Reviewed, UniProtKB/Swiss-Prot Q5R6L3 (DNLI4_PONAB)

Names and origin

Protein names

Recommended name:
    DNA ligase 4
    EC=6.5.1.1
Alternative name(s):
    DNA ligase IV
    Polydeoxyribonucleotide synthase [ATP] 4

Gene names

Name:

DNL4

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	911 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA nonhomologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends By similarity.
Catalytic activity	ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).
Cofactor	Magnesium By similarity.
Subunit structure	Binds to XRCC4. The LIG4-XRCC4 complex has probably a 1:2 stoichiometry. The LIG4-XRCC4 heteromer associates in a DNA-dependent manner with the DNA-dependent protein kinase complex DNA-PK, formed by the Ku p70/p86 dimer (G22P1/G22P2) and PRKDC By similarity.
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the ATP-dependent DNA ligase family. Contains 2 BRCT domains.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA damage DNA recombination DNA repair DNA replication
Cellular component	Nucleus
Domain	Repeat
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: InterPro DNA ligase (ATP) activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 911	911	DNA ligase 4		PRO_0000059578
Regions
	Domain	654 – 743	90	BRCT 1
	Domain	808 – 911	104	BRCT 2
Sites
	Active site	273	1	N6-AMP-lysine intermediate By similarity
	Metal binding	331	1	Magnesium 1 Potential
	Metal binding	427	1	Magnesium 2 Potential
	Binding site	271	1	ATP By similarity
	Binding site	278	1	ATP By similarity
	Binding site	293	1	ATP By similarity
	Binding site	432	1	ATP By similarity
	Binding site	443	1	ATP By similarity
	Binding site	449	1	ATP By similarity
Amino acid modifications
	Modified residue	347	1	Phosphothreonine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5R6L3-1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: C6AD9817E9EC2B59	FASTA	911	104,053
	10 20 30 40 50 60 MAASQTSQTV ASHVPFADLC STLERIQKSK GRAEKIRHFR EFLDSWRKFH DAFHKNQKDV 70 80 90 100 110 120 TDSFYPAMRL ILPQLERERM AYGIKETMLA KLYIELLNLP RDGKDALKLL NYRTPTGTHG 130 140 150 160 170 180 DAGDFAMIAY FVLKPRCLQK GSLTIQQVND LLDSIASNNS AKRKDLIKKS LLQLITQSSA 190 200 210 220 230 240 LEQKWLIRMI IKDLKLGVSQ QTIFSVFHSD AVELHNVTTD LEKVCRQLHD PSVGLSDISI 250 260 270 280 290 300 TLFSAFKPML AAIADIEHIE KDMKHQSFYI ETKLDGERMQ MHKDGDVYKY FSRNGYNYTD 310 320 330 340 350 360 QFGASPTEGS LTPFIHNAFK TDIQICILDG EMMAYNPNTQ TFMQKGTKFD IKRMVEDSDL 370 380 390 400 410 420 QTCYCVFDVL MVNNKKLGHE TLRKRYEILS SIFTPIPGRI EIVQKTQAHT KNEVIDALNE 430 440 450 460 470 480 AIDKREEGIM IKQPLSIYKP DKRGEGWLKI KPEYVSGLMD ELDILIVGGY WGKGSRGGMM 490 500 510 520 530 540 SHFLCAVAEK PPPGEKPSVF HTLSRVGSGC TMKELYDLGL KLAKYWKPFH KKAPPSSILC 550 560 570 580 590 600 GTEKPEVYIE PCNSVIVQIK AAEIVPSDMY KTGCTLRFPR IEKIRDDKEW HECMTLDDLE 610 620 630 640 650 660 QLRGKASGKL ASKHFYVGGD DEPQEKKRKA APKMKKVIGI IEHLKAPNLT NVNKISNIFE 670 680 690 700 710 720 DVEFCVMSGT DSQPKPDLEN RIAEFGGYIV QNPGPDTYCV IAGSKNIRVK NIILSNKHDV 730 740 750 760 770 780 VKPAWLLECF KTKSFVPWQP HFMIHMCPST KEHFAREYDC YGDSYFVDTD LNQLKEVFSG 790 800 810 820 830 840 IKNSNEQTPE EMASLIADLE YRYSWDCSPL SMFRRHTVYL DLYAVINDLS TKNEGTRLAI 850 860 870 880 890 900 KALELRFHGA KVVSCLAEGV SHVIIGEDHS RIADFKAFRR TFKRKFKILK ESWITDSIDK 910 CELQEENQYL I

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR860475 mRNA. Translation: CAH92597.1.
RefSeq	NP_001126522.1.
UniGene	Pab.18738
3D structure databases
SMR	Q5R6L3. Positions 654-759.
ModBase	Search...
Genome annotation databases
GeneID	100173511.
Phylogenomic databases
HOVERGEN	Q5R6L3.
Enzyme and pathway databases
BRENDA	6.5.1.1. 269192.
Family and domain databases
InterPro	IPR001357. BRCT. IPR000977. DNA_ligase. IPR012309. DNA_ligase_A_C. IPR012310. DNA_ligase_A_M. IPR012308. DNA_ligase_A_N. IPR016059. DNA_ligase_CS. IPR012340. NA-bd_OB-fold. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
Pfam	PF00533. BRCT. 2 hits. PF04679. DNA_ligase_A_C. 1 hit. PF01068. DNA_ligase_A_M. 1 hit. PF04675. DNA_ligase_A_N. 1 hit. [Graphical view]
SMART	SM00292. BRCT. 2 hits. [Graphical view]
TIGRFAMs	TIGR00574. dnl1. 1 hit.
PROSITE	PS50172. BRCT. 2 hits. PS00697. DNA_LIGASE_A1. 1 hit. PS00333. DNA_LIGASE_A2. 1 hit. PS50160. DNA_LIGASE_A3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DNLI4_PONAB

Accession

Primary (citable) accession number: Q5R6L3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	December 21, 2004
Last modified:	June 16, 2009
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)