GenomeNet

Database: UniProt
Entry: Q1DKE7
LinkDB: Q1DKE7
Original site: Q1DKE7 
ID   DNLI4_COCIM             Reviewed;         985 AA.
AC   Q1DKE7; J3K2J9;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   10-MAY-2017, entry version 69.
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=CIMG_09216;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J.,
RA   Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E.,
RA   Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M.,
RA   Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N., Orbach M.J.,
RA   Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens
RT   Coccidioides and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; GG704915; EAS28012.3; -; Genomic_DNA.
DR   RefSeq; XP_001239595.1; XM_001239594.2.
DR   ProteinModelPortal; Q1DKE7; -.
DR   SMR; Q1DKE7; -.
DR   STRING; 246410.XP_001239595.1; -.
DR   EnsemblFungi; EAS28012; EAS28012; CIMG_09216.
DR   GeneID; 4558489; -.
DR   KEGG; cim:CIMG_09216; -.
DR   EuPathDB; FungiDB:CIMG_09216; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   eggNOG; COG1793; LUCA.
DR   InParanoid; Q1DKE7; -.
DR   KO; K10777; -.
DR   OrthoDB; EOG092C18KW; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
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; 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; 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    985       DNA ligase 4.
FT                                /FTId=PRO_0000278379.
FT   DOMAIN      711    804       BRCT 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   DOMAIN      878    983       BRCT 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   ACT_SITE    312    312       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       379    379       Magnesium 1. {ECO:0000255}.
FT   METAL       480    480       Magnesium 2. {ECO:0000255}.
FT   BINDING     310    310       ATP. {ECO:0000250}.
FT   BINDING     317    317       ATP. {ECO:0000250}.
FT   BINDING     339    339       ATP. {ECO:0000250}.
FT   BINDING     485    485       ATP. {ECO:0000250}.
FT   BINDING     496    496       ATP. {ECO:0000250}.
FT   BINDING     502    502       ATP. {ECO:0000250}.
SQ   SEQUENCE   985 AA;  112847 MW;  ADD8E6B21A345FEB CRC64;
     MDRLNNVGGE TERELDEKYP NRPRNKHSTL PFHDLFLTLF NPLNGNKKRP TGPAAARKKL
     GPHGGQQTLS PQELRRDIIQ RFISRWRKEV GNDIYPAFRL IIPEKDRDRA MYGLKEKTIG
     KLLVKIMKID KNSEDGFNLL NWKLPGQSMA SRMAGDFAGR CYEVISKRPI RTDVGNMTIQ
     EVNDKLDVLA ATSKEDEQIP VLEEFYRNMN PEELMWLIRI ILRQMKVGAT ERTFFEIWHP
     DAESLFSISS SLRRVCWELY DPNVRLEADE ARVTLMQCFQ PQLAQFQMHS FPKMIERMRL
     SPDDPTFWIE EKLDGERIQL HMMSDDSIPG GKRFGFWSRK AKDYTYLYGN GFYDENGALT
     RHLKDAFADG VDNIILDGEM ITWDPEQDAP LPFGTLKTAA LSEQRNPFSA TGQRPLFRIF
     DILYLNDKAL TRYTLRDRRR ALEASIKPVH RRLEVHTYEI GNSAADIEPQ LRKVVAEASE
     GLVLKNPNSP YRLNDRHDDW MKVKPEYMTE FGESLDCVVI GGYYGSGKRG GGLASFLCGL
     RVDEAQVRQG ASPMKCYSFL KVGGGFTAPD YANIRHHTDG KWKDWNPKKP PTEFIELAGG
     DAQYERPDVW IRPDESVVLC VKAASVTPSD QFRLGLTVRF PRFKRLRMDK DWKSALSIQE
     FMDLKANAER EQKEKEFKID NSRRKRAKRA VKKPLTIAGY DESKRAGFTG PSGHVFEGMN
     FFVITDSVEP EKKSKLELEQ LIKANGGKIY QTHTAAPNTL CIAERRTVKV ASVQKVAKES
     IIRPSWLFDC IKQNEVDKGL PDLLIPFEPR HMYFTVKSQE EEIARHVDEY SDSYARDITP
     NELSKLLVSM PLIPNLPPPH ISKTETQIQE RESTFQELRG WLFKNQVLHF VKRRSDSMLS
     LPLRLASNLA RFAGASVANE LEDKSITHVV IDTDSQPADV SALRSAISKR VAAGRRIPHL
     VTIAWIQDSW KAESLLDEER FAPTA
//
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