ID   RFCS2_PYRAE             Reviewed;         319 AA.
AC   Q8ZWS2;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Replication factor C small subunit 2 {ECO:0000255|HAMAP-Rule:MF_01509};
DE            Short=RFC small subunit 2 {ECO:0000255|HAMAP-Rule:MF_01509};
DE   AltName: Full=Clamp loader small subunit 2 {ECO:0000255|HAMAP-Rule:MF_01509};
GN   Name=rfcS2 {ECO:0000255|HAMAP-Rule:MF_01509}; OrderedLocusNames=PAE1646;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL63627.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZWS2; -.
DR   SMR; Q8ZWS2; -.
DR   STRING; 178306.PAE1646; -.
DR   EnsemblBacteria; AAL63627; AAL63627; PAE1646.
DR   KEGG; pai:PAE1646; -.
DR   PATRIC; fig|178306.9.peg.1217; -.
DR   eggNOG; arCOG00469; Archaea.
DR   HOGENOM; CLU_042324_2_1_2; -.
DR   InParanoid; Q8ZWS2; -.
DR   OMA; TQIYGFV; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0005663; C:DNA replication factor C complex; IBA:GO_Central.
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:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
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..319
FT                   /note="Replication factor C small subunit 2"
FT                   /id="PRO_0000135982"
FT   BINDING         44..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01509"
SQ   SEQUENCE   319 AA;  36050 MW;  999C51588ACFA348 CRC64;
     MSELFWFEKY RPRSFDEVVD LEEVKARLRQ FVKAGNMPHL LFYGPPGTGK TTMALVLARE
     LYGEYWRENT LELNASDERG INVIRERVKE FARTAPVGKA PFKLVILDEA DNMTSDAQQA
     LRRIMEIYAQ NTRFILLANY VSGIIEPIQS RTVMIRFSPL PKEAVFARLR YIAENEGVKV
     SDDALEAIYE FTQGDMRRAI NALQIAATVS KAVTEEVVAK ALGMVSPRLL RETLYEAVKG
     SFGKAATQIY GFVADGGVGE LEIIKQIHRE MLRLDVQEYV KPEIAYIIAE AHYAILRGAH
     GLTQIYGALA KVRRLLKSV