RFCS_SULAC
ID RFCS_SULAC Reviewed; 325 AA.
AC Q4JAB0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Replication factor C small subunit {ECO:0000255|HAMAP-Rule:MF_01509};
DE Short=RFC small subunit {ECO:0000255|HAMAP-Rule:MF_01509};
DE AltName: Full=Clamp loader small subunit {ECO:0000255|HAMAP-Rule:MF_01509};
GN Name=rfcS {ECO:0000255|HAMAP-Rule:MF_01509}; OrderedLocusNames=Saci_0907;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
CC -!- FUNCTION: Part of the RFC clamp loader complex which loads the PCNA
CC sliding clamp onto DNA. {ECO:0000255|HAMAP-Rule:MF_01509}.
CC -!- SUBUNIT: Heteromultimer composed of small subunits (RfcS) and large
CC subunits (RfcL). {ECO:0000255|HAMAP-Rule:MF_01509}.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family. RfcS
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01509}.
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DR EMBL; CP000077; AAY80270.1; -; Genomic_DNA.
DR RefSeq; WP_011277772.1; NC_007181.1.
DR AlphaFoldDB; Q4JAB0; -.
DR SMR; Q4JAB0; -.
DR STRING; 330779.Saci_0907; -.
DR EnsemblBacteria; AAY80270; AAY80270; Saci_0907.
DR GeneID; 3473018; -.
DR KEGG; sai:Saci_0907; -.
DR PATRIC; fig|330779.12.peg.867; -.
DR eggNOG; arCOG00469; Archaea.
DR HOGENOM; CLU_042324_2_1_2; -.
DR OMA; SCNYSSQ; -.
DR Proteomes; UP000001018; 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 3: Inferred from homology;
KW ATP-binding; DNA replication; Nucleotide-binding; Reference proteome.
FT CHAIN 1..325
FT /note="Replication factor C small subunit"
FT /id="PRO_0000135983"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01509"
SQ SEQUENCE 325 AA; 37015 MW; 18B69C97FA30F9BF CRC64;
MEEEILWAEK YRPKSLDEIV NQKEIVERLK KFVKEKNMPH LLFAGPPGTG KTTAALALVR
DLYGNNYRQY FLELNASDER GIDVIRNKVK EFARTVASNN VPFKVILLDE ADNMTADAQQ
ALRRTMELYT ETTRFILACN YLSKIIEPIQ SRTALFRFYP LKKEDVVNRL IQIAKNEKVE
FDPKGIETIF DITQGDMRKA INVIQAASAY GKITVETVYK VLGLAQPKEI REMLHLALSG
KFLQARDKLR ELLINYGLSG EDIIKQVHKE LTGNEISIPD DLKVILVDYA GEVEFRIMEG
ADDEIQLSAF LAKLALHAEK YSGGK