DNA ligase 4 - Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

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P52496 (DNLI4_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 89. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
DNA ligase 4
Short name=CaLIG4
EC=6.5.1.1

Alternative name(s):
DNA ligase IV
Polydeoxyribonucleotide synthase [ATP] 4

Gene names

Name:	LIG4
Synonyms:	CDC9
ORF Names:	CaO19.13220, CaO19.5798

Organism

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]

Taxonomic identifier

237561 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida ›

Protein attributes

Sequence length	928 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Involved in ds DNA break (DSB) repair. Has a role in non-homologous integration (NHI) pathways where it is required in the final step of non-homologus end-joining (NHEJ). Not required for the repair of DSBs induced by ionizing radiation or UV light. Has a important role in morphogenesis, positively affecting the capacity to form hyphae. Ref.4 Ref.5 Ref.6
Catalytic activity	ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).
Cofactor	Magnesium By similarity.
Subcellular location	Nucleus.
Induction	Cell cycle-regulated. Expression peaks in late G1 and during the morphological transition. Ref.4
Sequence similarities	Belongs to the ATP-dependent DNA ligase family. Contains 2 BRCT domains.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair DNA replication
Cellular component	Nucleus
Domain	Repeat
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA ligation involved in DNA repair Inferred from electronic annotation. Source: InterPro DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW DNA replication Inferred from electronic annotation. Source: UniProtKB-KW filamentous growth of a population of unicellular organisms Inferred from mutant phenotype Ref.5. Source: CGD pathogenesis Inferred from mutant phenotype Ref.5 PubMed 16299301. Source: CGD
Cellular_component	nucleus Inferred from sequence or structural similarity Ref.1. Source: CGD
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 DNA ligase activity Inferred from genetic interaction Ref.4. Source: CGD metal 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 – 928

928

DNA ligase 4

PRO_0000059584

Regions

Domain

673 – 769

BRCT 1

Domain

821 – 927

107

BRCT 2

Sites

Active site

304

N6-AMP-lysine intermediate By similarity

Metal binding

362

Magnesium 1 Potential

Metal binding

469

Magnesium 2 Potential

Binding site

302

ATP By similarity

Binding site

309

ATP By similarity

Binding site

324

ATP By similarity

Binding site

474

ATP By similarity

Binding site

486

ATP By similarity

Binding site

492

ATP By similarity

Experimental info

Sequence conflict

531 – 534

VYYS → FIIV in CAA64457. Ref.1

Sequence conflict

564

A → S in CAA64457. Ref.1

Sequence conflict

698

T → R in CAA64457. Ref.1

Sequence conflict

894

E → K in CAA64457. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P52496 [UniParc].

Last modified September 2, 2008. Version 3.
Checksum: E15D5151593E462E
Show »

FASTA

928

107,997

        10         20         30         40         50         60 
MTYFLNDIRP PSPNDITPSF TLLTKELFDK LDGVRKESLG DFRTVTEKKA FIIKTFINTF 

        70         80         90        100        110        120 
RTHIGNDIYP SAKLIFPEKS GRIYFIKEVA LARLLIKMYK IPKESEDYIT LHDWNKSYQR 

       130        140        150        160        170        180 
SRRFSIDEKK IRDLPLQASR IISKRRPIVD KLEEYTVPQI NSSLDQLALE KVSQGQIDIL 

       190        200        210        220        230        240 
KPLFDNLSIP EVRWLIHILL NKSILTSMER FFFNTWHPDG YRVFSICNDL QKTLQFSTNP 

       250        260        270        280        290        300 
DLRLDPSQLA IHPCFKFKPQ LSERLTTSYK TLVKKLQRKH EMDPPYEKKF QELGLENKFY 

       310        320        330        340        350        360 
IEEKMDGDRM LLHKDGDSFK FFSRRLKDYS YLYGESFQFG ALTKFLAHAF AGNIQSVILD 

       370        380        390        400        410        420 
GEMVAYDYER NVILPFGTLK SSAIQESVRQ FTTIDQYEQQ TAYPFFLVFD ILFLNGKDLT 

       430        440        450        460        470        480 
NYPLFFRKNI LNRILRPIPN RFEVLDTRLG SSSEDIERAI REVVSSRCEG LVLKNVQSKY 

       490        500        510        520        530        540 
EIDGFRNPDW IKVKPEYLEK FGENLDLVVI GKSPAIKNSY MCGLKSVTDG VYYSFCTCAN 

       550        560        570        580        590        600 
GIEIEEFDKI ERLTHGKWIK TDVAMPPESL IKFGTKIPTF WIHPSDSLVL EIRARSIDTR 

       610        620        630        640        650        660 
AGTSYAVGST LHNNHCRKIR EDKSIDECVT LQEYTHIKAN YINDLNKAQT ALGKKREPVY 

       670        680        690        700        710        720 
SLDNESKLKK VKVESDLFSG IEFLIMSDKR EADGEVTTIE EMKAMVKQYG GKIVNSVDLA 

       730        740        750        760        770        780 
TNYQIMVITE RELPVSSQYL SKGIDLVKPI WIYECIKRGC VLQLEPYFIF ASKNWDNFNH 

       790        800        810        820        830        840 
MVDQYGDSYI IHHPLNIVVP KLSESELEDL RNGFDWGDLK PWIYLFKGLS FYVCGNNLSA 

       850        860        870        880        890        900 
RFLKERIERF SGDLSKHFIE CCYIVIPDNH SRPLMLREID KMSNQISREM VIDENGGSSR 

       910        920 
IPHFVTEAFV QASIKMNYIP DPDDYKFR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A Candida albicans gene encoding a DNA ligase." Andaluz E., Larriba G., Calderone R. Yeast 12:893-898(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 56884 / 366.
[2]	Larriba G. Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO C-TERMINUS.
[3]	"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314 / ATCC MYA-2876.
[4]	"Cell cycle regulation of a DNA ligase-encoding gene (CaLIG4) from Candida albicans." Andaluz E., Ciudad A., Rubio Coque J., Calderone R., Larriba G. Yeast 15:1199-1210(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION.
[5]	"Phenotypic analysis and virulence of Candida albicans LIG4 mutants." Andaluz E., Calderone R., Reyes G., Larriba G. Infect. Immun. 69:137-147(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"An evaluation of the role of LIG4 in genomic instability and adaptive mutagenesis in Candida albicans." Andaluz E., Ciudad T., Larriba G. FEMS Yeast Res. 2:341-348(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X95001 Genomic DNA. Translation: CAA64457.2. AACQ01000088 Genomic DNA. Translation: EAK96245.1. AACQ01000087 Genomic DNA. Translation: EAK96312.1.
RefSeq	XP_715274.1. XM_710181.1. XP_715339.1. XM_710246.1.
3D structure databases
ProteinModelPortal	P52496.
ModBase	Search...
Protein-protein interaction databases
STRING	5476.CAL0001558.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3642986. 3643043.
KEGG	cal:CaO19.13220. cal:CaO19.5798.
Organism-specific databases
CGD	CAL0001558. LIG4.
Phylogenomic databases
eggNOG	COG1793.
KO	K10777.
Family and domain databases
Gene3D	2.40.50.140. 1 hit.
InterPro	IPR001357. BRCT_dom. IPR000977. DNA_ligase_ATP-dep. IPR012310. DNA_ligase_ATP-dep_cent. IPR016059. DNA_ligase_ATP-dep_CS. IPR012308. DNA_ligase_ATP-dep_N. IPR012340. NA-bd_OB-fold. [Graphical view]
Pfam	PF00533. BRCT. 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]
SUPFAM	SSF52113. BRCT. 1 hit. SSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMs	TIGR00574. dnl1. 1 hit.
PROSITE	PS50172. BRCT. 1 hit. 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_CANAL

Accession

Primary (citable) accession number: P52496
Secondary accession number(s): Q5A0L3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	September 2, 2008
Last modified:	April 3, 2013
This is version 89 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Candida albicans

Candida albicans: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents