RFCS2_PYRIL
ID RFCS2_PYRIL Reviewed; 320 AA.
AC A1RV38;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Pisl_1668;
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; ABL88820.1; -; Genomic_DNA.
DR RefSeq; WP_011763395.1; NC_008701.1.
DR AlphaFoldDB; A1RV38; -.
DR SMR; A1RV38; -.
DR STRING; 384616.Pisl_1668; -.
DR EnsemblBacteria; ABL88820; ABL88820; Pisl_1668.
DR GeneID; 4617958; -.
DR KEGG; pis:Pisl_1668; -.
DR eggNOG; arCOG00469; Archaea.
DR HOGENOM; CLU_042324_2_1_2; -.
DR OMA; TQIYGFV; -.
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..320
FT /note="Replication factor C small subunit 2"
FT /id="PRO_0000292190"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01509"
SQ SEQUENCE 320 AA; 36426 MW; 1C8D41E2F9976A69 CRC64;
MSELFWFEKY RPRSFDEVVD LEEVKSRLRE FVKSGNMPHL LFYGPPGTGK TTMALVLARE
LYGEYWRENT LELNASDERG INVIRERVKE FARTAPVGKA PFKLVILDEA DNMTSDAQQA
LRRIMEIYAQ NTRFILLANY ISGIIEPIQS RVVMIRFNPL PKEAVISRLR YIAENEGVKI
SDDALETIYE FTQGDMRKAI NALQIAAATE KEITEDVVAR ALGMVSPRLL RETLQEALKG
NFSKAMTQIY GFVVDGGVGE LEIIRQIHRE VLRLDVPEYV KPELAYIIAE AHYATLRGAR
GLTQIFGALA KIRRLLKQAV