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Reviewed, UniProtKB/Swiss-Prot Q1SGF1 (PARP3_MEDTR)

Last modified June 16, 2009. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative poly [ADP-ribose] polymerase 3
      Short name=PARP-3
    EC=2.4.2.30
Alternative name(s):
    ADPRT 3
    NAD(+) ADP-ribosyltransferase 3
    Poly[ADP-ribose] synthetase 3
Gene names
Name: PARP3
OrganismMedicago truncatula (Barrel medic)
Taxonomic identifier3880 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IFabalesFabaceaePapilionoideaeTrifolieaeMedicago

Protein attributes

Sequence length799 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks By similarity.

Catalytic activity

NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.

Subcellular location

Nucleus Potential.

Sequence similarities

Contains 1 BRCT domain.

Contains 1 PARP alpha-helical domain.

Contains 1 PARP catalytic domain.

Contains 1 SAP domain.

Ontologies

Keywords
   Cellular componentNucleus
   LigandDNA-binding
NAD
   Molecular functionGlycosyltransferase
Transferase
   PTMADP-ribosylation
Gene Ontology (GO)
   Biological processprotein amino acid ADP-ribosylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

NAD+ ADP-ribosyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 799799Putative poly [ADP-ribose] polymerase 3
PRO_0000260501

Regions

Domain71 – 10535SAP
Domain165 – 26197BRCT
Domain436 – 555120PARP alpha-helical
Domain564 – 795232PARP catalytic

Sequences

Sequence LengthMass (Da)Tools
Q1SGF1-1 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 0B108316557FDE8A

FASTA79989,991
        10         20         30         40         50         60 
MKVESRSHNV HHAHGEEEKV MTRKQKAESK AHEVEHSPKK AKVEDEKNGH TNGKSASDVV 

        70         80         90        100        110        120 
QEYDEFCKAT NEQLSLEQMK EILEANDLDS SGSDLEITRR CQDLLFFGAL EKCMVCNGNM 

       130        140        150        160        170        180 
EFDGRRYGCR GFYSEWSSCT FSTREPPRKD EPIKLPDSVQ NSPVSDLLKK YQDPSKRPQR 

       190        200        210        220        230        240 
DLGLAIKPFT GMMISLMGRL NRTHLNFSGA SCLVASPAER DRGGTSKLAD AMERGIPVVR 

       250        260        270        280        290        300 
EAWLTDSIEK QEPQPLESYD LVSDLSVDGK GIPWDKQDPG EEAIESLSAE LKLYGKRGVY 

       310        320        330        340        350        360 
KDTKLHEQDG KIFEKDGILY NCAFSLCDQG RKLNDYCVMQ LIVVPENSLH LYFKKGRVGD 

       370        380        390        400        410        420 
DPSAEERLEE CENVDNAIKE FVRLFEEITG NEFESWEREK KFQKKPLKFY PIDMDDGVEV 

       430        440        450        460        470        480 
RHGALGLRQL GIAATHCKLE PMVANFMKVL CSQEIYKYAL MEMGYDSPDL PIGMVTNLHL 

       490        500        510        520        530        540 
KRCEEILLEF IEKVKTLKET GPKADAIWSD FSQKWFTLMH STRPFIFRDY QEIADHAAAA 

       550        560        570        580        590        600 
LEGVRDITLA SHLIGDMSGS TIDDPLSDTY KKLGCSITPL EKNSNDYEMI VKYLEKTYEP 

       610        620        630        640        650        660 
VKVGDIEYGV SVENIFTVES SACPSYADIV KMPNKVLLWC GSRSSNLLRH LHKGFLPAIC 

       670        680        690        700        710        720 
SLPVPGYMFG KAIVCSDAAA EAARYGFTAV DRPEGFLVLA IASLGNEITE LKSPPEDTTS 

       730        740        750        760        770        780 
LEEKKVGVKG LGKKKTDESE HFVWKDDIKV PCGSIIASEH EDSPLEYNEY AVYDPKQVRI 

       790 
SYLVGVKYEE KDAVIDTAE 

« Hide

References

[1]The International Medicago Genome Annotation Group
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AC144515 Genomic DNA. No translation available.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA2.4.2.30. 266820.

Family and domain databases

InterProIPR001357. BRCT.
IPR012982. PADR1.
IPR012317. PARP_catalytic.
IPR004102. PARP_reg.
IPR008893. WGR.
[Graphical view]
Gene3DG3DSA:1.20.142.10. PARP_reg. 1 hit.
PfamPF00533. BRCT. 1 hit.
PF08063. PADR1. 1 hit.
PF00644. PARP. 1 hit.
PF05406. WGR. 1 hit.
[Graphical view]
SMARTSM00773. WGR. 1 hit.
[Graphical view]
PROSITEPS50172. BRCT. 1 hit.
PS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
PS50800. SAP. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePARP3_MEDTR
AccessionPrimary (citable) accession number: Q1SGF1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: May 16, 2006
Last modified: June 16, 2009
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents