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Replication factor C subunit 2 (Activator 1 40 kDa subunit) (A1 40 kDa subunit) (Activator 1 subunit 2) (Replication factor C 40 kDa subunit) (RF-C 40 kDa subunit) (RFC40) (Replication factor C subunit 4) (DmRfc4)

 RFC2_DROME              Reviewed;         331 AA.
P53034; Q9VZH9;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 141.
RecName: Full=Replication factor C subunit 2;
AltName: Full=Activator 1 40 kDa subunit;
Short=A1 40 kDa subunit;
AltName: Full=Activator 1 subunit 2;
AltName: Full=Replication factor C 40 kDa subunit;
Short=RF-C 40 kDa subunit;
Short=RFC40;
AltName: Full=Replication factor C subunit 4;
Short=DmRfc4;
Name=RfC4; Synonyms=RfC40; ORFNames=CG14999;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND
DEVELOPMENTAL STAGE.
STRAIN=Iso-1 / Kennison;
PubMed=7789770;
Harrison S.D., Solomon N., Rubin G.M.;
"A genetic analysis of the 63E-64A genomic region of Drosophila
melanogaster: identification of mutations in a replication factor C
subunit.";
Genetics 139:1701-1709(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=11438670; DOI=10.1128/MCB.21.15.5156-5168.2001;
Krause S.A., Loupart M.-L., Vass S., Schoenfelder S., Harrison S.,
Heck M.M.S.;
"Loss of cell cycle checkpoint control in Drosophila Rfc4 mutants.";
Mol. Cell. Biol. 21:5156-5168(2001).
-!- FUNCTION: 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. {ECO:0000269|PubMed:11438670}.
-!- SUBUNIT: Heteropentamer of subunits of 140/145, 40, 38, 37, and
36.5 kDa that forms a complex with PCNA in the presence of ATP.
{ECO:0000250}.
-!- INTERACTION:
Q9VKW3:RfC3; NbExp=3; IntAct=EBI-184606, EBI-118156;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11438670,
ECO:0000269|PubMed:7789770}. Note=Localizes to all replicating
nuclei, it is dispersed from chromatin in mitosis.
-!- DEVELOPMENTAL STAGE: Expressed in early embryos.
{ECO:0000269|PubMed:7789770}.
-!- DISRUPTION PHENOTYPE: 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. {ECO:0000269|PubMed:11438670}.
-!- SIMILARITY: Belongs to the activator 1 small subunits family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U15967; AAB60241.1; -; Genomic_DNA.
EMBL; AE014296; AAF47843.1; -; Genomic_DNA.
EMBL; AY094829; AAM11182.1; -; mRNA.
PIR; S55020; S55020.
RefSeq; NP_523915.1; NM_079191.3.
UniGene; Dm.839; -.
ProteinModelPortal; P53034; -.
SMR; P53034; -.
BioGrid; 63972; 21.
DIP; DIP-22077N; -.
IntAct; P53034; 5.
MINT; MINT-925288; -.
STRING; 7227.FBpp0073120; -.
PaxDb; P53034; -.
PRIDE; P53034; -.
EnsemblMetazoa; FBtr0073264; FBpp0073120; FBgn0260985.
GeneID; 38492; -.
KEGG; dme:Dmel_CG14999; -.
CTD; 5984; -.
FlyBase; FBgn0260985; RfC4.
eggNOG; KOG0991; Eukaryota.
eggNOG; COG0470; LUCA.
GeneTree; ENSGT00550000075050; -.
InParanoid; P53034; -.
KO; K10755; -.
OMA; QSTWSGF; -.
OrthoDB; EOG091G0CKT; -.
PhylomeDB; P53034; -.
Reactome; R-DME-110312; Translesion synthesis by REV1.
Reactome; R-DME-110314; Recognition of DNA damage by PCNA-containing replication complex.
Reactome; R-DME-110320; Translesion Synthesis by POLH.
Reactome; R-DME-174411; Polymerase switching on the C-strand of the telomere.
Reactome; R-DME-176187; Activation of ATR in response to replication stress.
Reactome; R-DME-5651801; PCNA-Dependent Long Patch Base Excision Repair.
Reactome; R-DME-5655862; Translesion synthesis by POLK.
Reactome; R-DME-5656121; Translesion synthesis by POLI.
Reactome; R-DME-5656169; Termination of translesion DNA synthesis.
Reactome; R-DME-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
Reactome; R-DME-6782135; Dual incision in TC-NER.
Reactome; R-DME-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-DME-69091; Polymerase switching.
GenomeRNAi; 38492; -.
PRO; PR:P53034; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0260985; -.
Genevisible; P53034; DM.
GO; GO:0005663; C:DNA replication factor C complex; ISS:FlyBase.
GO; GO:0031391; C:Elg1 RFC-like complex; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IMP:UniProtKB.
GO; GO:0000077; P:DNA damage checkpoint; IMP:FlyBase.
GO; GO:0006281; P:DNA repair; TAS:FlyBase.
GO; GO:0006260; P:DNA replication; IMP:UniProtKB.
GO; GO:0000076; P:DNA replication checkpoint; IMP:FlyBase.
GO; GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:FlyBase.
GO; GO:0016321; P:female meiosis chromosome segregation; IMP:FlyBase.
GO; GO:0046331; P:lateral inhibition; IMP:FlyBase.
GO; GO:0006272; P:leading strand elongation; ISS:FlyBase.
GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
GO; GO:0007076; P:mitotic chromosome condensation; IMP:FlyBase.
GO; GO:0007062; P:sister chromatid cohesion; ISS:FlyBase.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR013748; Rep_factorC_C.
Pfam; PF00004; AAA; 1.
Pfam; PF08542; Rep_fac_C; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF48019; SSF48019; 1.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
ATP-binding; Cell cycle; Complete proteome; DNA replication;
DNA-binding; Nucleotide-binding; Nucleus; Reference proteome.
CHAIN 1 331 Replication factor C subunit 2.
/FTId=PRO_0000121769.
NP_BIND 56 63 ATP. {ECO:0000255}.
SEQUENCE 331 AA; 37173 MW; 0ACE1C6DCBA8AF8F CRC64;
MPEEPEKTAD DKRSHLPWIE KYRPVKFKEI VGNEDTVARL SVFATQGNAP NIIIAGPPGV
GKTTTIQCLA RILLGDSYKE AVLELNASNE RGIDVVRNKI KMFAQQKVTL PRGRHKIVIL
DEADSMTEGA QQALRRTMEI YSSTTRFALA CNTSEKIIEP IQSRCAMLRF TKLSDAQVLA
KLIEVAKWEK LNYTEDGLEA IVFTAQGDMR QGLNNLQSTA QGFGDITAEN VFKVCDEPHP
KLLEEMIHHC AANDIHKAYK ILAKLWKLGY SPEDIIANIF RVCKRINIDE HLKLDFIREI
GITHMKIIDG INSLLQLTAL LAKLCIAAEK H


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