ID A0A256ZW75_9CREN Unreviewed; 326 AA.
AC A0A256ZW75;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=rfc {ECO:0000313|EMBL:OYT56697.1};
GN Synonyms=rfcS {ECO:0000256|HAMAP-Rule:MF_01509};
GN ORFNames=B6U76_02970 {ECO:0000313|EMBL:OYT56697.1};
OS Desulfurococcales archaeon ex4484_217_2.
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales.
OX NCBI_TaxID=2012519 {ECO:0000313|EMBL:OYT56697.1, ECO:0000313|Proteomes:UP000216854};
RN [1] {ECO:0000313|Proteomes:UP000216854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K.W., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (JUN-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:OYT56697.1}.
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DR EMBL; NJEC01000030; OYT56697.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A256ZW75; -.
DR Proteomes; UP000216854; 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 40..168
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 48..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01509"
SQ SEQUENCE 326 AA; 36808 MW; 939DF2C67839610C CRC64;
MASIEAELLW AEKYRPKSLD EIVNQKEIVE RLKQFVKHRN MPHCLFAGPP GTGKTTAALA
LAHDLYGENY HRYVLELNAS DARGIDVIRT TVKEFARSIV PGEIPFKIII LDEADNMTAD
AQQALRRTME LFTATCRFIL IANYPSKIIE PIQSRTAFFR FTPLSKEDVV ARLKWIADQE
KVEYDMEALE TIYELSEGDM RRAINILQAA SALGRVTVEA VYKVIGAAHP AEVREMIKAA
LAGRFTEARE KLRALMINYG LSGVDVVKAM HREIFSSEIK IPEELRVIIA DYLGEVQYRL
AEGADDEIQL SALIAKLVML GRKLRV
//
