ID   RFCL_PYRAE              Reviewed;         422 AA.
AC   Q8ZYK3;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=PAE0735;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL62990.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZYK3; -.
DR   SMR; Q8ZYK3; -.
DR   STRING; 178306.PAE0735; -.
DR   PRIDE; Q8ZYK3; -.
DR   EnsemblBacteria; AAL62990; AAL62990; PAE0735.
DR   KEGG; pai:PAE0735; -.
DR   PATRIC; fig|178306.9.peg.535; -.
DR   eggNOG; arCOG00470; Archaea.
DR   HOGENOM; CLU_027255_1_1_2; -.
DR   InParanoid; Q8ZYK3; -.
DR   OMA; GGWTRYG; -.
DR   Proteomes; UP000002439; 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..422
FT                   /note="Replication factor C large subunit"
FT                   /id="PRO_0000135961"
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;  48133 MW;  633381A917A95716 CRC64;
     MALPWIEKYR PKSFAEIVNQ EEAKYTLASW ICLKFRAPKE FCTRWAKKRD KEVAEAKAIL
     LAGPPGVGKT TLVHALAREI RYELIELNAS DVRTADRLRQ VIGRGLRESS LFGFEGKMVL
     FDEVDGLHVK EDKGGLEEII EIIETAKIPI IMTANNPYDP KFRPLRDISL VVNLKRLSEE
     EVVEVLRRIC TSEGAKCEEE ALRSIAKSSM GDLRAAINDL QMYLSGGRRI LTLDDIKRVG
     ERNPQLSMFE ILDRVYKARW FDEARAVSFN PSFDWEQYFI WALESIPVVY KDLEIASTAY
     DRLSKADVFM GRIKRTQEWE LLPYALELAL GGVSQIKGKP RLPPFIKYGF PQRLLLLAKS
     KEARRRRDAL VEYLAQNLHA SKSVIKSEII YVLSALSKNN QSIIEKLSKA LGINAIDIKS
     VL