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Entry version 183 (11 Dec 2019)
Sequence version 1 (01 Oct 1994)
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Protein

Replication factor C subunit 1

Gene

RFC1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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.

Miscellaneous

Present with 2360 molecules/cell in log phase SD medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei299ATP; via carbonyl oxygen1
Binding sitei311ATP; via amide nitrogen and carbonyl oxygen1
Binding sitei456ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi353 – 361ATP9

<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

  • cell division Source: UniProtKB-KW
  • DNA repair Source: SGD
  • leading strand elongation Source: SGD
  • mismatch repair Source: SGD
  • mitotic cell cycle Source: SGD

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-33719-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
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-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

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Replication factor C subunit 1
Short name:
Replication factor C1
Alternative name(s):
Activator 1 95 kDa subunit
Cell division control protein 44
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RFC1
Synonyms:CDC44
Ordered Locus Names:YOR217W
ORF Names:YOR50-7
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XV

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YOR217W

Saccharomyces Genome Database

More...
SGDi
S000005743 RFC1

<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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi427D → H in cs mutant CDC44-2; causes cell cycle arrest. 1 Publication1
Mutagenesisi436G → R in cs mutant CDC44-3/4; causes cell cycle arrest. 1 Publication1
Mutagenesisi512G → A in cs mutant CDC44-9; no effect. 1 Publication1
Mutagenesisi513D → N in cs mutants CDC44-1/5/8 and CDC44-9; causes cell cycle arrest. 1 Publication1

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001217761 – 861Replication factor C subunit 1Add BLAST861

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei38PhosphothreonineCombined sources1
Modified residuei40PhosphoserineCombined sources1
Modified residuei63PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P38630

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P38630

PRoteomics IDEntifications database

More...
PRIDEi
P38630

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P38630

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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.

Interacts with ECO1 and POL30/PCNA.

5 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
34612, 276 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-545 DNA replication factor C complex

Database of interacting proteins

More...
DIPi
DIP-2527N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P38630

Protein interaction database and analysis system

More...
IntActi
P38630, 16 interactors

Molecular INTeraction database

More...
MINTi
P38630

STRING: functional protein association networks

More...
STRINGi
4932.YOR217W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P38630 protein

<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

1861
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P38630

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P38630

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini153 – 243BRCTPROSITE-ProRule annotationAdd BLAST91

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi830 – 834Nuclear localization signalSequence analysis5
Motifi855 – 860Nuclear localization signalSequence analysis6

<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

Belongs to the activator 1 large subunit family.Curated

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000164552

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P38630

KEGG Orthology (KO)

More...
KOi
K10754

Identification of Orthologs from Complete Genome Data

More...
OMAi
HVVLKPW

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.10190, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003593 AAA+_ATPase
IPR003959 ATPase_AAA_core
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR008921 DNA_pol3_clamp-load_cplx_C
IPR013725 DNA_replication_fac_RFC1_C
IPR027417 P-loop_NTPase
IPR012178 RFC1

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00004 AAA, 1 hit
PF00533 BRCT, 1 hit
PF08519 RFC1, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF036578 RFC1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00382 AAA, 1 hit
SM00292 BRCT, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48019 SSF48019, 1 hit
SSF52113 SSF52113, 1 hit
SSF52540 SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50172 BRCT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P38630-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVNISDFFGK NKKSVRSSTS RPTRQVGSSK PEVIDLDTES DQESTNKTPK
60 70 80 90 100
KMPVSNVIDV SETPEGEKKL PLPAKRKASS PTVKPASSKK TKPSSKSSDS
110 120 130 140 150
ASNITAQDVL DKIPSLDLSN VHVKENAKFD FKSANSNADP DEIVSEIGSF
160 170 180 190 200
PEGKPNCLLG LTIVFTGVLP TLERGASEAL AKRYGARVTK SISSKTSVVV
210 220 230 240 250
LGDEAGPKKL EKIKQLKIKA IDEEGFKQLI AGMPAEGGDG EAAEKARRKL
260 270 280 290 300
EEQHNIATKE AELLVKKEEE RSKKLAATRV SGGHLERDNV VREEDKLWTV
310 320 330 340 350
KYAPTNLQQV CGNKGSVMKL KNWLANWENS KKNSFKHAGK DGSGVFRAAM
360 370 380 390 400
LYGPPGIGKT TAAHLVAQEL GYDILEQNAS DVRSKTLLNA GVKNALDNMS
410 420 430 440 450
VVGYFKHNEE AQNLNGKHFV IIMDEVDGMS GGDRGGVGQL AQFCRKTSTP
460 470 480 490 500
LILICNERNL PKMRPFDRVC LDIQFRRPDA NSIKSRLMTI AIREKFKLDP
510 520 530 540 550
NVIDRLIQTT RGDIRQVINL LSTISTTTKT INHENINEIS KAWEKNIALK
560 570 580 590 600
PFDIAHKMLD GQIYSDIGSR NFTLNDKIAL YFDDFDFTPL MIQENYLSTR
610 620 630 640 650
PSVLKPGQSH LEAVAEAANC ISLGDIVEKK IRSSEQLWSL LPLHAVLSSV
660 670 680 690 700
YPASKVAGHM AGRINFTAWL GQNSKSAKYY RLLQEIHYHT RLGTSTDKIG
710 720 730 740 750
LRLDYLPTFR KRLLDPFLKQ GADAISSVIE VMDDYYLTKE DWDSIMEFFV
760 770 780 790 800
GPDVTTAIIK KIPATVKSGF TRKYNSMTHP VAIYRTGSTI GGGGVGTSTS
810 820 830 840 850
TPDFEDVVDA DDNPVPADDE ETQDSSTDLK KDKLIKQKAK PTKRKTATSK
860
PGGSKKRKTK A
Length:861
Mass (Da):94,903
Last modified:October 1, 1994 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA7D9208D66DD9A98
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U03102 Unassigned DNA Translation: AAC48916.1
U26027 Genomic DNA Translation: AAC49060.1
X92441 Genomic DNA Translation: CAA63180.1
Z75125 Genomic DNA Translation: CAA99434.1
BK006948 Genomic DNA Translation: DAA10989.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S44763

NCBI Reference Sequences

More...
RefSeqi
NP_014860.1, NM_001183636.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YOR217W_mRNA; YOR217W; YOR217W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
854392

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YOR217W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03102 Unassigned DNA Translation: AAC48916.1
U26027 Genomic DNA Translation: AAC49060.1
X92441 Genomic DNA Translation: CAA63180.1
Z75125 Genomic DNA Translation: CAA99434.1
BK006948 Genomic DNA Translation: DAA10989.1
PIRiS44763
RefSeqiNP_014860.1, NM_001183636.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SXJX-ray2.85A295-785[»]
SMRiP38630
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi34612, 276 interactors
ComplexPortaliCPX-545 DNA replication factor C complex
DIPiDIP-2527N
ELMiP38630
IntActiP38630, 16 interactors
MINTiP38630
STRINGi4932.YOR217W

PTM databases

iPTMnetiP38630

Proteomic databases

MaxQBiP38630
PaxDbiP38630
PRIDEiP38630

Genome annotation databases

EnsemblFungiiYOR217W_mRNA; YOR217W; YOR217W
GeneIDi854392
KEGGisce:YOR217W

Organism-specific databases

EuPathDBiFungiDB:YOR217W
SGDiS000005743 RFC1

Phylogenomic databases

HOGENOMiHOG000164552
InParanoidiP38630
KOiK10754
OMAiHVVLKPW

Enzyme and pathway databases

BioCyciYEAST:G3O-33719-MONOMER
ReactomeiR-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-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

Miscellaneous databases

EvolutionaryTraceiP38630

Protein Ontology

More...
PROi
PR:P38630
RNActiP38630 protein

Family and domain databases

Gene3Di3.40.50.10190, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR003959 ATPase_AAA_core
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR008921 DNA_pol3_clamp-load_cplx_C
IPR013725 DNA_replication_fac_RFC1_C
IPR027417 P-loop_NTPase
IPR012178 RFC1
PfamiView protein in Pfam
PF00004 AAA, 1 hit
PF00533 BRCT, 1 hit
PF08519 RFC1, 1 hit
PIRSFiPIRSF036578 RFC1, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SM00292 BRCT, 1 hit
SUPFAMiSSF48019 SSF48019, 1 hit
SSF52113 SSF52113, 1 hit
SSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS50172 BRCT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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 subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRFC1_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P38630
Secondary accession number(s): D6W2S3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: December 11, 2019
This is version 183 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<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

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names
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