ID A0A151ERL0_9EURY Unreviewed; 320 AA.
AC A0A151ERL0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Replication factor C small subunit {ECO:0000256|ARBA:ARBA00014164, ECO:0000256|HAMAP-Rule:MF_01509};
DE Short=RFC small subunit {ECO:0000256|HAMAP-Rule:MF_01509};
DE AltName: Full=Clamp loader small subunit {ECO:0000256|ARBA:ARBA00031749, ECO:0000256|HAMAP-Rule:MF_01509};
GN Name=rfcS {ECO:0000256|HAMAP-Rule:MF_01509};
GN ORFNames=AYK23_04035 {ECO:0000313|EMBL:KYK31276.1};
OS Candidatus Proteinoplasmatales archaeon SG8-5.
OC Archaea; Euryarchaeota; Candidatus Proteinoplasmatales.
OX NCBI_TaxID=1803822 {ECO:0000313|EMBL:KYK31276.1, ECO:0000313|Proteomes:UP000075319};
RN [1] {ECO:0000313|Proteomes:UP000075319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RL Submitted (FEB-2016) 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:0000256|HAMAP-Rule:MF_01509}.
CC -!- SUBUNIT: Heteromultimer composed of small subunits (RfcS) and large
CC subunits (RfcL). {ECO:0000256|HAMAP-Rule:MF_01509}.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family. RfcS
CC subfamily. {ECO:0000256|ARBA:ARBA00009668, ECO:0000256|HAMAP-
CC Rule:MF_01509}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYK31276.1}.
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DR EMBL; LSSH01000004; KYK31276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151ERL0; -.
DR Proteomes; UP000075319; Unassembled WGS sequence.
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 CDD; cd00009; AAA; 1.
DR CDD; cd18140; HLD_clamp_RFC; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 InterPro; IPR047854; RFC_lid.
DR PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR PANTHER; PTHR11669:SF5; REPLICATION FACTOR C SUBUNIT 2; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08542; Rep_fac_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01509}; DNA replication {ECO:0000256|HAMAP-Rule:MF_01509};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01509}.
FT DOMAIN 35..160
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01509"
SQ SEQUENCE 320 AA; 36057 MW; 4DD87F6FF8C0C75C CRC64;
MKRVWVEKYR PKTLDEVVGH KEIVSRLKAY VGSGNMPHLM FAGPAGTGKT TCAIALAREM
FGEHWQNNFH ELNASDERGI DVVRNTIKNF ARTAPLGEGE FKIIFLDEAD ALTSDAQAAL
RRTMEKYTNT CRFILSCNFS SKIIDPIQSR CAVFRFRPLN REEVMEYIGR IAKAEEIDIT
DDGHEALLYV ARGDLRKAVN VFQVSAALGE KVDSEIVYKT SATGRPENIS EMMQLALSGK
FLEAREKLDE LLIEFGLSGE DVIRQMHRAI FDLEVSEEGK VRLIETIGEI EFRLIEGSNS
RIQLESLLAN LAIIGKQLVR
//
