ID   RFCL_METM7              Reviewed;         482 AA.
AC   A6VIW1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=MmarC7_1324;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-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; CP000745; ABR66387.1; -; Genomic_DNA.
DR   RefSeq; WP_012067854.1; NC_009637.1.
DR   AlphaFoldDB; A6VIW1; -.
DR   SMR; A6VIW1; -.
DR   STRING; 426368.MmarC7_1324; -.
DR   EnsemblBacteria; ABR66387; ABR66387; MmarC7_1324.
DR   GeneID; 5328527; -.
DR   KEGG; mmz:MmarC7_1324; -.
DR   eggNOG; arCOG00470; Archaea.
DR   HOGENOM; CLU_027255_1_0_2; -.
DR   OMA; GGWTRYG; -.
DR   OrthoDB; 24257at2157; -.
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..482
FT                   /note="Replication factor C large subunit"
FT                   /id="PRO_0000318541"
FT   REGION          420..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..476
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|HAMAP-Rule:MF_01508"
SQ   SEQUENCE   482 AA;  54080 MW;  F138936C97B97609 CRC64;
     MEEWVEKYRP KSLNDVAGHN KTKESLIEWI ESFINGQKQK PILLAGPPGS GKTTLAYAIA
     KDYAFDVIEL NASDKRNKDV ISQVVGTAAT SKSLTGKRTL IVLDEVDGLS GNDDRGGVAE
     IIKVLKTAEN PVILTANDVY KPALMTLRNS VNLINVGSVH TNSIPPVLRK IALKEGFEID
     EKVIKTIASH AGGDLRAAIN DLQSLATGGS IEVEDAKELP DRDSEKSIFD AMRIIMKTTH
     YDIATSATRD VKEELGTIEE WISENLPKEY LKYKDLANGY DYLSKSDVFL GRVFRRQYFG
     LWRYASALMT AGTALAKEEK YRGFTRYAPP AIFTKLSRTK GSRQRMKDIL KKIALKTHTS
     TKRARNTLDY MVVVFESNEA VSAELVEYYE LTKEEIEFLT NKTIAKNIFS VIAGKKPKVE
     KETPKKKKKA EDVVPIIPKR PKISEPPKEP LKEVIEETVE KTDKKEKEKK DPKKQATLDS
     FF