ID   RFCS2_PYRAR             Reviewed;         322 AA.
AC   A4WLY0;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=Pars_1846;
OS   Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=340102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700994 / DSM 13514 / JCM 11321 / PZ6;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000660; ABP51397.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WLY0; -.
DR   SMR; A4WLY0; -.
DR   STRING; 340102.Pars_1846; -.
DR   EnsemblBacteria; ABP51397; ABP51397; Pars_1846.
DR   KEGG; pas:Pars_1846; -.
DR   HOGENOM; CLU_042324_2_1_2; -.
DR   OMA; TQIYGFV; -.
DR   PhylomeDB; A4WLY0; -.
DR   Proteomes; UP000001567; 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.
FT   CHAIN           1..322
FT                   /note="Replication factor C small subunit 2"
FT                   /id="PRO_0000296652"
FT   BINDING         44..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01509"
SQ   SEQUENCE   322 AA;  36441 MW;  A94667AD8DEAF238 CRC64;
     MSELFWFEKY RPRSFDEVVD LEEVKARLRE FVRGGNMPHL LFYGPPGTGK TTMALVLARE
     LYGEYWRENT LELNASDERG INVIRERVKE FARTAPVGKA PFKLVILDEA DNMTSDAQQA
     LRRIMEMYAQ NTRFILLANY ISGIIEPIQS RTVMIRFSPL PKEAVFARLR YIADNEGVKI
     SDDALEAIYE FTQGDMRRAI NALQIAATTG KEITEETVAK ALGMVSPRLL RETLNDAFRG
     NFGKAATQIY GFVVDGGIGE LEIVKQLHRE ALKLDVPEYL KPEIAYIIAE AHYAILRGAH
     GLTQIYGALA KIRKLLKYTA SI