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Protein data for RFC2_DROME:

Description:
Activator 1 40 kDa subunit (Replication factor C 40 kDa subunit) (A140 kDa subunit) (RF-C 40 kDa subunit) (RFC40).

Molecular weight: 37173

View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):

DNA repair( GO:0006281 )


Important dates:
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
07-FEB-2006, entry version 44.

Phylogenetic order:
Eukaryota Metazoa Arthropoda Hexapoda Insecta Pterygota Neoptera Endopterygota Diptera Brachycera Muscomorpha Ephydroidea Drosophilidae Drosophila.

To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html

Links to references in other databases for protein RFC2_DROME:

DatabasePointerAdd. info#1Add. info#2
EMBLU15967AAB60241.1-
EMBLAE003480AAF47843.1-
EMBLAY094829AAM11182.1-
PIRS55020S55020.
HSSPQ9P9H21IQP
IntActP53034-.1
EnsemblCG14999Drosophila melanogaster.1
FlyBaseFBgn0015287RfC40.
BioCycDMEL-XXX-02:DMEL-XXX-02-015117-MONOMER-.1
GOGO:0005515F:protein bindingIPI.
GOGO:0006281P:DNA repairTAS.
GOGO:0006260P:DNA replicationTAS.
GOGO:0006271P:DNA strand elongationTAS.
GOGO:0016321P:female meiosis chromosome segregationIMP.
GOGO:0007067P:mitosisIMP.
GOGO:0007076P:mitotic chromosome condensationIMP.
InterProIPR003593AAA_ATPase.
InterProIPR003959AAA_ATPase_centr.
InterProIPR000862RFC.
PfamPF00004AAA1.
SMARTSM00382AAA1.

General information about the databases mentioned above

Keywords:
ATP-binding; Complete proteome; DNA replication; Nuclear protein; Nucleotide-binding.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Iso-1 / Kennison;
RX MEDLINE=95309683; PubMed=7789770;
RA Harrison S.D., Solomon N., Rubin G.M.;
RT "A genetic analysis of the 63E-64A genomic region of Drosophila
RT melanogaster: identification of mutations in a replication factor C
RT subunit.";
RL Genetics 139:1701-1709(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z.,
RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O.,
RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RX MEDLINE=22426069; PubMed=12537572;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a
RT systematic review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX MEDLINE=22426066; PubMed=12537569;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA Rubin G.M., Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).

Feature:
CHAIN 1 331 Activator 1 40 kDa subunit.
/FTId=PRO_0000121769.
NP_BIND 56 63 ATP (Potential).

Comments:
-!- 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 (By similarity).
-!- 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 (By
similarity).
-!- INTERACTION:
Q9VKW3:RfC3; NbExp=1; IntAct=EBI-184606, EBI-118156;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- DEVELOPMENTAL STAGE: Expressed in early embryos.
-!- SIMILARITY: Belongs to the activator 1 small subunits family.
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Sequence length: 331

     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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