RFCL_NATPD
ID RFCL_NATPD Reviewed; 483 AA.
AC Q3ISA5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
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}; Synonyms=rfcB;
GN OrderedLocusNames=NP_1782A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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; CR936257; CAI48982.1; -; Genomic_DNA.
DR RefSeq; WP_011322615.1; NC_007426.1.
DR AlphaFoldDB; Q3ISA5; -.
DR SMR; Q3ISA5; -.
DR STRING; 348780.NP_1782A; -.
DR EnsemblBacteria; CAI48982; CAI48982; NP_1782A.
DR GeneID; 3703101; -.
DR KEGG; nph:NP_1782A; -.
DR eggNOG; arCOG00470; Archaea.
DR HOGENOM; CLU_027255_1_0_2; -.
DR OMA; GGWTRYG; -.
DR OrthoDB; 24257at2157; -.
DR Proteomes; UP000002698; 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..483
FT /note="Replication factor C large subunit"
FT /id="PRO_0000135958"
FT REGION 415..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..446
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01508"
SQ SEQUENCE 483 AA; 53153 MW; 1B9659185F183982 CRC64;
MSDWTEAYRP TTLSEVRGNN KARDAFEEWA KAWEDHREAV ILHGSPGVGK TSAAHALAND
MGWPVLEMNA SDARTKDEIE RFAGRAASNA TLGGGRQLII LDEADNLHQH KDRGGAAAMT
RLVKDATQPV VLIANDYYEM SSGLRSACRD VEFRDVSARS IVPVLRDICR QENVEFDEDV
LQEIAEANRG DLRGAVKDLQ ARERDGEIKP EGSEGSRDRT EDIFAFLDAV LKEESAEEAL
QTAYAVDETP DNLLQWIEDK VPKVYEGDEL ADAYEHLADA DVWLGRVRAT QNYSYWRYAT
DNVAAGVAAV RQEDRGGWTR YGGAPYRSSR DSTRDYIATR IAESAGVSTA TARREILPYL
SAMTHHCNNR ELTVRMTARY ELDAEHVAFI TGSGKTTNKV QGIVEDAETR RETAAVDHGG
GIFAPAVDDA QSDTESDDDD DGDTLAAFGA DEPKEESVNR EQSDGTADAE ESDDGQAGLS
DFM
