ID   RFCL_METJA              Reviewed;         516 AA.
AC   Q58294;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Replication factor C large subunit;
DE            Short=RFC large subunit;
DE   AltName: Full=Clamp loader large subunit;
GN   Name=rfcL; OrderedLocusNames=MJ0884;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   CRYSTALLIZATION.
RX   PubMed=11856841; DOI=10.1107/s090744490102159x;
RA   Lee I., Lokanath N.K., Min K., Ha S.C., Kim D.Y., Kim K.K.;
RT   "Cloning, purification, crystallization and preliminary X-ray studies of
RT   RFC boxes II-VIII of replication factor C from Methanococcus jannaschii.";
RL   Acta Crystallogr. D 58:519-521(2002).
CC   -!- FUNCTION: Part of the RFC clamp loader complex which loads the PCNA
CC       sliding clamp onto DNA. {ECO:0000250}.
CC   -!- SUBUNIT: Heteromultimer composed of small subunits (RfcS) and large
CC       subunits (RfcL). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family. RfcL
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L77117; AAB98888.1; -; Genomic_DNA.
DR   PIR; D64410; D64410.
DR   RefSeq; WP_010870398.1; NC_000909.1.
DR   AlphaFoldDB; Q58294; -.
DR   SMR; Q58294; -.
DR   STRING; 243232.MJ_0884; -.
DR   PRIDE; Q58294; -.
DR   EnsemblBacteria; AAB98888; AAB98888; MJ_0884.
DR   GeneID; 1451773; -.
DR   KEGG; mja:MJ_0884; -.
DR   eggNOG; arCOG00470; Archaea.
DR   HOGENOM; CLU_027255_1_1_2; -.
DR   InParanoid; Q58294; -.
DR   OMA; GGWTRYG; -.
DR   OrthoDB; 24257at2157; -.
DR   PhylomeDB; Q58294; -.
DR   Proteomes; UP000000805; 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   1: Evidence at protein level;
KW   ATP-binding; DNA replication; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..516
FT                   /note="Replication factor C large subunit"
FT                   /id="PRO_0000135952"
FT   REGION          422..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..445
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..494
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         46..53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   516 AA;  58770 MW;  800BF6A70560859E CRC64;
     MLSWVEKYRP KSLKDVAGHE KVKEKLKTWI ESYLKGETPK PILLVGPPGC GKTTLAYALA
     NDYGFEVIEL NASDKRNSSA IKKVVGHAAT SSSIFGKKFL IVLDEVDGIS GKEDAGGVSE
     LIKVIKKAKN PIILTANDAY APSIRSLLPY VEVIQLNPVH TNSVYKVLKK IAEKEGLDVD
     DKTLKMIAQH SAGDLRSAIN DLEALALSGD LSYEAAQKLP DRKREANIFD ALRVILKTTH
     YGIATTALMN VDETPDVVIE WIAENVPKEY EKPEEVARAF EYLSKADRYL GRVMRRQNYS
     FWKYATTLMT AGVALSKDEK YRKWTPYSYP KIFRLLTKTK AEREILNKIL KKIGEKTHTS
     SKRARFDLQM LKLLAKENPS VAADLVDYFE IKEDELKVLV GDKLASEILK ILKEKKKLER
     KKKKEKEKLE KEKKKEEKAK EKQSNLIIQP KEIKEEVKAE VEKKEEVKEK IVEKPKAEEV
     KEKSKTEEKE TKKDKKKGKK KKEDKGKQLT LDAFFK