RFCS_METS3
ID RFCS_METS3 Reviewed; 315 AA.
AC A5UMF3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Msm_1176;
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ87381.1; -; Genomic_DNA.
DR RefSeq; WP_011954334.1; NC_009515.1.
DR AlphaFoldDB; A5UMF3; -.
DR SMR; A5UMF3; -.
DR STRING; 420247.Msm_1176; -.
DR EnsemblBacteria; ABQ87381; ABQ87381; Msm_1176.
DR GeneID; 5216359; -.
DR KEGG; msi:Msm_1176; -.
DR PATRIC; fig|420247.28.peg.1175; -.
DR eggNOG; arCOG00469; Archaea.
DR HOGENOM; CLU_042324_2_0_2; -.
DR OMA; SCNYSSQ; -.
DR Proteomes; UP000001992; 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..315
FT /note="Replication factor C small subunit"
FT /id="PRO_0000301268"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01509"
SQ SEQUENCE 315 AA; 35554 MW; D6B40C12B132B2C8 CRC64;
MSGPWVEKYR PQNLDDIIGQ KQIVNRLQKY VGEESMPNLM FTGPAGVGKT TTAIALVKAI
LGEYWRQNFL ELNASDARGI DTVRNDIKNF CRLKPVGAPF RIIFLDEVDN MTKDAQHALR
REMEMYTKTA SFILSCNYSS KIIDPIQSRC AIFRFGPIKG EEIANRLKYI CTSERFEYTD
GGIEAIEYFA EGDMRKAVNV LQAAASEGKQ VDEDAVYEVV SKAKPQDVHN LITKALSGDF
MGARNLLRET MVLQGTSGED MVSQIYQDVS KRVFEGKMEA DIYIDLIEAI ADCDFRIREG
ANPRIQLEAL LTQFL