GenomeNet

Database: UniProt
Entry: L0IA92_HALRX
LinkDB: L0IA92_HALRX
Original site: L0IA92_HALRX 
ID   L0IA92_HALRX            Unreviewed;       334 AA.
AC   L0IA92;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Replication factor C small subunit {ECO:0000256|ARBA:ARBA00014164};
DE   AltName: Full=Clamp loader small subunit {ECO:0000256|ARBA:ARBA00031749};
GN   OrderedLocusNames=Halru_0528 {ECO:0000313|EMBL:AGB15161.1};
OS   Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Halovivax.
OX   NCBI_TaxID=797302 {ECO:0000313|EMBL:AGB15161.1, ECO:0000313|Proteomes:UP000010846};
RN   [1] {ECO:0000313|Proteomes:UP000010846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18193 / JCM 13892 / XH-70
RC   {ECO:0000313|Proteomes:UP000010846};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA   Anderson I., Woyke T.;
RT   "Complete sequence of Halovivax ruber XH-70.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family. RfcS
CC       subfamily. {ECO:0000256|ARBA:ARBA00009668}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003050; AGB15161.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0IA92; -.
DR   STRING; 797302.Halru_0528; -.
DR   KEGG; hru:Halru_0528; -.
DR   eggNOG; arCOG00469; Archaea.
DR   HOGENOM; CLU_042324_2_1_2; -.
DR   OrthoDB; 301951at2157; -.
DR   Proteomes; UP000010846; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd18140; HLD_clamp_RFC; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013748; Rep_factorC_C.
DR   InterPro; IPR047854; RFC_lid.
DR   PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR   PANTHER; PTHR11669:SF5; REPLICATION FACTOR C SUBUNIT 2; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF08542; Rep_fac_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010846}.
FT   DOMAIN          32..181
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   334 AA;  36793 MW;  9569C6BD38195E3C CRC64;
     MDAPLWTEAY APTLAELPQD DARETLGQTV EEPLNLILQG PPGSGKTASA RALARETHDN
     PDSDLIEINV ADFFGRTKTE IKNDPRFEGF LVGRSDMSKR DMINHVLKES ASYAPVAGDH
     KTLLLDNAEA VREDFQQALR RIMEQHHRTT RFIVTTRQPT KLIPPIRSRC FPVTMRAPTS
     EEIVSVLEPI VEAEGVEYDA DGLEFVAGYA GGNLREAILA AQTTAVDAGE ITMSAAYEVL
     GEVGLDDEID GMLDDAEAGA FTDARKTLDD LLVDEGLDGQ EVLDAILEQG RKRYQGERLA
     ELHRLVADIE FDMQEGTSDR IHVSHLLAEL GRKA
//
DBGET integrated database retrieval system