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Database: UniProt/SWISS-PROT
Entry: DNLI4_ASHGO
LinkDB: DNLI4_ASHGO
Original site: DNLI4_ASHGO 
ID   DNLI4_ASHGO             Reviewed;         981 AA.
AC   Q75CA4;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-OCT-2017, entry version 102.
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; OrderedLocusNames=ACR008W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS   Y-1056) (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient
RT   Saccharomyces cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016816; AAS51235.1; -; Genomic_DNA.
DR   RefSeq; NP_983411.1; NM_208764.2.
DR   ProteinModelPortal; Q75CA4; -.
DR   SMR; Q75CA4; -.
DR   STRING; 33169.AAS51235; -.
DR   EnsemblFungi; AAS51235; AAS51235; AGOS_ACR008W.
DR   GeneID; 4619536; -.
DR   KEGG; ago:AGOS_ACR008W; -.
DR   HOGENOM; HOG000093622; -.
DR   InParanoid; Q75CA4; -.
DR   KO; K10777; -.
DR   OMA; HEAMSET; -.
DR   OrthoDB; EOG092C18KW; -.
DR   Proteomes; UP000000591; Chromosome 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:0000790; C:nuclear chromatin; IEA:EnsemblFungi.
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   GO; GO:0001302; P:replicative cell aging; IEA:EnsemblFungi.
DR   CDD; cd00027; BRCT; 2.
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; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR10459:SF7; PTHR10459:SF7; 1.
DR   Pfam; PF16589; BRCT_2; 2.
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; 2.
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    981       DNA ligase 4.
FT                                /FTId=PRO_0000278374.
FT   DOMAIN      721    819       BRCT 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   DOMAIN      875    980       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       380    380       Magnesium 1. {ECO:0000255}.
FT   METAL       484    484       Magnesium 2. {ECO:0000255}.
FT   BINDING     320    320       ATP. {ECO:0000250}.
FT   BINDING     327    327       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   981 AA;  111881 MW;  9883B3EEDACA8A25 CRC64;
     MVIYPWLKNT TELTIALPKK PIIHANMDVL GSPRGGTPTG EHEINAQDGS PINFSPSPDF
     CWLCDELFIK LEEVALKKKD LGKPRKVRNL EITSNFVSLW RKTVGNDIYP ALVLSLPYND
     RRSYRVKDVT LVKALCKHMK LPRNSETERR LLHWKQNAPR GVKLSTFCVE ELQKRRREPV
     VPKRMSIDEV NGMLDKLEHE SNVGKWSYIS LAESPAFNYC LEHMSYVELR FFFDIVLKVP
     IVSGLESLLL SCWHPDAESY FKVVSDLRIV AHTLYDPNER LEKNDLSVRI GYAFAPHMAQ
     RVKIPYEKVS TKLGNDFYVE EKMDGDRIQV HYMDYGNSIA YFSRNGINYT YLYGENSSKG
     SISNHLKFVE GVKECILDGE MVSYDKEMQC ILPFGLTKSG ASHQVNFETT GHTEPTYRPL
     YAVFDLLYLN GQLLTNQDVV KRKEYLEKIL IPSKNVVHLL SGPRCSDAEA ITAALGAAVA
     HGSEGIVLKK ARSKYSVGKR DDSWIKIKPE YLENFGENMD LVVIGRDKGR KDSFICALAV
     TDDSEKNNPS SYESGSDSDS DSEPIIVQPK IEKFISFCSI ANGISNEEFK EIDRLTRGNW
     FPYDERKPPT DWVEFGTKTP REWIDPKNSV VLEVKARSID NEESKSDLYK TGSTLYNAYC
     KRIRHDKNWS TASTVAEYDT AREARSYFNV SQNAKFGKDR SSPRKRRTFH LVGDIDVTKP
     SKADFLKGYY FYVTSGYFDL QSKKNIDASE IGEAVVSCGG TYIHNLRIRA SLDKLYILGC
     KDTRELKMLI ERGYDIIHPE WLMDCVKYGT MLQIEPKYVY SASEELMKQA RNQEDKYGES
     YQLPVTEDTL KALANKQVEE GYASEMGTDA VSEYERLLIF KGWLFYILDD YAYHSSWSDI
     VKWNIESCGG EVTNDLELAT IVVAVKDCFS QLSLQAVRNN IGARITGSND VQPIPKIVTS
     EWVEACMEAQ YLVDEDEYAA I
//
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