RFCS_METST
ID RFCS_METST Reviewed; 321 AA.
AC Q2NH89;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Msp_0413;
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
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; CP000102; ABC56814.1; -; Genomic_DNA.
DR RefSeq; WP_011406014.1; NC_007681.1.
DR AlphaFoldDB; Q2NH89; -.
DR SMR; Q2NH89; -.
DR STRING; 339860.Msp_0413; -.
DR EnsemblBacteria; ABC56814; ABC56814; Msp_0413.
DR GeneID; 41324987; -.
DR KEGG; mst:Msp_0413; -.
DR eggNOG; arCOG00469; Archaea.
DR HOGENOM; CLU_042324_2_0_2; -.
DR OMA; SCNYSSQ; -.
DR OrthoDB; 37207at2157; -.
DR Proteomes; UP000001931; 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..321
FT /note="Replication factor C small subunit"
FT /id="PRO_0000245640"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01509"
SQ SEQUENCE 321 AA; 36751 MW; 309DB6FFEF415651 CRC64;
MKTPWVEKYR PQTLDDVVGQ EQIVGRLKRY VEEKSLPNIM FTGFAGVGKT TCALALAKSL
LGEYWQQNFL ELNASDARGI DTVRNEIKSF CKLKAVGAPF RIIFLDEVDN MTKDAQQALR
REMEMYTKTS SFILSCNYSS KIIDPIQSRC AIFRFSPIKA ANIIKRLKYI ASEEGIEAEQ
SALENIVYFT QGDMRKSINI LQASTTTENT VTEEAVYDVI SRAKPKDVRK IINKALNHDF
MEARDLLRDI MIIEGVSGDD LITQFYQEVA QMTQEELIPE VEFIKLMEYM SECDYRIREG
SNPRLQLEAL LSKFLLVKQD A