GenomeNet

Database: UniProt/TrEMBL
Entry: F8MM01_NEUT8
LinkDB: F8MM01_NEUT8
Original site: F8MM01_NEUT8 
ID   F8MM01_NEUT8            Unreviewed;      1046 AA.
AC   F8MM01;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   25-OCT-2017, entry version 33.
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;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   Neurospora.
OX   NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO57675.1, ECO:0000313|Proteomes:UP000008065};
RN   [1] {ECO:0000313|Proteomes:UP000008065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC 2508 / P0657 {ECO:0000313|Proteomes:UP000008065};
RX   PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V.,
RA   Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to
RT   self-fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Genetics 189:55-69(2011).
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|RuleBase:RU000617}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|RuleBase:RU004196}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; GL891304; EGO57675.1; -; Genomic_DNA.
DR   RefSeq; XP_009850774.1; XM_009852472.1.
DR   EnsemblFungi; EGO57675; EGO57675; NEUTE1DRAFT_81451.
DR   GeneID; 20830407; -.
DR   KEGG; nte:NEUTE1DRAFT81451; -.
DR   EuPathDB; FungiDB:NEUTE1DRAFT_81451; -.
DR   KO; K10777; -.
DR   OrthoDB; EOG092C18KW; -.
DR   Proteomes; UP000008065; Unassembled WGS sequence.
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; cd00027; BRCT; 2.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   Gene3D; 3.40.50.10190; -; 2.
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   PANTHER; PTHR10459:SF7; PTHR10459:SF7; 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; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 2.
DR   TIGRFAMs; TIGR00574; dnl1; 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|RuleBase:RU000617};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008065};
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|RuleBase:RU000617};
KW   Ligase {ECO:0000256|RuleBase:RU000617, ECO:0000313|EMBL:EGO57675.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617}.
FT   DOMAIN      433    556       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   DOMAIN      738    823       BRCT. {ECO:0000259|PROSITE:PS50172}.
FT   DOMAIN      932   1045       BRCT. {ECO:0000259|PROSITE:PS50172}.
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
//
DBGET integrated database retrieval system