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Database: UniProt
Entry: Q7SB49
LinkDB: Q7SB49
Original site: Q7SB49 
ID   DNLI4_NEUCR             Reviewed;        1050 AA.
AC   Q7SB49;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 2.
DT   25-OCT-2017, entry version 112.
DE   RecName: Full=DNA ligase 4;
DE            EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE   AltName: Full=DNA ligase IV;
DE   AltName: Full=Mutagen-sensitive protein 53;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4;
GN   Name=mus-53; Synonyms=lig4; ORFNames=NCU06264;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
OS   1257 / FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=17003123; DOI=10.1073/pnas.0604477103;
RA   Ishibashi K., Suzuki K., Ando Y., Takakura C., Inoue H.;
RT   "Nonhomologous chromosomal integration of foreign DNA is completely
RT   dependent on MUS-53 (human Lig4 homolog) in Neurospora.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14871-14876(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
RA   Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA   Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA   Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA   Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA   Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA   Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA   Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
RA   Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Involved in ds DNA break repair. Has a role in non-
CC       homologous integration (NHI) pathways where it is required in the
CC       final step of non-homologus end-joining.
CC       {ECO:0000269|PubMed:17003123}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000255|PROSITE-ProRule:PRU10135}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF34364.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AB261106; BAF34364.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM002238; EAA33632.2; -; Genomic_DNA.
DR   RefSeq; XP_962868.2; XM_957775.2.
DR   SMR; Q7SB49; -.
DR   EnsemblFungi; EAA33632; EAA33632; NCU06264.
DR   GeneID; 3879007; -.
DR   KEGG; ncr:NCU06264; -.
DR   EuPathDB; FungiDB:NCU06264; -.
DR   HOGENOM; HOG000176213; -.
DR   InParanoid; Q7SB49; -.
DR   KO; K10777; -.
DR   OrthoDB; EOG092C18KW; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0032807; C:DNA ligase IV complex; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IBA:GO_Central.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
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   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; Complete proteome; DNA damage; DNA recombination;
KW   DNA repair; DNA replication; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Nucleus; Reference proteome; Repeat.
FT   CHAIN         1   1050       DNA ligase 4.
FT                                /FTId=PRO_0000278384.
FT   DOMAIN      742    840       BRCT 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   DOMAIN      936   1049       BRCT 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   ACT_SITE    331    331       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       398    398       Magnesium 1. {ECO:0000255}.
FT   METAL       498    498       Magnesium 2. {ECO:0000255}.
FT   BINDING     329    329       ATP. {ECO:0000250}.
FT   BINDING     336    336       ATP. {ECO:0000250}.
FT   BINDING     358    358       ATP. {ECO:0000250}.
FT   BINDING     503    503       ATP. {ECO:0000250}.
FT   BINDING     514    514       ATP. {ECO:0000250}.
FT   BINDING     520    520       ATP. {ECO:0000250}.
SQ   SEQUENCE   1050 AA;  119433 MW;  CDA8E04CF37AFA99 CRC64;
     MNTNRRSRSP DEEALEEDQH QYGAGTLSLE ELDEHFPNRP RNHSKTFPFS DLFRTLFNPL
     IDCKPSTSGG TVRGPKPGRG GHFSKVSYHE QRRHIIERFM SRWRSEVGND FYPAMRLILP
     DKDRDRGVYG LKENTIGKLL VKVMKIDRNS EDGYNLMHWK LPGGQSGVSR SVGDFAGRCL
     EVVSKRAMRA QPGDLTIADV NVLLDRLAAA SGEAEQLPIF EEFYRQMNAE EMMWLVRIIL
     KDMRVGATER TFLNLWHPDA EALFSVSSSL RRVCWELFDP EFRLEQQETG IKLMQCFQPQ
     LAQFQMTTTW EKLVKNLGVT EENPEFWIEE KLDGERMQMH MIEDDTVPGG FRFAFWSRKA
     KDYTYLYGES LGDEQSALTR HLHKAFDDGV RNLILDGEMI TWDIDIDKMV PFGTLKTAAL
     EQQKNPSKAG PRPLYRVFDI LLLNDKPLTE YTLNDRRRAL ERAVVGVHRR LEILPFERAT
     SPDAIEPLLR RVVAEASEGL VLKNPRSRYS LNSRNNDWIK VKPEYMSDFG ESLDCVVVGG
     YFGSGRRGGT LSSFLCGVRV SQNFIKSGNA SAEKCLSFVK VGGGFKAEDY AEIRHHTEGK
     WQDWDPSSPP TEYIELGGGE KLQYEKPDVW IRPSDSVVIS VKAASITQSD QFAMGWTLRF
     PRFRKLRLDR AWDSALDMDE FEVLRSKIKD QEQERKKMEM ENRKRKPATK RARKDLVIAG
     MSDPSSSSAA TPVIAPKETR EASKRLFEGL DFCVLSDSLK PNKMTKPALE KLIKDHGGRI
     HQQVMDHSGQ GKIIIPIADK NVIKVASLRK ANPEMDIIRP KWIFDCLVQP MPFTKQKENK
     KGYLLPFEPT HLFHSGSEET SEEAEQAVDK FGDSYAGDLA DINELKAIME GMESDDYVSD
     SDWDSDSGRG RGGGDGFDMN HFLDHLEEQG TSLDDLRSFM FRRCRVFFAL PSAGNGDGAA
     ESKALRLKNY IRFGNGKVVD ELETATHVVV VTAPLGESSK KEEREIAAEL RYKISLREMG
     SPMPRIVKGE WVEDSWKEGT VVDEEEYVAG
//
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