RFCL_PYRNV
ID RFCL_PYRNV Reviewed; 422 AA.
AC B1YC69;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=Tneu_2009;
OS Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 /
OS V24Sta) (Thermoproteus neutrophilus).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=444157;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA Saltikov C., House C.H., Richardson P.;
RT "Complete sequence of Thermoproteus neutrophilus V24Sta.";
RL Submitted (MAR-2008) 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; CP001014; ACB40923.1; -; Genomic_DNA.
DR AlphaFoldDB; B1YC69; -.
DR SMR; B1YC69; -.
DR STRING; 444157.Tneu_2009; -.
DR EnsemblBacteria; ACB40923; ACB40923; Tneu_2009.
DR KEGG; tne:Tneu_2009; -.
DR eggNOG; arCOG00470; Archaea.
DR HOGENOM; CLU_027255_1_1_2; -.
DR OMA; GGWTRYG; -.
DR Proteomes; UP000001694; 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.
FT CHAIN 1..422
FT /note="Replication factor C large subunit"
FT /id="PRO_1000195422"
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; 47984 MW; C9C0516C9694EBC0 CRC64;
MGIPWVEKYR PKAFSEIVNQ EEAKTLLASW ICARFRAPKE FCARWAKKRE KEVAEAKAVL
LAGPPGIGKT TVVHALAREI RYELIELNAS DIRTGERIKL VVGRGLKESS LFGYEGKLVL
FDEVDGLHVK EDEGGLEAIV EIVETAKVPI VMTANNPYDP KFRPLRDISL VVNLKRLSEE
EVVEVLRRIC TAEGAKCEEE ALRSIAKSSL GDLRAAINDL QMYLSGGRKT LTVDDIKRVG
ERNPQLSMFE VLDRVYRARW FDEARAVSFN PSFDWEQYFL WALETVPVVY KDVETAAAAY
DRLSKADMFL GRIKRMQEWE LLPYALELAL GGVSQVKNKP RLPPFIKYGF PQRLLLLAKS
REARRRREAL VEYLAQNLHI SRSLARSDII YVLSALARRD PKVVERLSRA LGINAIDVKN
LL