ID   RFCL_PYRAR              Reviewed;         422 AA.
AC   A4WGV3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=Pars_0003;
OS   Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=340102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700994 / DSM 13514 / JCM 11321 / PZ6;
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 arsenaticum DSM 13514.";
RL   Submitted (APR-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; CP000660; ABP49620.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WGV3; -.
DR   SMR; A4WGV3; -.
DR   STRING; 340102.Pars_0003; -.
DR   EnsemblBacteria; ABP49620; ABP49620; Pars_0003.
DR   KEGG; pas:Pars_0003; -.
DR   HOGENOM; CLU_027255_1_1_2; -.
DR   OMA; GGWTRYG; -.
DR   PhylomeDB; A4WGV3; -.
DR   Proteomes; UP000001567; 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..422
FT                   /note="Replication factor C large subunit"
FT                   /id="PRO_0000300155"
FT   BINDING         63..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01508"
SQ   SEQUENCE   422 AA;  47996 MW;  B4A0D2A7EA456FB3 CRC64;
     MALPWVEKYR PKSFADVVDQ EEAKYVLASW ICARFRAPKD FCTRWAKKKD KEILDARAVL
     LAGPPGVGKT TLIHALAREI GYELIELNAS DVRTAERLKE VVGRGLREGS LFGYGGKIVL
     FDEVDGLHVK EDAGGLEAII EIIENSKVPI VMTANNPYDP RFRPLRDISL VVNLKRLSEE
     EVVEVLRRIC TSEGAKCEEE ALRSIAKSSL GDLRAAINDL QMYLSGGRKT LTVDDIKRVG
     ERNPQLSMFE ILDRVYRARW FDEARAISFN PSFDWEQYFI WATETIPVVY KEIETMSVAY
     DRLSKADMFI GRIKRTQEWE LLPYALELAL GGVSQIKSKP RLPPFIKYGF PQRLLILAKS
     REARKRRDVL VEYLAQNLHV SRSYVKSEII YVLGVLAKSD SKIVERLSKA LGINAIDIKT
     LL