RFCL_HALWD
ID RFCL_HALWD Reviewed; 516 AA.
AC Q18GQ9;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=HQ_2729A;
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001;
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA Pfeiffer F., Oesterhelt D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(2006).
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; AM180088; CAJ52837.1; -; Genomic_DNA.
DR RefSeq; WP_011571952.1; NC_008212.1.
DR AlphaFoldDB; Q18GQ9; -.
DR SMR; Q18GQ9; -.
DR STRING; 362976.HQ_2729A; -.
DR EnsemblBacteria; CAJ52837; CAJ52837; HQ_2729A.
DR GeneID; 4194576; -.
DR KEGG; hwa:HQ_2729A; -.
DR eggNOG; arCOG00470; Archaea.
DR HOGENOM; CLU_027255_1_0_2; -.
DR OMA; GGWTRYG; -.
DR Proteomes; UP000001975; 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..516
FT /note="Replication factor C large subunit"
FT /id="PRO_0000292179"
FT REGION 421..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..516
FT /note="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 516 AA; 56342 MW; 46D91A1FBC65CF37 CRC64;
MTDWTERYRP TTLSAVRGNN AARDEFIEWA ESWDDHHESV VLHGAPGVGK TSAAHALASD
MGWETVELNA SDQRTSDVIE RLAGRAAKNA TLAGAVSGTT STRQLIIMDE ADNIHYQYDR
GGKQAVTTLL KDANQPIVLI ANEYYDMSRG LRNAAQDIEF RDISARSIVP VLRNILRKEN
IEFEEAALKQ IAEVNSGDLR AAIKDLQTTV EGSDRITVDD VKTGGRDRAM GLFSFLDSVL
KEDAAEEALQ NSYDVDETPD DLLKWVEDKV PLVYDDAELA RAYEFLSNAD IWTNRVYATD
YNYRWWRYAT DNLAGGVAAA RETQRGGWTR YGGAPYRSTR DSTRDTVVRE VAKTGGFSMA
TARTAVIPFL SAITHLCKPR SLTVGMAAWY ELDEAGVSYI TGSGETTKKV ASIVEDAAER
RSEAVEAHAG SAFAETETEE KTNFTGNQDS DVDVQSHKSA ESGDDTVRTA NTPAEDHAQS
GASETASATE SASDSDASTD TDADDDDGQA GLSEFM