RFCL_HALMA
ID RFCL_HALMA Reviewed; 508 AA.
AC Q5V1F7;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=rrnAC1744;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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; AY596297; AAV46645.1; -; Genomic_DNA.
DR RefSeq; WP_011223815.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V1F7; -.
DR SMR; Q5V1F7; -.
DR STRING; 272569.rrnAC1744; -.
DR EnsemblBacteria; AAV46645; AAV46645; rrnAC1744.
DR GeneID; 40152700; -.
DR KEGG; hma:rrnAC1744; -.
DR PATRIC; fig|272569.17.peg.2424; -.
DR eggNOG; arCOG00470; Archaea.
DR HOGENOM; CLU_027255_1_1_2; -.
DR OMA; GGWTRYG; -.
DR Proteomes; UP000001169; Chromosome I.
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..508
FT /note="Replication factor C large subunit"
FT /id="PRO_0000135949"
FT REGION 425..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..500
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01508"
SQ SEQUENCE 508 AA; 55200 MW; 305372E783FC1DFD CRC64;
MDWTEKYRPT TLSEVRGNDK ARDALKKWAE TWDDHREAVI LYGSPGIGKT SAAHALANDM
EWPTIELNAS DSRTKDVINR VAGEAAKSGT LTAGGGGRRL VIMDEADNIH GNADRGGARA
ITALVKEASQ PMILIANEYY EMSNGLRNNC QDIEFRDVSP RSIVPVLRDL CRQEGVEYES
DALQELAEQN SGGLRGAVKD LQAIAETTER LTADDVVTGE RDTTEGIFEY LDVVLKEAGA
QDALEASYDV DETPDDLINW IEDNMPKDYE GTELVRAYEF LSNADQWLGR VRETQNYSFW
RYAGDNMTAG VAAARDGTKG GWTRYGPPSY WSKLGRSKGT RNTRDYVAQQ IAAIDGVSMR
TARREIMPFL ATMTHHCRNR ELTVAMAATY DMEAEHVSFV TGSGKDTNKV QDIVADAEAL
KEEAAVEHSG GVFEGASANG GDGDSDADGD APDTDAGEES GDQQVTLAAD DGAESDATSD
GTTTDDETET ASEAAEDDDQ QSGLSDFM
