ID B8D4I4_DESA1 Unreviewed; 326 AA.
AC B8D4I4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
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 OrderedLocusNames=DKAM_0689 {ECO:0000313|EMBL:ACL11015.1};
OS Desulfurococcus amylolyticus (strain DSM 18924 / JCM 16383 / VKM B-2413 /
OS 1221n) (Desulfurococcus kamchatkensis).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Desulfurococcus.
OX NCBI_TaxID=490899 {ECO:0000313|EMBL:ACL11015.1, ECO:0000313|Proteomes:UP000006903};
RN [1] {ECO:0000313|EMBL:ACL11015.1, ECO:0000313|Proteomes:UP000006903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18924 / JCM 16383 / VKM B-2413 / 1221n
RC {ECO:0000313|Proteomes:UP000006903};
RX PubMed=19114480; DOI=10.1128/JB.01525-08;
RA Ravin N.V., Mardanov A.V., Beletsky A.V., Kublanov I.V., Kolganova T.V.,
RA Lebedinsky A.V., Chernyh N.A., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Complete genome sequence of the anaerobic, protein-degrading
RT hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis.";
RL J. Bacteriol. 191:2371-2379(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001140; ACL11015.1; -; Genomic_DNA.
DR RefSeq; WP_012608356.1; NC_011766.1.
DR AlphaFoldDB; B8D4I4; -.
DR STRING; 490899.DKAM_0689; -.
DR GeneID; 7170868; -.
DR KEGG; dka:DKAM_0689; -.
DR eggNOG; arCOG00469; Archaea.
DR HOGENOM; CLU_042324_2_1_2; -.
DR Proteomes; UP000006903; 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 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; IPR000641; CbxX/CfxQ.
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 PRINTS; PR00819; CBXCFQXSUPER.
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 39..170
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01509"
SQ SEQUENCE 326 AA; 37059 MW; 2498B26464EF479B CRC64;
MSEEVELLWA EKYRPRTLDE VVNQKEVVVR LKKFVEEKNI PHMLFAGPPG TGKTTIAHCL
AHDLYGDDYR KYMLELNASD ERKIEVIRGK VKEFARTRVV GDVPFKIVLL DEADNMTADA
QQALRRLMEL YSATTRFILT ANYPSKIIEP IQSRTAIFRF SPLSREDVVG RLKYICNAEK
IECAEKALET IYELSEGDMR RAINILQTAA ALGEVVEEAV YKVLGMAHPR EVREMINTAL
AGNFTEARNK LRTLMIEYGL SGLDIVKQIH REIFSQDVKI PDEIRVLIAD LAGEIQFRLV
EGADDEIQLN AFLARLALIG KKFKTG
//
