RFC5

Functionⁱ

Component of ATP-dependent clamp loader (RFC and RFC-like) complexes for DNA clamps, such as the POL30/PCNA homotrimer and the checkpoint clamp DDC1:MEC3:RAD17 complex. 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. Component of the replication factor C (RFC or activator 1) complex which loads POL30/PCNA and 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. Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. Component of the RFC-like RAD24-RFC complex which loads the checkpoint clamp DDC1:MEC3:RAD17 complex and is involved in DNA repair pathways. Component of the RFC-like ELG1-RFC complex which appears to have a role in DNA replication, replication fork re-start, recombination and repair.5 Publications

Miscellaneous

Present with 5040 molecules/cell in log phase SD medium.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	5	ATP; via carbonyl oxygen	1
Binding siteⁱ	17	ATP	1
Binding siteⁱ	231	ATP	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	43 – 51	ATP		9

GO - Molecular functionⁱ

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

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

DNA repair Source: GO_Central
leading strand elongation
Source: SGD
Inferred from direct assayⁱ
- 1346062
sister chromatid cohesion
Source: SGD
Inferred from mutant phenotypeⁱ
- 12665596

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding
Biological process	Cell cycle, DNA replication
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCycⁱ	YEAST:G3O-29054-MONOMER
Reactomeⁱ	R-SCE-110312 Translesion synthesis by REV1 R-SCE-110314 Recognition of DNA damage by PCNA-containing replication complex R-SCE-110320 Translesion Synthesis by POLH R-SCE-174411 Polymerase switching on the C-strand of the telomere R-SCE-5651801 PCNA-Dependent Long Patch Base Excision Repair R-SCE-5655862 Translesion synthesis by POLK R-SCE-5656121 Translesion synthesis by POLI R-SCE-5656169 Termination of translesion DNA synthesis R-SCE-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER R-SCE-5696400 Dual Incision in GG-NER R-SCE-6782135 Dual incision in TC-NER R-SCE-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER R-SCE-69091 Polymerase switching

BioCycⁱ

YEAST:G3O-29054-MONOMER

Reactomeⁱ

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

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Replication factor C subunit 5 Short name: Replication factor C5 Alternative name(s): Activator 1 40 kDa subunit
Gene namesⁱ	Name:RFC5 Ordered Locus Names:YBR087W ORF Names:YBR0810
Organismⁱ	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifierⁱ	559292 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae
Proteomesⁱ	UP000002311 Componentⁱ: Chromosome II

Organism-specific databases

EuPathDBⁱ	FungiDB:YBR087W
Saccharomyces Genome Database More...SGDⁱ	S000000291 RFC5

Keywords - Cellular componentⁱ

Nucleus

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000121765	1 – 354	Replication factor C subunit 5Add BLAST		354

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P38251
PaxDbⁱ	P38251
PRIDEⁱ	P38251

PTM databases

iPTMnetⁱ	P38251

iPTMnetⁱ

P38251

Interactionⁱ

Subunit structureⁱ

Replication factor C (RFC) is a heteropentamer of subunits RFC1, RFC2, RFC3, RFC4 and RFC5 and forms a complex with POL30/PCNA in the presence of ATP. Component of the RAD24-RFC complex which consists of RAD24, RFC2, RFC3, RFC4 and RFC5 and associates with the checkpoint clamp DDC1:MEC3:RAD17 complex. Component of the ELG1-RFC complex which consists of ELG1, RFC2, RFC3, RFC4 and RFC5. Component of the CTF18-RFC complex, which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. RFC5 interacts with ECO1.9 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
CTF18	P49956	4	EBI-15016,EBI-4560
CTF8	P38877	2	EBI-15016,EBI-5216
ELG1	Q12050	4	EBI-15016,EBI-32195
RAD24	P32641	4	EBI-15016,EBI-14675

Protein-protein interaction databases

BioGridⁱ	32793, 290 interactors
ComplexPortalⁱ	CPX-1731 CTF18-RFC complex CPX-1807 Rad17 RFC-like complex CPX-422 ELG1-RFC complex CPX-545 DNA replication factor C complex
Database of interacting proteins More...DIPⁱ	DIP-2531N
IntActⁱ	P38251, 15 interactors
Molecular INTeraction database More...MINTⁱ	P38251
STRINGⁱ	4932.YBR087W

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	5 – 8	Combined sources	4
Helixⁱ	13 – 15	Combined sources	3
Helixⁱ	20 – 27	Combined sources	8
Turnⁱ	28 – 31	Combined sources	4
Beta strandⁱ	39 – 42	Combined sources	4
Helixⁱ	49 – 54	Combined sources	6
Helixⁱ	56 – 60	Combined sources	5
Beta strandⁱ	91 – 96	Combined sources	6
Helixⁱ	106 – 116	Combined sources	11
Turnⁱ	117 – 120	Combined sources	4
Beta strandⁱ	136 – 141	Combined sources	6
Helixⁱ	148 – 160	Combined sources	13
Turnⁱ	162 – 164	Combined sources	3
Beta strandⁱ	165 – 172	Combined sources	8
Helixⁱ	179 – 182	Combined sources	4
Beta strandⁱ	185 – 189	Combined sources	5
Helixⁱ	195 – 209	Combined sources	15
Helixⁱ	217 – 226	Combined sources	10
Helixⁱ	230 – 237	Combined sources	8
Helixⁱ	239 – 242	Combined sources	4
Turnⁱ	243 – 246	Combined sources	4
Helixⁱ	258 – 272	Combined sources	15
Helixⁱ	276 – 290	Combined sources	15
Turnⁱ	291 – 293	Combined sources	3
Helixⁱ	296 – 305	Combined sources	10
Turnⁱ	306 – 309	Combined sources	4
Helixⁱ	315 – 333	Combined sources	19
Helixⁱ	338 – 353	Combined sources	16

Show more details

3D structure databases

ProteinModelPortalⁱ	P38251
SMRⁱ	P38251
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P38251

EvolutionaryTraceⁱ

P38251

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the activator 1 small subunits family.Curated

Phylogenomic databases

Ensembl GeneTree More...GeneTreeⁱ	ENSGT00550000075006
HOGENOMⁱ	HOG000224153
InParanoidⁱ	P38251
KEGG Orthology (KO) More...KOⁱ	K10756
OMAⁱ	LSHCIPP
Database of Orthologous Groups More...OrthoDBⁱ	EOG092C317A

Family and domain databases

InterProⁱ	View protein in InterPro IPR003593 AAA+_ATPase IPR008921 DNA_pol3_clamp-load_cplx_C IPR027417 P-loop_NTPase
SMARTⁱ	View protein in SMART SM00382 AAA, 1 hit
SUPFAMⁱ	SSF48019 SSF48019, 1 hit SSF52540 SSF52540, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P38251-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSLWVDKYRP KSLNALSHNE ELTNFLKSLS DQPRDLPHLL LYGPNGTGKK 
        60         70         80         90        100
TRCMALLESI FGPGVYRLKI DVRQFVTASN RKLELNVVSS PYHLEITPSD 
       110        120        130        140        150
MGNNDRIVIQ ELLKEVAQME QVDFQDSKDG LAHRYKCVII NEANSLTKDA 
       160        170        180        190        200
QAALRRTMEK YSKNIRLIMV CDSMSPIIAP IKSRCLLIRC PAPSDSEIST 
       210        220        230        240        250
ILSDVVTNER IQLETKDILK RIAQASNGNL RVSLLMLESM ALNNELALKS 
       260        270        280        290        300
SSPIIKPDWI IVIHKLTRKI VKERSVNSLI ECRAVLYDLL AHCIPANIIL 
       310        320        330        340        350
KELTFSLLDV ETLNTTNKSS IIEYSSVFDE RLSLGNKAIF HLEGFIAKVM 

CCLD

Length:354

Mass (Da):39,942

Last modified:October 1, 1994 - v1

Checksum:ⁱ4CD403AF2AFA2961

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U26031 Genomic DNA Translation: AAC49065.1 X78993 Genomic DNA Translation: CAA55595.1 Z35956 Genomic DNA Translation: CAA85036.1 AY693173 Genomic DNA Translation: AAT93192.1 BK006936 Genomic DNA Translation: DAA07208.1
PIRⁱ	S48257
NCBI Reference Sequences More...RefSeqⁱ	NP_009644.3, NM_001178435.3

Genome annotation databases

EnsemblFungiⁱ	YBR087W; YBR087W; YBR087W
GeneIDⁱ	852383
KEGGⁱ	sce:YBR087W

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P38251	Rfc5p		YEASB		354	UniRef100_P38251
Replication factor C subunit 5		YEAS1		354
K7_Rfc5p		YEASK		354
Rfc5p		YEAS8		354
Rfc5p		YEASA		354
+6

Protein	Similar proteins		Species	Score	Length	Source
P38251	Rfc5p		YEASB		354	UniRef90_P38251
Replication factor C subunit 5		YEAS1		354
K7_Rfc5p		YEASK		354
Rfc5p		YEAS8		354
Rfc5p		YEASA		354
+11

Protein	Similar proteins		Species	Score	Length	Source
P38251	Rfc5p		YEASB		354	UniRef50_P38251
Replication factor C subunit 5		YEAS1		354
K7_Rfc5p		YEASK		354
Rfc5p		YEAS8		354
Rfc5p		YEASA		354
+36

Entry informationⁱ

Entry nameⁱ	RFC5_YEAST
Accessionⁱ	P38251Primary (citable) accession number: P38251 Secondary accession number(s): D6VQ88
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
	Last sequence update:	October 1, 1994
	Last modified:	September 12, 2018
	This is version 160 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Fungal Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

UniProtKB

UniParc

Help

UniRef

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Annotation systems

Supporting data

UniProtKB - P38251 (RFC5_YEAST)

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Replication factor C subunit 5

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ