RFCS1_PYRAR
ID RFCS1_PYRAR Reviewed; 329 AA.
AC A4WGV2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Replication factor C small subunit 1 {ECO:0000255|HAMAP-Rule:MF_01509};
DE Short=RFC small subunit 1 {ECO:0000255|HAMAP-Rule:MF_01509};
DE AltName: Full=Clamp loader small subunit 1 {ECO:0000255|HAMAP-Rule:MF_01509};
GN Name=rfcS1 {ECO:0000255|HAMAP-Rule:MF_01509}; OrderedLocusNames=Pars_0002;
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; ABP49619.1; -; Genomic_DNA.
DR AlphaFoldDB; A4WGV2; -.
DR SMR; A4WGV2; -.
DR STRING; 340102.Pars_0002; -.
DR EnsemblBacteria; ABP49619; ABP49619; Pars_0002.
DR KEGG; pas:Pars_0002; -.
DR HOGENOM; CLU_042324_2_1_2; -.
DR OMA; SCNYSSQ; -.
DR PhylomeDB; A4WGV2; -.
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..329
FT /note="Replication factor C small subunit 1"
FT /id="PRO_0000296651"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01509"
SQ SEQUENCE 329 AA; 37504 MW; FBAB6B2564D0BC7C CRC64;
MAELFWFEKY RPRSFDEVVD LEEVKARLRE FVRGGNMPHL LFYGPPGTGK TTMALVLARE
LYGEYWRENT LELNASDERG INVIRERVKE FARTAPVGKA PFKLVILDEA DNMTSDAQQA
LRRIMEMYAQ NTRFILLANY VSRIIDPIIS RCAVFRFSPM PRSLMAERLR HIAKSEGIEL
RDDAIDLIYE VSEGDMRKAI NLLQVAAATS KVVDANAVAS ATTMIRPADV VELFNLAFNG
DVTKAREKLR ELMYVKGIAG IDFIRAFQRE LIRMPLDDEV KAEIAELLAE VDYRLTQGSD
EELQLLYLLS KLGAIGKRAR QTPPPSKRR