Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Replication factor C small subunit

Gene

rfcS

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA. The complex possesses DNA-dependent ATPase activity which is further stimulated by PCNA.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Replication factor C small subunit
Short name:
RFC small subunit
Alternative name(s):
Clamp loader small subunit
PfuRFC small subunit
Cleaved into the following chain:
Gene namesi
Name:rfcS
Ordered Locus Names:PF0093
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000001013 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi785 – 7851E → A: Decreases the stability of the PCNA-RFC complex and reduces the clamp-loading activity; when associated with A-795; A-796; A-831 and A-835. 1 Publication
Mutagenesisi795 – 7951E → A: Decreases the stability of the PCNA-RFC complex and reduces the clamp-loading activity; when associated with A-785; A-796; A-831 and A-835. 1 Publication
Mutagenesisi796 – 7961D → A: Decreases the stability of the PCNA-RFC complex and reduces the clamp-loading activity; when associated with A-785; A-795; A-831 and A-835. 1 Publication
Mutagenesisi831 – 8311E → A: Decreases the stability of the PCNA-RFC complex and reduces the clamp-loading activity; when associated with A-785; A-795; A-796 and A-835. 1 Publication
Mutagenesisi835 – 8351E → A: Decreases the stability of the PCNA-RFC complex and reduces the clamp-loading activity; when associated with A-785; A-795; A-796 and A-831. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5959Replication factor C small subunit, 1st partSequence analysisPRO_0000030376Add
BLAST
Chaini60 – 584525Pfu RFC inteinSequence analysisPRO_0000030377Add
BLAST
Chaini585 – 852268Replication factor C small subunit, 2nd partSequence analysisPRO_0000030378Add
BLAST

Post-translational modificationi

This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.Curated

Keywords - PTMi

Autocatalytic cleavage, Protein splicing

Proteomic databases

PRIDEiQ8U4J3.

Interactioni

Subunit structurei

Heteromultimer composed of three to four small subunits (RfcS) and one to two large subunits (RfcL).1 Publication

Protein-protein interaction databases

STRINGi186497.PF0093.

Structurei

Secondary structure

1
852
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi584 – 59613Combined sources
Helixi597 – 5993Combined sources
Helixi600 – 6034Combined sources
Beta strandi604 – 6085Combined sources
Helixi612 – 6165Combined sources
Helixi619 – 6279Combined sources
Helixi631 – 6333Combined sources
Beta strandi637 – 6426Combined sources
Helixi644 – 6463Combined sources
Helixi649 – 66113Combined sources
Turni662 – 6654Combined sources
Beta strandi666 – 6738Combined sources
Helixi675 – 6773Combined sources
Helixi680 – 6845Combined sources
Beta strandi686 – 6905Combined sources
Helixi696 – 70813Combined sources
Turni709 – 7113Combined sources
Helixi716 – 72611Combined sources
Helixi730 – 74112Combined sources
Beta strandi745 – 7473Combined sources
Helixi749 – 7557Combined sources
Helixi761 – 77313Combined sources
Helixi776 – 79015Combined sources
Helixi794 – 80411Combined sources
Helixi805 – 8073Combined sources
Beta strandi808 – 8103Combined sources
Helixi812 – 83019Combined sources
Helixi835 – 85016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IQPX-ray2.80A/B/C/D/E/F1-59[»]
A/B/C/D/E/F585-852[»]
ProteinModelPortaliQ8U4J3.
SMRiQ8U4J3. Positions 2-59, 571-852.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8U4J3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini183 – 306124DOD-type homing endonucleasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 DOD-type homing endonuclease domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiarCOG00469. Archaea.
arCOG03154. Archaea.
COG0470. LUCA.
COG1372. LUCA.
HOGENOMiHOG000154101.
KOiK04801.
OMAiRFMELTE.

Family and domain databases

Gene3Di2.170.16.10. 2 hits.
3.10.28.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR008921. DNA_pol3_clamp-load_cplx_C.
IPR028992. Hedgehog/Intein_dom.
IPR003586. Hint_dom_C.
IPR003587. Hint_dom_N.
IPR027434. Homing_endonucl.
IPR006142. INTEIN.
IPR030934. Intein_C.
IPR004042. Intein_endonuc.
IPR006141. Intein_N.
IPR004860. LAGLIDADG_2.
IPR027417. P-loop_NTPase.
IPR013748. Rep_factorC_C.
IPR008824. RuvB_N.
[Graphical view]
PfamiPF14528. LAGLIDADG_3. 1 hit.
PF08542. Rep_fac_C. 1 hit.
PF05496. RuvB_N. 1 hit.
[Graphical view]
PRINTSiPR00379. INTEIN.
SMARTiSM00305. HintC. 1 hit.
SM00306. HintN. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF51294. SSF51294. 2 hits.
SSF52540. SSF52540. 2 hits.
SSF55608. SSF55608. 1 hit.
TIGRFAMsiTIGR01443. intein_Cterm. 1 hit.
TIGR01445. intein_Nterm. 1 hit.
PROSITEiPS50818. INTEIN_C_TER. 1 hit.
PS50819. INTEIN_ENDONUCLEASE. 1 hit.
PS50817. INTEIN_N_TER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8U4J3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEEIREVKV LEKPWVEKYR PQRLDDIVGQ EHIVKRLKHY VKTGSMPHLL
60 70 80 90 100
FAGPPGVGKC LTGDTKVIAN GQLFELGELV EKLSGGRFGP TPVKGLKVLG
110 120 130 140 150
IDEDGKLREF EVQYVYKDRT DRLIKIKTQL GRELKVTPYH PLLVNRENGE
160 170 180 190 200
IKWIKAEELK PGDKLAIPSF LPLITGENPL AEWLGYFMGS GYAYPSNSVI
210 220 230 240 250
TFTNEDPLIR QRFMELTEKL FPDAKIRERI HADGTPEVYV VSRKAWSLVN
260 270 280 290 300
SISLTLIPRE GWKGIRSFLR AYSDCNGRIE SDAIVLSTDN NDMAQQIAYA
310 320 330 340 350
LASFGIIAKM DGEDVIISGS DNIERFLNEI GFSTQSKLKE AQKLIRKTNV
360 370 380 390 400
RSDGLKINYE LISYVKDRLR LNVNDKRNLS YRNAKELSWE LMKEIYYRLE
410 420 430 440 450
ELERLKKVLS EPILIDWNEV AKKSDEVIEK AKIRAEKLLE YIKGERKPSF
460 470 480 490 500
KEYIEIAKVL GINVERTIEA MKIFAKRYSS YAEIGRKLGT WNFNVKTILE
510 520 530 540 550
SDTVDNVEIL EKIRKIELEL IEEILSDGKL KEGIAYLIFL FQNELYWDEI
560 570 580 590 600
TEVKELRGDF IIYDLHVPGY HNFIAGNMPT VVHNTTAALA LARELFGENW
610 620 630 640 650
RHNFLELNAS DERGINVIRE KVKEFARTKP IGGASFKIIF LDEADALTQD
660 670 680 690 700
AQQALRRTME MFSSNVRFIL SCNYSSKIIE PIQSRCAIFR FRPLRDEDIA
710 720 730 740 750
KRLRYIAENE GLELTEEGLQ AILYIAEGDM RRAINILQAA AALDKKITDE
760 770 780 790 800
NVFMVASRAR PEDIREMMLL ALKGNFLKAR EKLREILLKQ GLSGEDVLVQ
810 820 830 840 850
MHKEVFNLPI EEPKKVLLAD KIGEYNFRLV EGANEIIQLE ALLAQFTLIG

KK
Length:852
Mass (Da):97,793
Last modified:June 1, 2002 - v1
Checksum:iD4C8B4B945F9946A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL80217.1.
AB037375 Genomic DNA. Translation: BAB03291.1.
AB037375 Genomic DNA. Translation: BAB03292.1.
RefSeqiWP_011011205.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL80217; AAL80217; PF0093.
GeneIDi1467922.
KEGGipfu:PF0093.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL80217.1.
AB037375 Genomic DNA. Translation: BAB03291.1.
AB037375 Genomic DNA. Translation: BAB03292.1.
RefSeqiWP_011011205.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IQPX-ray2.80A/B/C/D/E/F1-59[»]
A/B/C/D/E/F585-852[»]
ProteinModelPortaliQ8U4J3.
SMRiQ8U4J3. Positions 2-59, 571-852.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF0093.

Proteomic databases

PRIDEiQ8U4J3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL80217; AAL80217; PF0093.
GeneIDi1467922.
KEGGipfu:PF0093.

Phylogenomic databases

eggNOGiarCOG00469. Archaea.
arCOG03154. Archaea.
COG0470. LUCA.
COG1372. LUCA.
HOGENOMiHOG000154101.
KOiK04801.
OMAiRFMELTE.

Miscellaneous databases

EvolutionaryTraceiQ8U4J3.

Family and domain databases

Gene3Di2.170.16.10. 2 hits.
3.10.28.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR008921. DNA_pol3_clamp-load_cplx_C.
IPR028992. Hedgehog/Intein_dom.
IPR003586. Hint_dom_C.
IPR003587. Hint_dom_N.
IPR027434. Homing_endonucl.
IPR006142. INTEIN.
IPR030934. Intein_C.
IPR004042. Intein_endonuc.
IPR006141. Intein_N.
IPR004860. LAGLIDADG_2.
IPR027417. P-loop_NTPase.
IPR013748. Rep_factorC_C.
IPR008824. RuvB_N.
[Graphical view]
PfamiPF14528. LAGLIDADG_3. 1 hit.
PF08542. Rep_fac_C. 1 hit.
PF05496. RuvB_N. 1 hit.
[Graphical view]
PRINTSiPR00379. INTEIN.
SMARTiSM00305. HintC. 1 hit.
SM00306. HintN. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF51294. SSF51294. 2 hits.
SSF52540. SSF52540. 2 hits.
SSF55608. SSF55608. 1 hit.
TIGRFAMsiTIGR01443. intein_Cterm. 1 hit.
TIGR01445. intein_Nterm. 1 hit.
PROSITEiPS50818. INTEIN_C_TER. 1 hit.
PS50819. INTEIN_ENDONUCLEASE. 1 hit.
PS50817. INTEIN_N_TER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRFCS_PYRFU
AccessioniPrimary (citable) accession number: Q8U4J3
Secondary accession number(s): Q9P9H2, Q9P9H3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: June 1, 2002
Last modified: January 20, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The intein interrupts the potential ATP-binding site.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Intein-containing proteins
    List of intein-containing protein entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.