RFCS_ARCFU
ID RFCS_ARCFU Reviewed; 319 AA.
AC O28219;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Replication factor C small subunit;
DE Short=RFC small subunit;
DE AltName: Full=Clamp loader small subunit;
DE AltName: Full=afRFC small subunit;
DE Short=afRFCsm;
GN Name=rfcS; OrderedLocusNames=AF_2060;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP FUNCTION, AND SUBUNIT.
RX PubMed=12384579; DOI=10.1093/nar/gkf584;
RA Seybert A., Scott D.J., Scaife S., Singleton M.R., Wigley D.B.;
RT "Biochemical characterisation of the clamp/clamp loader proteins from the
RT euryarchaeon Archaeoglobus fulgidus.";
RL Nucleic Acids Res. 30:4329-4338(2002).
CC -!- FUNCTION: Part of the RFC clamp loader complex which loads the PCNA
CC sliding clamp onto DNA. The complex possesses DNA-dependent ATPase
CC activity which is further stimulated by PCNA.
CC {ECO:0000269|PubMed:12384579}.
CC -!- SUBUNIT: Heteropentamer composed of four small subunits (RfcS) and one
CC large subunit (RfcL). Both subunits interact with PCNA.
CC {ECO:0000269|PubMed:12384579}.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family. RfcS
CC subfamily. {ECO:0000305}.
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DR EMBL; AE000782; AAB89191.1; -; Genomic_DNA.
DR PIR; C69507; C69507.
DR RefSeq; WP_010879552.1; NC_000917.1.
DR PDB; 2CHG; X-ray; 2.10 A; A/B/C/D=1-226.
DR PDB; 2CHQ; X-ray; 3.50 A; A/B/C=1-319.
DR PDB; 2CHV; X-ray; 4.00 A; A/B/C/D/E/F=1-319.
DR PDBsum; 2CHG; -.
DR PDBsum; 2CHQ; -.
DR PDBsum; 2CHV; -.
DR AlphaFoldDB; O28219; -.
DR SMR; O28219; -.
DR STRING; 224325.AF_2060; -.
DR EnsemblBacteria; AAB89191; AAB89191; AF_2060.
DR GeneID; 24795809; -.
DR KEGG; afu:AF_2060; -.
DR eggNOG; arCOG00469; Archaea.
DR HOGENOM; CLU_042324_1_0_2; -.
DR OMA; SCNYSSQ; -.
DR OrthoDB; 37207at2157; -.
DR PhylomeDB; O28219; -.
DR BRENDA; 3.6.4.B8; 414.
DR EvolutionaryTrace; O28219; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005663; C:DNA replication factor C complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003689; F:DNA clamp loader activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01509; RfcS; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR023748; Rep_factor-C_ssu_arc.
DR InterPro; IPR013748; Rep_factorC_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08542; Rep_fac_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA replication; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..319
FT /note="Replication factor C small subunit"
FT /id="PRO_0000135971"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:2CHG"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:2CHG"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:2CHG"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:2CHG"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:2CHG"
FT HELIX 64..70
FT /evidence="ECO:0007829|PDB:2CHG"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:2CHG"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:2CHG"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2CHQ"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:2CHG"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2CHG"
FT HELIX 116..128
FT /evidence="ECO:0007829|PDB:2CHG"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:2CHG"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:2CHG"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2CHG"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:2CHG"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:2CHG"
FT HELIX 163..177
FT /evidence="ECO:0007829|PDB:2CHG"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:2CHG"
FT HELIX 197..209
FT /evidence="ECO:0007829|PDB:2CHG"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:2CHQ"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:2CHG"
FT HELIX 228..240
FT /evidence="ECO:0007829|PDB:2CHQ"
FT HELIX 243..256
FT /evidence="ECO:0007829|PDB:2CHQ"
FT HELIX 261..273
FT /evidence="ECO:0007829|PDB:2CHQ"
FT HELIX 281..297
FT /evidence="ECO:0007829|PDB:2CHQ"
FT HELIX 302..315
FT /evidence="ECO:0007829|PDB:2CHQ"
SQ SEQUENCE 319 AA; 35994 MW; 0EBD27AE0AD827DC CRC64;
MENFEIWVEK YRPRTLDEVV GQDEVIQRLK GYVERKNIPH LLFSGPPGTG KTATAIALAR
DLFGENWRDN FIEMNASDER GIDVVRHKIK EFARTAPIGG APFKIIFLDE ADALTADAQA
ALRRTMEMYS KSCRFILSCN YVSRIIEPIQ SRCAVFRFKP VPKEAMKKRL LEICEKEGVK
ITEDGLEALI YISGGDFRKA INALQGAAAI GEVVDADTIY QITATARPEE MTELIQTALK
GNFMEARELL DRLMVEYGMS GEDIVAQLFR EIISMPIKDS LKVQLIDKLG EVDFRLTEGA
NERIQLDAYL AYLSTLAKK
