RFCL_METBF
ID RFCL_METBF Reviewed; 642 AA.
AC Q46AT6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Mbar_A2075;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ71006.1; -; Genomic_DNA.
DR RefSeq; WP_011307052.1; NC_007355.1.
DR AlphaFoldDB; Q46AT6; -.
DR SMR; Q46AT6; -.
DR STRING; 269797.Mbar_A2075; -.
DR EnsemblBacteria; AAZ71006; AAZ71006; Mbar_A2075.
DR GeneID; 3626469; -.
DR KEGG; mba:Mbar_A2075; -.
DR eggNOG; arCOG00470; Archaea.
DR HOGENOM; CLU_027255_0_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..642
FT /note="Replication factor C large subunit"
FT /id="PRO_0000245636"
FT REGION 432..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01508"
SQ SEQUENCE 642 AA; 71040 MW; 171E0DD22C301462 CRC64;
MTLAIEWAEK YRPQTLKEIV GNKKAVQYLR TWAEKWLSGI PDRRAVVLHG PAGVGKTSTA
HALARDLDWE VIELNASDQR TAGVIERVAG SAASMNTFFG GKRLIILDEA DNIHGTADRG
GMRAIAGIIK NTLQPIVLIA NDIYGLTPTI RNLCLEIKFG SVQSRSMVPA LKKVCESEDI
LCSPDAIQQI AEGAGGDLRS AINDLQAAAT GRKTLEVEDL STSGRDVKEN IFKAMQRIFK
STDCKKALEA ARGLDESPED LVHWIDENLP FQYASKDGNL EDIKTGFGYL SKADLYLGRV
KKRQNYRMWR YASMLMVCGT SVSKTRPYPG FIKYQPPSLW KKMGQIRSKR DLRDNIASKV
GEHNFESMRY SRNNLLELYS RMLKNEESAI EITAGLGLEL EELIYLSGST KASKKLQKIY
ERAQELLLEG NEESDGAEFF RTPAPPGNSK EDLSVFSVNN SVEKDGKHSE RLEVPNSRTS
QGGQKTLNFG FDIPPEISPE TKNSENNTSD TIKPGNLAPD ILAPVTLTPD SFTSDTLIPE
QDQAEIDDIG IKSDSLTSIS LEHDSLKVKN SSSLPGPVEK EAFSDSEPIE NSISPELSRS
VKSVNREPAI KKVSDNSEKS EVKVSETPKK VESKTQKTLF DF