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 01-MAY-2013, entry version 47.
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; mitosporic Onygenales; 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 (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) +
CC (deoxyribonucleotide)(m) = AMP + diphosphate +
CC (deoxyribonucleotide)(n+m).
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC -!- SIMILARITY: Contains 2 BRCT domains.
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DR EMBL; GG704915; EAS28319.2; -; Genomic_DNA.
DR RefSeq; XP_001239595.1; XM_001239594.1.
DR RefSeq; XP_001239902.1; XM_001239901.1.
DR ProteinModelPortal; Q1DKE7; -.
DR GeneID; 4558489; -.
DR GeneID; 4558890; -.
DR KEGG; cim:CIMG_09216; -.
DR KEGG; cim:CIMG_09523; -.
DR KO; K10777; -.
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:EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Gene3D; 2.40.50.140; -; 1.
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; IPR012340; NA-bd_OB-fold.
DR Pfam; PF00533; BRCT; 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; SSF52113; BRCT; 2.
DR SUPFAM; SSF50249; Nucleic_acid_OB; 1.
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.
FT DOMAIN 878 983 BRCT 2.
FT ACT_SITE 312 312 N6-AMP-lysine intermediate (By
FT similarity).
FT METAL 379 379 Magnesium 1 (Potential).
FT METAL 480 480 Magnesium 2 (Potential).
FT BINDING 310 310 ATP (By similarity).
FT BINDING 317 317 ATP (By similarity).
FT BINDING 339 339 ATP (By similarity).
FT BINDING 485 485 ATP (By similarity).
FT BINDING 496 496 ATP (By similarity).
FT BINDING 502 502 ATP (By similarity).
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
//
