ID A0A256YZC8_9ARCH Unreviewed; 325 AA.
AC A0A256YZC8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=B6U84_02030 {ECO:0000313|EMBL:OYT45577.1};
OS Candidatus Bathyarchaeota archaeon ex4484_40.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=2012513 {ECO:0000313|EMBL:OYT45577.1, ECO:0000313|Proteomes:UP000216196};
RN [1] {ECO:0000313|Proteomes:UP000216196}
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:OYT45577.1}.
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DR EMBL; NJDU01000023; OYT45577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A256YZC8; -.
DR Proteomes; UP000216196; 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 36..168
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01509"
SQ SEQUENCE 325 AA; 36807 MW; 54DC29A4C3C98B5A CRC64;
MSFEVWAEKY RPKRLDDIIN QKHIVARIKV FVEDRNIPHM LFAGPPGTGK TTMALCIARE
LYGDQWRQNV LETNASDERG IGVVRGKIKD FARTIAMGGA EYRMIILDEA DALTSEAQQA
LRRTMETYSA TVRFILICNY SSKIIPPIQS RTAVFRFRTL SEEDVRKFIG WIVQGENLEV
EEEAVKAIMH LCEGDLRRVA NLLQAAATLG SKITEEMIYE VASQARPQDV RRMLQLALNG
RFKDAREILY KMLVNQGLAG EDVVREIHRQ VYALDLPEEA KIRLVEAIGE YEFRISEGAD
ALIQLEALLA RFAAYGASAP PFRGL
//
