAG NGDGAAESKA
     SRLKNYIRFG NGKVVDELET ATHVVVVTAP SGESSKKEGR EMAAEIRYKI SLREMGSPMP
     RIVKGEWVED SWKEATVVDE EEYVAG
//

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