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Database: UniProt/SWISS-PROT
Entry: DNLI4_EMENI
LinkDB: DNLI4_EMENI
Original site: DNLI4_EMENI 
ID   DNLI4_EMENI             Reviewed;        1009 AA.
AC   Q5BH83; C8VQN0;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   05-JUL-2017, entry version 87.
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=AN0097;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000003; EAA65275.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF90206.1; -; Genomic_DNA.
DR   RefSeq; XP_657701.1; XM_652609.1.
DR   ProteinModelPortal; Q5BH83; -.
DR   SMR; Q5BH83; -.
DR   STRING; 162425.CADANIAP00002653; -.
DR   EnsemblFungi; CADANIAT00002653; CADANIAP00002653; CADANIAG00002653.
DR   EnsemblFungi; EAA65275; EAA65275; AN0097.2.
DR   GeneID; 2875873; -.
DR   KEGG; ani:AN0097.2; -.
DR   HOGENOM; HOG000176213; -.
DR   InParanoid; Q5BH83; -.
DR   KO; K10777; -.
DR   OMA; HMCPSTK; -.
DR   OrthoDB; EOG092C18KW; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Partially assembled WGS sequence.
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; 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; 2.
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   1009       DNA ligase 4.
FT                                /FTId=PRO_0000278382.
FT   DOMAIN      715    808       BRCT 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   DOMAIN      887    995       BRCT 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   ACT_SITE    317    317       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       384    384       Magnesium 1. {ECO:0000255}.
FT   METAL       484    484       Magnesium 2. {ECO:0000255}.
FT   BINDING     315    315       ATP. {ECO:0000250}.
FT   BINDING     322    322       ATP. {ECO:0000250}.
FT   BINDING     344    344       ATP. {ECO:0000250}.
FT   BINDING     489    489       ATP. {ECO:0000250}.
FT   BINDING     500    500       ATP. {ECO:0000250}.
FT   BINDING     506    506       ATP. {ECO:0000250}.
SQ   SEQUENCE   1009 AA;  115689 MW;  60055FF8D2E80557 CRC64;
     METDQDMHDQ AMAGEETDLD EKYPNRPQNK APTLPFHDLY ETLFRPLREI KKKPVGPAGN
     RRKAGPHGLS AANLNPIERR RDIIERFISR WRKEVGDDIY PAFRLILPDK DRDRAMYGMK
     EKIIGKMLVN IMKIDKNSED GFNLLNWKLP GQSATSSMAG DFAGRCYDVV SKRPMRTEFG
     NMLIEEVNEK LDQLSSASKE EEQLPILAEF YRRMNPEELA WLIRIILRQM KLGATERTFF
     DVWHPDAENL YSISSSLRRV CWELHDPNIR LDAEDRGVSL MQCFQPQLAQ FQMQSLDRMI
     ARMRPTEDDP VFWIEEKLDG ERMQLHMVSD ASAPGGRRFR FWSRKAKDYT YLYGNGIYDE
     AGSLTRHLKD AFADGVDNLI LDGEMITWNT EQDAPEPFGT LKTAALSEQR NPFRQGIHPL
     FRVFDILYLN GRDLTRYTLR DRRNALQKVI KPVHRRFEVH SYEEATTKAE VEASLRKAVA
     EASEGLVLKN PRSPYRLNER HDDWMKVKPE YMTEFGESLD LVVIGGYYGS GHRGGKLSSF
     LCGLRVDEGQ SSQGSNPTKC YSFCKVGGGF TAADYANIRH HTDGKWVEWN PKKPPTTYIE
     LAGGDSQYER PDMWIKPEDS VVICVKAASV SVSDQFRIGL TLRFPRFKRL RMDKDWKSAL
     SVQEFLDLKS HAEQEHREKE FNVENFRKKR VKKTTKKPLA IAGYDENAEV QYAGPSGHIF
     DGLNFFILTD SNAPVKKSKA ELENLVKANG GRIFQTNDAV PDTICIADRR TVKAASLQKK
     GDIDIIRPSW ILDCIKQSEI DAGLPDLLLP LEPGHMFFMT KDKEEIVAGS LDQFNDSYAR
     DITVEELRNL LDQMAKDGKT DSFCSPEAIQ KVTEHIQEKV DSGWTMPCGW LFKGLVLCFP
     ENENDSASEG PEPKQSQRIH LAQNTAKFAG ASVTTSLKDT SITHVVVDPD FTSSELPKLR
     RTLSTRRKLP HIVKVNWIED SWKENTLLDE EQHMPVYMRR YPNIQLMKV
//
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