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Database: UniProt/SWISS-PROT
Entry: DNLI4_ASPFU
LinkDB: DNLI4_ASPFU
Original site: DNLI4_ASPFU 
ID   DNLI4_ASPFU             Reviewed;         979 AA.
AC   Q4WVG8;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   05-JUL-2017, entry version 86.
DE   RecName: Full=DNA ligase 4;
DE            EC=6.5.1.1;
DE   AltName: Full=DNA ligase IV;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4;
GN   Name=lig4; ORFNames=AFUA_5G12050;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S.,
RA   Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W.,
RA   Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
RA   Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R.,
RA   Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
RA   Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J.,
RA   Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J.,
RA   Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
RA   Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A.,
RA   Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M.,
RA   Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I.,
RA   Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M.,
RA   Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
RA   Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
RA   White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K.,
RA   Machida M., Hall N., Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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. {ECO:0000250}.
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}.
DR   EMBL; AAHF01000003; EAL91408.1; -; Genomic_DNA.
DR   RefSeq; XP_753446.1; XM_748353.1.
DR   ProteinModelPortal; Q4WVG8; -.
DR   SMR; Q4WVG8; -.
DR   STRING; 5085.CADAFUBP00005836; -.
DR   PRIDE; Q4WVG8; -.
DR   EnsemblFungi; CADAFUAT00006159; CADAFUAP00006159; CADAFUAG00006159.
DR   GeneID; 3511447; -.
DR   KEGG; afm:AFUA_5G12050; -.
DR   EuPathDB; FungiDB:Afu5g12050; -.
DR   HOGENOM; HOG000176213; -.
DR   InParanoid; Q4WVG8; -.
DR   KO; K10777; -.
DR   OMA; HMCPSTK; -.
DR   OrthoDB; EOG092C18KW; -.
DR   Proteomes; UP000002530; Chromosome 5.
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: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; 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; 1.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   Gene3D; 3.40.50.10190; -; 2.
DR   InterPro; IPR001357; BRCT_dom.
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; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR10459:SF84; PTHR10459:SF84; 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; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 2.
DR   TIGRFAMs; TIGR00574; dnl1; 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; 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    979       DNA ligase 4.
FT                                /FTId=PRO_0000278375.
FT   DOMAIN      721    814       BRCT 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   DOMAIN      867    965       BRCT 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   ACT_SITE    322    322       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       389    389       Magnesium 1. {ECO:0000255}.
FT   METAL       490    490       Magnesium 2. {ECO:0000255}.
FT   BINDING     320    320       ATP. {ECO:0000250}.
FT   BINDING     327    327       ATP. {ECO:0000250}.
FT   BINDING     349    349       ATP. {ECO:0000250}.
FT   BINDING     495    495       ATP. {ECO:0000250}.
FT   BINDING     506    506       ATP. {ECO:0000250}.
FT   BINDING     512    512       ATP. {ECO:0000250}.
SQ   SEQUENCE   979 AA;  111878 MW;  2E5C1E83EB5F302A CRC64;
     MDSDEIMPDE EHPNVPVGDE ESDIDEKYPN RPRNHSPTLP FHELFQTLFN PLGEIKKKPA
     GAVAARRKVG PHGQSAANLN PLERRRDVIE RFISRWRKEV GDDIYPAFRL ILPDKDRDRA
     MYGIKEKAIG KMLVKIMKID KNSEDGFNLL NWKLPGQAAT SRMTGDFAGR CFDVISKRPM
     RTDVGDMLIE EVNEKLDKLS AASKEEQQLP ILAEFYRRMN PEELMWLIRI ILRQMKVGAT
     ERTFFDVWHP DAENLYSISS SLRRVCWELH DPNIRLDAED RGISLMQCFQ PQLAQFQMDS
     LDRMVARMRP TEEDPVFWIE EKLDGERMQL HMASDDSVPG GRRFRFWSRK AKEYTYLYGN
     GIYDENGSLT RYLKDAFADG VQSLILDGEM ITWDPEQDAP APFGTLKTAA LSEQRNPFST
     TGARPLLRVF DILYLNGRDL TGYTLRDRRK ALQKAVRPVH RRFEIHPYEE ATTKDQVEAA
     LRKVVAEASE GLVLKNPRSP YRLNERHDDW MKVKPEYMTE FGESLDLIVI GGYYGSGRRG
     GNLSSFLCGL RVDDGHASQG ASASKCYSFC KVGGGFNAAD YANIRHHTDG KWMEWNPKKP
     PTAYIELAGR DAQYERPDMW IKPEDSVVIC VKAASVSASD QFRLGLTLRF PRFKRLRMDK
     DWKSALSVQE FLDLKSNVEQ EHREKELNVD NSRRKRVKRT AKKPLTVAGY DMDEDVKYAG
     PSGHIFDGLN FYILTDSSAP IKKTKPELEQ LVKANGGMFF QTNNAAPHTI CVADRRTVKA
     ASLQKRGDVD IIRPSWIIDC VKQNEIDAGL PDFLLPFEPR HMFFATPGKH DEVASNVDQF
     GDSYARDTTS EELSDCPESI TKLIERLQES VNSGHEMPCG LLFKSLTILF PHRNDDVSES
     EAKTSSHPSI THVVIDPESS SKEISSLRGK WSRKPGRKVP HIVTVDWVEE SWKSRTLLDE
     ERFQPKRCIS GIAKPYWPG
//
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