RFCL_PYRFU
ID RFCL_PYRFU Reviewed; 479 AA.
AC Q9UWR2;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Replication factor C large subunit;
DE Short=RFC large subunit;
DE AltName: Full=Clamp loader large subunit;
DE AltName: Full=PfuRFC large subunit;
GN Name=rfcL; OrderedLocusNames=PF0092;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=11274122; DOI=10.1128/jb.183.8.2614-2623.2001;
RA Cann I.K.O., Ishino S., Yuasa M., Daiyasu H., Toh H., Ishino Y.;
RT "Biochemical analysis of replication factor C from the hyperthermophilic
RT archaeon Pyrococcus furiosus.";
RL J. Bacteriol. 183:2614-2623(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP ROLE OF THE C-TERMINAL BASIC CLUSTER REGION, AND DOMAIN.
RX PubMed=16172520; DOI=10.1266/ggs.80.83;
RA Nishida H., Ishino S., Miyata T., Morikawa K., Ishino Y.;
RT "Identification of the critical region in replication factor C from
RT Pyrococcus furiosus for the stable complex formation with proliferating
RT cell nuclear antigen and DNA.";
RL Genes Genet. Syst. 80:83-93(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, AND DOMAIN.
RX PubMed=12296822; DOI=10.1046/j.1365-2443.2002.00572.x;
RA Matsumiya S., Ishino S., Ishino Y., Morikawa K.;
RT "Physical interaction between proliferating cell nuclear antigen and
RT replication factor C from Pyrococcus furiosus.";
RL Genes Cells 7:911-922(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:11274122, ECO:0000269|PubMed:12296822}.
CC -!- SUBUNIT: Heteromultimer composed of three to four small subunits (RfcS)
CC and one to two large subunits (RfcL). {ECO:0000269|PubMed:11274122}.
CC -!- DOMAIN: The C-terminal basic cluster region, which consists mainly of
CC lysine residues, is important for the formation of a stable RFC-PCNA-
CC DNA complex, although it is not critical for loading PCNA onto DNA in
CC vitro (PubMed:16172520). An 11-mer corresponding to the PIP-box
CC inhibits DNA synthesis by Pol I (pol). {ECO:0000269|PubMed:12296822,
CC ECO:0000269|PubMed:16172520}.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family. RfcL
CC subfamily. {ECO:0000305}.
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DR EMBL; AB034755; BAA88155.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL80216.1; -; Genomic_DNA.
DR RefSeq; WP_011011204.1; NC_018092.1.
DR PDB; 1ISQ; X-ray; 2.30 A; B=469-479.
DR PDBsum; 1ISQ; -.
DR AlphaFoldDB; Q9UWR2; -.
DR SMR; Q9UWR2; -.
DR STRING; 186497.PF0092; -.
DR EnsemblBacteria; AAL80216; AAL80216; PF0092.
DR GeneID; 41711879; -.
DR KEGG; pfu:PF0092; -.
DR PATRIC; fig|186497.12.peg.96; -.
DR eggNOG; arCOG00470; Archaea.
DR HOGENOM; CLU_027255_1_1_2; -.
DR OMA; GGWTRYG; -.
DR OrthoDB; 24257at2157; -.
DR PhylomeDB; Q9UWR2; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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_01508; RfcL; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR023935; Rep_factor-C_lsu.
DR Pfam; PF00004; AAA; 1.
DR SMART; SM00382; AAA; 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..479
FT /note="Replication factor C large subunit"
FT /id="PRO_0000135962"
FT REGION 424..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..479
FT /note="PCNA interacting protein box (PIP-box)"
FT COMPBIAS 428..452
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:1ISQ"
SQ SEQUENCE 479 AA; 55288 MW; D3D2092F2D9230E8 CRC64;
MPELPWVEKY RPKKLSEIVN QEEAIEKVRA WIESWLHGHP PKKKALLLAG PPGSGKTTTV
YALANEYNFE VIELNASDER TYEKISRYVQ AAYTMDILGK RRKIIFLDEA DNIEPSGAKE
IAKLIDKAKN PIIMAANKYW EVPKEIREKA ELVEYKRLTQ RDVMNALIRI LKREGITVPK
EILLEIAKRS SGDLRAAIND LQTVVVGGYE DATQVLAYRD VEKTVFQALG LVFGSDNAKR
AKMAMWNLDM SPDEFLLWVD ENIPHLYLNP EEIAQAYDAI SRADIYLGRA ARTGNYSLWK
YAIDMMTAGV AVAGRKRRGF VKFYPPNTLK ILAESKEERE IRESIIKKII REMHMSRLQA
IETMKIIREI FENNLDLAAH FTVFLGLSEK EVEFLAGKEK AGTIWGKALA LRRKLKELGI
REEEKPKVEI EEEEEEEEKT EEEKEEIEEK PEEEKEEEKK EKEKPKKGKQ ATLFDFLKK
