CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006959
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Replication factor C subunit 1 
Protein Synonyms/Alias
 Replication factor C1; Activator 1 95 kDa subunit; Cell division control protein 44 
Gene Name
 RFC1 
Gene Synonyms/Alias
 CDC44; YOR217W; YOR50-7 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
68SETPEGEKKLPLPAKacetylation[1]
128VHVKENAKFDFKSANacetylation[1]
655SSVYPASKVAGHMAGubiquitination[2]
698RLGTSTDKIGLRLDYubiquitination[2]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
 Component of the ATP-dependent clamp loader RFC complex for the POL30/PCNA homotrimer DNA clamp. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA. Replication factor C (RFC or activator 1) complex acts during elongation of primed DNA templates by DNA polymerase delta and epsilon. RFC has an essential but redundant activity in sister chromatid cohesion establishment. 
Sequence Annotation
 DOMAIN 153 243 BRCT.
 NP_BIND 353 361 ATP.
 MOTIF 830 834 Nuclear localization signal (Potential).
 MOTIF 855 860 Nuclear localization signal (Potential).
 BINDING 299 299 ATP; via carbonyl oxygen.
 BINDING 311 311 ATP; via amide nitrogen and carbonyl
 BINDING 456 456 ATP.
 MOD_RES 38 38 Phosphothreonine.
 MOD_RES 40 40 Phosphoserine.
 MOD_RES 63 63 Phosphothreonine.  
Keyword
 3D-structure; ATP-binding; Cell cycle; Cell division; Complete proteome; DNA replication; DNA-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 861 AA 
Protein Sequence
MVNISDFFGK NKKSVRSSTS RPTRQVGSSK PEVIDLDTES DQESTNKTPK KMPVSNVIDV 60
SETPEGEKKL PLPAKRKASS PTVKPASSKK TKPSSKSSDS ASNITAQDVL DKIPSLDLSN 120
VHVKENAKFD FKSANSNADP DEIVSEIGSF PEGKPNCLLG LTIVFTGVLP TLERGASEAL 180
AKRYGARVTK SISSKTSVVV LGDEAGPKKL EKIKQLKIKA IDEEGFKQLI AGMPAEGGDG 240
EAAEKARRKL EEQHNIATKE AELLVKKEEE RSKKLAATRV SGGHLERDNV VREEDKLWTV 300
KYAPTNLQQV CGNKGSVMKL KNWLANWENS KKNSFKHAGK DGSGVFRAAM LYGPPGIGKT 360
TAAHLVAQEL GYDILEQNAS DVRSKTLLNA GVKNALDNMS VVGYFKHNEE AQNLNGKHFV 420
IIMDEVDGMS GGDRGGVGQL AQFCRKTSTP LILICNERNL PKMRPFDRVC LDIQFRRPDA 480
NSIKSRLMTI AIREKFKLDP NVIDRLIQTT RGDIRQVINL LSTISTTTKT INHENINEIS 540
KAWEKNIALK PFDIAHKMLD GQIYSDIGSR NFTLNDKIAL YFDDFDFTPL MIQENYLSTR 600
PSVLKPGQSH LEAVAEAANC ISLGDIVEKK IRSSEQLWSL LPLHAVLSSV YPASKVAGHM 660
AGRINFTAWL GQNSKSAKYY RLLQEIHYHT RLGTSTDKIG LRLDYLPTFR KRLLDPFLKQ 720
GADAISSVIE VMDDYYLTKE DWDSIMEFFV GPDVTTAIIK KIPATVKSGF TRKYNSMTHP 780
VAIYRTGSTI GGGGVGTSTS TPDFEDVVDA DDNPVPADDE ETQDSSTDLK KDKLIKQKAK 840
PTKRKTATSK PGGSKKRKTK A 861 
Gene Ontology
 GO:0005663; C:DNA replication factor C complex; IDA:SGD.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003689; F:DNA clamp loader activity; IEA:InterPro.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0006272; P:leading strand elongation; IDA:SGD.
 GO:0006298; P:mismatch repair; TAS:SGD.
 GO:0000278; P:mitotic cell cycle; IMP:SGD. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR003959; ATPase_AAA_core.
 IPR001357; BRCT_dom.
 IPR008921; DNA_pol3_clamp-load_cplx_C.
 IPR012178; DNA_replication_fac_C_lsu.
 IPR013725; DNA_replication_fac_RFC1_C.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00004; AAA
 PF00533; BRCT
 PF08519; RFC1 
SMART
 SM00382; AAA
 SM00292; BRCT 
PROSITE
 PS50172; BRCT 
PRINTS