ID   RFCL_PYRCJ              Reviewed;         421 AA.
AC   A3MS27;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=Pcal_0004;
OS   Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=410359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21063 / JCM 11548 / VA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL   Submitted (FEB-2007) 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: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}.
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DR   EMBL; CP000561; ABO07444.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3MS27; -.
DR   SMR; A3MS27; -.
DR   STRING; 410359.Pcal_0004; -.
DR   EnsemblBacteria; ABO07444; ABO07444; Pcal_0004.
DR   KEGG; pcl:Pcal_0004; -.
DR   eggNOG; arCOG00470; Archaea.
DR   HOGENOM; CLU_027255_1_1_2; -.
DR   OMA; GGWTRYG; -.
DR   Proteomes; UP000001431; Chromosome.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR023935; Rep_factor-C_lsu.
DR   Pfam; PF00004; AAA; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA replication; Nucleotide-binding.
FT   CHAIN           1..421
FT                   /note="Replication factor C large subunit"
FT                   /id="PRO_0000300156"
FT   BINDING         63..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01508"
SQ   SEQUENCE   421 AA;  47937 MW;  BBAE8C7B89EE061C CRC64;
     MPIPWVEKYR PKSFSEIVNQ EEAKQILASW ICTRFKAPQE FCARWAKRRD KEIKEARAVL
     LWGPPGIGKT TLVHALAKEI GYELVELNAS DVRTGERIRQ VVGRGLREAS LFGYAGKIVL
     FDEVDGLHVK EDLGGLEAIL NLIETAKVPI VLTANNPFDP KLRPLRDISL VVGLKRLSED
     EVVEVLKRIC ASEGAKCEEE ALRSLAKSSY GDLRAAINDL QLYLAGRKVL TVDDIKRAGE
     RNPQLSMFEI LDRVYKARWF DEARAVSFNP SFDWEQYFVW ALETIPIVYK DLEVMSEAFD
     RLSKADMFIG IVKRTQEWEL LSYAMELALG GVSQVKNKPR LPPFIRYGFP QRLLLLAKSK
     EARRRREMVV EYLARNLHVS KGLVNAEIFY VLSALAKKDD HVVERLARAL GISPIDIKNL
     L