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Protein

Replication factor C subunit 2

Gene

RfC4

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1. Subunit 2 binds ATP.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi56 – 63ATPSequence analysis8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: UniProtKB

GO - Biological processi

  • DNA damage checkpoint Source: FlyBase
  • DNA repair Source: FlyBase
  • DNA replication Source: UniProtKB
  • DNA replication checkpoint Source: FlyBase
  • DNA strand elongation involved in DNA replication Source: FlyBase
  • female meiosis chromosome segregation Source: FlyBase
  • leading strand elongation Source: FlyBase
  • mitotic cell cycle Source: FlyBase
  • mitotic chromosome condensation Source: FlyBase
  • sister chromatid cohesion Source: FlyBase

Keywordsi

Molecular functionDNA-binding
Biological processCell cycle, DNA replication
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-110312 Translesion synthesis by REV1
R-DME-110314 Recognition of DNA damage by PCNA-containing replication complex
R-DME-110320 Translesion Synthesis by POLH
R-DME-174411 Polymerase switching on the C-strand of the telomere
R-DME-176187 Activation of ATR in response to replication stress
R-DME-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-DME-5655862 Translesion synthesis by POLK
R-DME-5656121 Translesion synthesis by POLI
R-DME-5656169 Termination of translesion DNA synthesis
R-DME-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER
R-DME-5696400 Dual Incision in GG-NER
R-DME-6782135 Dual incision in TC-NER
R-DME-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-DME-69091 Polymerase switching

Names & Taxonomyi

Protein namesi
Recommended name:
Replication factor C subunit 2
Alternative name(s):
Activator 1 40 kDa subunit
Short name:
A1 40 kDa subunit
Activator 1 subunit 2
Replication factor C 40 kDa subunit
Short name:
RF-C 40 kDa subunit
Short name:
RFC40
Replication factor C subunit 4
Short name:
DmRfc4
Gene namesi
Name:RfC4
Synonyms:RfC40
ORF Names:CG14999
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0260985 RfC4

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Defects in mitotic chromosome cohesion and condensation due to aberrant checkpoint control in response to DNA replication inhibition or damage to chromosomes; premature chromosome condensation and precocious sister chromatid separation figures.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001217691 – 331Replication factor C subunit 2Add BLAST331

Proteomic databases

PaxDbiP53034
PRIDEiP53034

Expressioni

Developmental stagei

Expressed in early embryos.1 Publication

Gene expression databases

BgeeiFBgn0260985
GenevisibleiP53034 DM

Interactioni

Subunit structurei

Heteropentamer of subunits of 140/145, 40, 38, 37, and 36.5 kDa that forms a complex with PCNA in the presence of ATP.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
RfC3Q9VKW33EBI-184606,EBI-118156

Protein-protein interaction databases

BioGridi63972, 21 interactors
DIPiDIP-22077N
IntActiP53034, 5 interactors
STRINGi7227.FBpp0073120

Structurei

3D structure databases

ProteinModelPortaliP53034
SMRiP53034
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the activator 1 small subunits family.Curated

Phylogenomic databases

eggNOGiKOG0991 Eukaryota
COG0470 LUCA
GeneTreeiENSGT00550000075050
InParanoidiP53034
KOiK10755
OMAiQSTWSGF
OrthoDBiEOG091G0CKT
PhylomeDBiP53034

Family and domain databases

InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR003959 ATPase_AAA_core
IPR008921 DNA_pol3_clamp-load_cplx_C
IPR027417 P-loop_NTPase
IPR013748 Rep_factorC_C
PfamiView protein in Pfam
PF00004 AAA, 1 hit
PF08542 Rep_fac_C, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF48019 SSF48019, 1 hit
SSF52540 SSF52540, 1 hit

Sequencei

Sequence statusi: Complete.

P53034-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEEPEKTAD DKRSHLPWIE KYRPVKFKEI VGNEDTVARL SVFATQGNAP
60 70 80 90 100
NIIIAGPPGV GKTTTIQCLA RILLGDSYKE AVLELNASNE RGIDVVRNKI
110 120 130 140 150
KMFAQQKVTL PRGRHKIVIL DEADSMTEGA QQALRRTMEI YSSTTRFALA
160 170 180 190 200
CNTSEKIIEP IQSRCAMLRF TKLSDAQVLA KLIEVAKWEK LNYTEDGLEA
210 220 230 240 250
IVFTAQGDMR QGLNNLQSTA QGFGDITAEN VFKVCDEPHP KLLEEMIHHC
260 270 280 290 300
AANDIHKAYK ILAKLWKLGY SPEDIIANIF RVCKRINIDE HLKLDFIREI
310 320 330
GITHMKIIDG INSLLQLTAL LAKLCIAAEK H
Length:331
Mass (Da):37,173
Last modified:October 1, 1996 - v1
Checksum:i0ACE1C6DCBA8AF8F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15967 Genomic DNA Translation: AAB60241.1
AE014296 Genomic DNA Translation: AAF47843.1
AY094829 mRNA Translation: AAM11182.1
PIRiS55020
RefSeqiNP_523915.1, NM_079191.3
UniGeneiDm.839

Genome annotation databases

EnsemblMetazoaiFBtr0073264; FBpp0073120; FBgn0260985
GeneIDi38492
KEGGidme:Dmel_CG14999

Similar proteinsi

Entry informationi

Entry nameiRFC2_DROME
AccessioniPrimary (citable) accession number: P53034
Secondary accession number(s): Q9VZH9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 23, 2018
This is version 144 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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