RFCS1_PYRIL
ID RFCS1_PYRIL Reviewed; 329 AA.
AC A1RSA2;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=Pisl_0656;
OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=384616;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL Submitted (DEC-2006) 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; CP000504; ABL87834.1; -; Genomic_DNA.
DR RefSeq; WP_011762410.1; NC_008701.1.
DR AlphaFoldDB; A1RSA2; -.
DR SMR; A1RSA2; -.
DR STRING; 384616.Pisl_0656; -.
DR EnsemblBacteria; ABL87834; ABL87834; Pisl_0656.
DR GeneID; 4618319; -.
DR KEGG; pis:Pisl_0656; -.
DR eggNOG; arCOG00469; Archaea.
DR HOGENOM; CLU_042324_2_1_2; -.
DR OMA; SCNYSSQ; -.
DR OrthoDB; 37207at2157; -.
DR Proteomes; UP000002595; 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_0000292189"
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; 37462 MW; F6C68F9A4A3B919E CRC64;
MAELFWFEKY RPRSFDEVVD LEEVKSRLRE FVKSGNMPHL LFYGPPGTGK TTMALVLARE
LYGEYWRENT LELNASDERG INVIRERVKE FARTAPVGKA PFKLVILDEA DNMTSDAQQA
LRRIMEIYAQ NTRFILLANY VSRIIDPIIS RCAVFRFSPM PRHLMAERLK YIAKSEGVEV
KEDAIDLIYE LSEGDMRKAI NILQVAAATN KIVDRNVVAA AAAAIRPTDI VELFNLALSG
DYLKAREKMR ELMYVKGVAG VDFIRAFQRE LIRMSLDDET KAEVAELLAD VDYRLTQGAD
EEIQLSYFLA KLGSIGKKIR AASLPPKKR
