ID   RFCS_NANEQ              Reviewed;         322 AA.
AC   P60374;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=NEQ170;
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M;
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA   Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA   Stetter K.O., Short J.M., Noorderwier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
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; AE017199; AAR39023.1; -; Genomic_DNA.
DR   AlphaFoldDB; P60374; -.
DR   SMR; P60374; -.
DR   STRING; 228908.NEQ170; -.
DR   EnsemblBacteria; AAR39023; AAR39023; NEQ170.
DR   KEGG; neq:NEQ170; -.
DR   PATRIC; fig|228908.8.peg.173; -.
DR   HOGENOM; CLU_042324_2_1_2; -.
DR   OMA; SCNYSSQ; -.
DR   Proteomes; UP000000578; 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..322
FT                   /note="Replication factor C small subunit"
FT                   /id="PRO_0000135978"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01509"
SQ   SEQUENCE   322 AA;  36825 MW;  41A8EAA5C3F932EE CRC64;
     MEIWTEKYRP KRIDDIINQE EIKKALKSFV EKKNMPHLLF AGPPGTGKTT AALALAHELY
     GDAWRENFLE LNASDERGID VIRHKVKEFA RAKPIGDVPF KIVFLDEADA LTRDAQQALR
     RIMEKYSQST RFILSCNYFS KIIEPIQSRV TVFKFKPLEK EAFRELINRI VKGEGLILEN
     EDEIINALYD IAEGDLRKAI NILQAAAMMS KTITVDRLYE IASIAKPKEI DEVLNKAMQG
     NFLEARSMLI DLMLKYGMSG EDVIKAIQKR VWSLPISDRE KLMILDKIGD IEFRIVEGAD
     DLVQLDALLA WLGLGKYKNF TS