RFCL_SULAC
ID RFCL_SULAC Reviewed; 437 AA.
AC Q4JAB1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Saci_0906;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(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; CP000077; AAY80269.1; -; Genomic_DNA.
DR RefSeq; WP_011277771.1; NC_007181.1.
DR AlphaFoldDB; Q4JAB1; -.
DR SMR; Q4JAB1; -.
DR STRING; 330779.Saci_0906; -.
DR PRIDE; Q4JAB1; -.
DR EnsemblBacteria; AAY80269; AAY80269; Saci_0906.
DR GeneID; 3473017; -.
DR KEGG; sai:Saci_0906; -.
DR PATRIC; fig|330779.12.peg.866; -.
DR eggNOG; arCOG00470; Archaea.
DR HOGENOM; CLU_027255_1_1_2; -.
DR OMA; GGWTRYG; -.
DR Proteomes; UP000001018; 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..437
FT /note="Replication factor C large subunit"
FT /id="PRO_0000135965"
FT REGION 410..437
FT /note="Disordered"
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 437 AA; 50532 MW; 9A9423AAFDFD3DFC CRC64;
MPLQWFLKYR PKSLQEVENQ DEVKEELKKW IESWLNGEPT AKAVLLYGPP GVGKTTLAEA
LARDYKLELL EMNASDSRNL RDIKDVAERA SISGSLFGIK GKIILLDEID GIYSRADAGA
IPAILELIEK TKYPVILTAN DPWDPSLRSL RNAVKMIELK RLGKYPLKRL LKRICEKEKI
VCIDEALDHI IEQSEGDARY CINMLQGIAE GYGKVTLDNV KELVRRKDRE LDPFETLRDV
FWAKYYWQAK NAVTNSQVDY ELLMRWFDEN IPLQYTSMED VWRAYEALSR ASVFLTRAKQ
VGWDLLSYVF DLMGPGIAFA SLEKKKPGYK ARWVKYQFPQ YIQALARTKE KRDSIETLLK
KIGEKTHTSK RKVLNDTLPF LASYYTRHAE AVENYLQLTE GEKEILNVFT QASKPTSEEK
AEKSKKYYPK RSSSRKT
