RFCL_HYPBU
ID RFCL_HYPBU Reviewed; 484 AA.
AC A2BL93;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Replication factor C large subunit {ECO:0000255|HAMAP-Rule:MF_01508};
DE Short=RFC large subunit {ECO:0000255|HAMAP-Rule:MF_01508};
DE AltName: Full=Clamp loader large subunit {ECO:0000255|HAMAP-Rule:MF_01508};
GN Name=rfcL {ECO:0000255|HAMAP-Rule:MF_01508}; OrderedLocusNames=Hbut_0906;
OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Hyperthermus.
OX NCBI_TaxID=415426;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX PubMed=17350933; DOI=10.1155/2007/745987;
RA Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA She Q., Garrett R.A., Klenk H.-P.;
RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL Archaea 2:127-135(2007).
CC -!- FUNCTION: Part of the RFC clamp loader complex which loads the PCNA
CC sliding clamp onto DNA. {ECO:0000255|HAMAP-Rule:MF_01508}.
CC -!- SUBUNIT: Heteromultimer composed of small subunits (RfcS) and large
CC subunits (RfcL). {ECO:0000255|HAMAP-Rule:MF_01508}.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family. RfcL
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01508}.
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; CP000493; ABM80754.1; -; Genomic_DNA.
DR RefSeq; WP_011822072.1; NC_008818.1.
DR AlphaFoldDB; A2BL93; -.
DR SMR; A2BL93; -.
DR STRING; 415426.Hbut_0906; -.
DR EnsemblBacteria; ABM80754; ABM80754; Hbut_0906.
DR GeneID; 4782052; -.
DR KEGG; hbu:Hbut_0906; -.
DR eggNOG; arCOG00470; Archaea.
DR HOGENOM; CLU_027255_1_1_2; -.
DR OMA; GGWTRYG; -.
DR OrthoDB; 24257at2157; -.
DR Proteomes; UP000002593; 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:0003689; F:DNA clamp loader activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01508; RfcL; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR013725; DNA_replication_fac_RFC1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR023935; Rep_factor-C_lsu.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08519; RFC1; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; Nucleotide-binding; Reference proteome.
FT CHAIN 1..484
FT /note="Replication factor C large subunit"
FT /id="PRO_0000292180"
FT REGION 435..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..473
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01508"
SQ SEQUENCE 484 AA; 55156 MW; 74DE8D7EB29BF389 CRC64;
MSDKLPWIIK YRPKRVEDVV DQEEAKKLFL PWLRSWLQGR IPERKAALFY GPAGVGKTSL
VEAAANEYGL ELIEMNASDF RRKSDIERIA KIAATQFSLF GRKRKIILLD EVDGISGTAD
RGGLDAILEL INITKHPIVM TANDPWDQKL KPLRDASLMV PFYRLSERYV VQVLKRICAA
ENIECEDEAL KLIAQRAEGD LRSAINDLQA IAEGYGVVRV DLVRALLATR DRQYSPWEML
RNLFMSKYIW QAKRAVTHTD LDYDTLLQWI NENIAVQYTH PEDIWRAHEA LARADIFLGR
IKRSLSWDLL PYVFDLVGPG VALARKKSKF KWAKYQFPQK ILMLAKTKEV REIREAVAEV
FAKRLHTSKA TVKREVLPFL FIIFRERPDY AARIAIGYNL TDNMIKYLAG PLASKVKEHM
NALLMRLEKP ATVSTATTAT TARTTAAETS VAASRAAKRT STSRRRTSKS RRRGKGSGTQ
TTLF