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Database: UniProt
Entry: RFCS4_MIMIV
LinkDB: RFCS4_MIMIV
Original site: RFCS4_MIMIV 
ID   RFCS4_MIMIV             Reviewed;         363 AA.
AC   Q5UQ72;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Putative replication factor C small subunit L510;
DE            Short=RFC small subunit L510;
DE   AltName: Full=Clamp loader small subunit L510;
GN   OrderedLocusNames=MIMI_R510;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Megamimivirinae; Mimivirus;
OC   Mimivirus bradfordmassiliense.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
CC   -!- FUNCTION: Part of the RFC clamp loader complex which loads the PCNA
CC       sliding clamp onto DNA. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family. RfcS
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY653733; AAV50774.1; -; Genomic_DNA.
DR   RefSeq; YP_003987022.1; NC_014649.1.
DR   SMR; Q5UQ72; -.
DR   GeneID; 9925141; -.
DR   KEGG; vg:9925141; -.
DR   OrthoDB; 6135at10239; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:UniProtKB-KW.
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; DNA replication; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..363
FT                   /note="Putative replication factor C small subunit L510"
FT                   /id="PRO_0000244641"
FT   BINDING         47..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   363 AA;  41602 MW;  506C99EF9DF27C7C CRC64;
     MIDDESVPWI EKYRPKKLED ITQSQNLLDL FKNSTKKGEM THFLFYGPPG TGKTSAILAM
     GREIFKEHFQ NRVIEFNASD DRGINAVREK ITNEAKKYVA EIKLEDGTII PSYKIIILDE
     ADSMTDEAQD ALRVIIEQYS TATRFCFICN YITKITDAIK SRCSSVYFKK LSDECMVEKL
     NDISLKESME LPKNILHTII DVSNGDMRKA IMLLQNFKYT YNFKKNLTKK LKDMTLLELK
     TILFMTKKSS ITSTISEEDV YEISASITLD KAKGIIDDTI DCNNIVEVSN LSKKIIAMGF
     PIDNILTQLN KCILESNKLD VNQISKIIIY SGDILLKMKE CGNEYIQLLN YLAYVNRVSK
     HFD
//
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