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Q9ZSV1 (PARP1_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Poly [ADP-ribose] polymerase 1

Short name=PARP-1
EC=2.4.2.30
Alternative name(s):
NAD(+) ADP-ribosyltransferase 1
Short name=ADPRT-1
Poly[ADP-ribose] synthase 1
Gene names
Name:PARP1
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Protein attributes

Sequence length980 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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 2 PARP-type zinc fingers.

Contains 1 SAP domain.

Ontologies

Keywords
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
NAD
Zinc
   Molecular functionGlycosyltransferase
Transferase
   PTMADP-ribosylation
Gene Ontology (GO)
   Biological processprotein 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 binding

Inferred from electronic annotation. Source: InterPro

NAD+ ADP-ribosyltransferase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 980980Poly [ADP-ribose] polymerase 1
PRO_0000260500

Regions

Domain257 – 29135SAP
Domain385 – 47692BRCT
Domain629 – 748120PARP alpha-helical
Domain755 – 980226PARP catalytic
Zinc finger8 – 9184PARP-type 1
Zinc finger104 – 18481PARP-type 2

Experimental info

Sequence conflict54 – 6411Missing in CAA10889. Ref.1
Sequence conflict2921L → I in CAA10889. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9ZSV1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 9D8AED26BC37E5C1

FASTA980110,475
        10         20         30         40         50         60 
MAAPPKAWKA EYAKSGRASC KSCRSPIAKD QLRLGKMVQA SQFDGFMPMW NHARCIFSKK 

        70         80         90        100        110        120 
NQIKSVDDVE GIDALRWDDQ EKIRNYVGSA SAGTSSTAAP PEKCTIEIAP SARTSCRRCS 

       130        140        150        160        170        180 
EKITKGSVRL SAKLESEGPK GIPWYHANCF FEVSPSATVE KFSGWDTLSD EDKRTMLDLV 

       190        200        210        220        230        240 
KKDVGNNEQN KGSKRKKSEN DIDSYKSARL DESTSEGTVR NKGQLVDPRG SNTSSADIQL 

       250        260        270        280        290        300 
KLKEQSDTLW KLKDGLKTHV SAAELRDMLE ANGQDTSGPE RHLLDRCADG MLFGALGPCP 

       310        320        330        340        350        360 
VCANGMYYYN GQYQCSGNVS EWSKCTYSAT EPVRVKKKWQ IPHGTKNDYL MKWFKSQKVK 

       370        380        390        400        410        420 
KPERVLPPMS PEKSGSKATQ RTSLLSSKGL DKLRFSVVGQ SKEAANEWIE KLKLAGANFY 

       430        440        450        460        470        480 
ARVVKDIDCL IACGELDNEN AEVRKARRLK IPIVREGYIG ECVKKNKMLP FDLYKLENAL 

       490        500        510        520        530        540 
ESSKGSTVTV KVKGRSAVHE SSGLQDTAHI LEDGKSIYNA TLNMSDLALG VNSYYVLQII 

       550        560        570        580        590        600 
EQDDGSECYV FRKWGRVGSE KIGGQKLEEM SKTEAIKEFK RLFLEKTGNS WEAWECKTNF 

       610        620        630        640        650        660 
RKQPGRFYPL DVDYGVKKAP KRKDISEMKS SLAPQLLELM KMLFNVETYR AAMMEFEINM 

       670        680        690        700        710        720 
SEMPLGKLSK ENIEKGFEAL TEIQNLLKDT ADQALAVRES LIVAASNRFF TLIPSIHPHI 

       730        740        750        760        770        780 
IRDEDDLMIK AKMLEALQDI EIASKIVGFD SDSDESLDDK YMKLHCDITP LAHDSEDYKL 

       790        800        810        820        830        840 
IEQYLLNTHA PTHKDWSLEL EEVFSLDRDG ELNKYSRYKN NLHNKMLLWH GSRLTNFVGI 

       850        860        870        880        890        900 
LSQGLRIAPP EAPVTGYMFG KGLYFADLVS KSAQYCYVDR NNPVGLMLLS EVALGDMYEL 

       910        920        930        940        950        960 
KKATSMDKPP RGKHSTKGLG KTVPLESEFV KWRDDVVVPC GKPVPSSIRS SELMYNEYIV 

       970        980 
YNTSQVKMQF LLKVRFHHKR 

« Hide

References

[1]"Higher plants possess two structurally different poly(ADP-ribose) polymerases."
Babiychuk E., Cottrill P.B., Storozhenko S., Fuangthong M., Chen Y., O'Farrell M.K., Van Montagu M., Inze D., Kushnir S.
Plant J. 15:635-645(1998) [PubMed: 9778846] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Purification and cDNA cloning of maize poly(ADP)-ribose polymerase."
Mahajan P.B., Zuo Z.
Plant Physiol. 118:895-905(1998) [PubMed: 9808734] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ222589 mRNA. Translation: CAA10889.1.
AF093627 mRNA. Translation: AAC79704.1.
PIRT03657.

3D structure databases

HSSPHSSP built from PDB template 1GS0 based on UniProtKB O88554.
ProteinModelPortalQ9ZSV1.
SMRQ9ZSV1. Positions 6-91.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsGRMZM5G831712_T02; GRMZM5G831712_P02; GRMZM5G831712.

Organism-specific databases

GrameneQ9ZSV1.
MaizeGDB403204.

Phylogenomic databases

GeneTreeEPGT00070000030126.

Family and domain databases

InterProIPR001357. BRCT.
IPR008288. NAD_ADPRT.
IPR012982. PADR1.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR003034. SAP_DNA-bd.
IPR008893. WGR_domain.
IPR001510. Znf_PARP.
[Graphical view]
Gene3DG3DSA:1.20.142.10. PARP_reg. 1 hit.
G3DSA:3.30.1740.10. Znf_PARP. 2 hits.
PfamPF00533. BRCT. 1 hit.
PF08063. PADR1. 1 hit.
PF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF05406. WGR. 1 hit.
PF00645. zf-PARP. 2 hits.
[Graphical view]
PIRSFPIRSF000489. NAD_ADPRT. 1 hit.
SMARTSM00292. BRCT. 1 hit.
SM00773. WGR. 1 hit.
[Graphical view]
SUPFAMSSF52113. BRCT. 1 hit.
SSF47587. PARP_reg. 1 hit.
SSF142921. SSF142921. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
PS50064. PARP_ZN_FINGER_2. 2 hits.
PS50800. SAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePARP1_MAIZE
AccessionPrimary (citable) accession number: Q9ZSV1
Secondary accession number(s): O24570
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: May 1, 1999
Last modified: September 21, 2011
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families