ID A0A2H9I152_9ARCH Unreviewed; 320 AA.
AC A0A2H9I152;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=CP083_01015 {ECO:0000313|EMBL:PDM27008.1};
OS Candidatus Bathyarchaeota archaeon B24-2.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=2041147 {ECO:0000313|EMBL:PDM27008.1, ECO:0000313|Proteomes:UP000228824};
RN [1] {ECO:0000313|EMBL:PDM27008.1, ECO:0000313|Proteomes:UP000228824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B24-2 {ECO:0000313|EMBL:PDM27008.1};
RA Feng X., Perumal V., Wang F.;
RT "Metabolic analysis of an uncultured genome Bathyarchaeota B242 based on
RT metagenomic technology.";
RL Submitted (SEP-2017) 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:PDM27008.1}.
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DR EMBL; PCNA01000006; PDM27008.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9I152; -.
DR Proteomes; UP000228824; 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 32..159
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01509"
SQ SEQUENCE 320 AA; 36248 MW; 6F6F3E3B037B1EB7 CRC64;
MWTEKYRPRS LSEIVNQEDI VNRLIGFVKA KNVPHCLFAG PPGTGKTTAA LCLAHDLYGE
GYRDYIMELN ASDERGIDVI RETVKTFART RPIGEVPFKI LILDEADNMT ADAQQALRRT
MERYTETCRF ILIANFPGRI IEPIQSRCAP FRFTFLSRED LTGRLRYIAE MEKVQLLEDG
IDAIIEISEG DLRKAINILQ AAASVGKPVD KEVVYGVVGR ANPYDVRELI RMAMEGEFVK
AREKLRELML KYGVSGSDLV KQIHSEIFQL EIPEKWKIRL ASAIGETEFR LIQGGDDEIQ
LSALLARLVE VGQIIGKDRE
//
