RFCL_METKA
ID RFCL_METKA Reviewed; 510 AA.
AC Q8TZC5;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=MK0005;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(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; AE009439; AAM01222.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TZC5; -.
DR SMR; Q8TZC5; -.
DR STRING; 190192.MK0005; -.
DR PRIDE; Q8TZC5; -.
DR EnsemblBacteria; AAM01222; AAM01222; MK0005.
DR KEGG; mka:MK0005; -.
DR PATRIC; fig|190192.8.peg.5; -.
DR HOGENOM; CLU_027255_1_1_2; -.
DR OMA; GGWTRYG; -.
DR Proteomes; UP000001826; 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; Reference proteome.
FT CHAIN 1..510
FT /note="Replication factor C large subunit"
FT /id="PRO_0000135953"
FT REGION 459..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..488
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01508"
SQ SEQUENCE 510 AA; 58255 MW; E3676E6348A8DED2 CRC64;
MVPWVEKYRP RSLKELVNQD EAKKELAAWA NEWARGSIPE PRAVLLHGPP GTGKTSAAYA
LAHDFGWDVI ELNASDKRTR NVIEKIVGGA STSRSLLRMT REAGGDYEHV EGHSDRVLVL
VDEVDGIDPR EDRGGVTALT RAVRQARNPM VLVANDPWVL PKSLRDAVRM IEFRRLRVND
IVEALRRICE REGIEYEEVA LRRIAKRARG DLRAAINDLE ALARPTGRVT SDDVEALGWR
DKEITIFEAL GRIFNKPPRQ ARRALWNLDE DPDDVILWIA QNIPRAYRDP EEIARAYDYL
SKADVFSSRA IETGDWRFKY VYATDLMTSG VAAARKGKPP GFVRFQPPKI LRKLGTTRKE
REVRNSIAKK IAERMHVSTR RAKMDVISVL EIAFRKVADN PTDRGLEILG GIAGYLELSK
REIGFLCGDP QVAQRVYQRA LRVREKLRKI RRERVKGAME SMLERKREES EVEEEAKEIE
EAVEKAEEEE EREEKKKEGG GEQRTLDAFF