ID   RFC4_ENCCU              Reviewed;         309 AA.
AC   Q8SQM0;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Replication factor C subunit 4;
DE            Short=Replication factor C4;
GN   Name=RFC4; OrderedLocusNames=ECU09_1330;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- FUNCTION: Component of ATP-dependent clamp loader (RFC and RFC-like)
CC       complexes for DNA clamps. During a clamp loading circle, the RFC:clamp
CC       complex binds to DNA and the recognition of the double-stranded/single-
CC       stranded junction stimulates ATP hydrolysis by RFC. The complex
CC       presumably provides bipartite ATP sites in which one subunit supplies a
CC       catalytic site for hydrolysis of ATP bound to the neighboring subunit.
CC       Dissociation of RFC from the clamp leaves the clamp encircling DNA.
CC       Component of the replication factor C (RFC or activator 1) complex
CC       which acts during elongation of primed DNA templates by DNA polymerase
CC       delta and epsilon. RFC has an essential but redundant activity in
CC       sister chromatid cohesion establishment (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the replication factor C (RFC) complex.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- MISCELLANEOUS: Present with 2760 molecules/cell in log phase SD medium.
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC       {ECO:0000305}.
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DR   EMBL; AL590451; CAD27104.1; -; Genomic_DNA.
DR   RefSeq; XP_955685.1; XM_950592.1.
DR   AlphaFoldDB; Q8SQM0; -.
DR   SMR; Q8SQM0; -.
DR   STRING; 284813.Q8SQM0; -.
DR   PRIDE; Q8SQM0; -.
DR   GeneID; 860470; -.
DR   KEGG; ecu:ECU09_1330; -.
DR   VEuPathDB; MicrosporidiaDB:ECU09_1330; -.
DR   HOGENOM; CLU_042324_0_1_1; -.
DR   InParanoid; Q8SQM0; -.
DR   OMA; TQIYGFV; -.
DR   OrthoDB; 1071197at2759; -.
DR   Proteomes; UP000000819; Chromosome IX.
DR   GO; GO:0031391; C:Elg1 RFC-like complex; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0090618; P:DNA clamp unloading; IEA:UniProt.
DR   GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:UniProt.
DR   Gene3D; 3.40.50.300; -; 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   Pfam; PF00004; AAA; 1.
DR   Pfam; PF08542; Rep_fac_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF48019; SSF48019; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; DNA replication; DNA-binding; Nucleotide-binding;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..309
FT                   /note="Replication factor C subunit 4"
FT                   /id="PRO_0000381755"
FT   BINDING         5
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         42..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   309 AA;  35310 MW;  4E9227F7D5D7C293 CRC64;
     MDLLVNKYQP SEIQDIVGNE ATMELVSLMI ESRDMPHLLF TGPPGTGKTT CAKILARRLL
     GNKEGLLELN ASDERGIDTV RTTIKSFAQR RVKDCEFKII ILDEADSMTT TAQQAMRRVM
     EIHSSECRFI LICNVFTKIF EPIQSRCAIL RFDRIEQSVI LKRLKEISEG EGIRITAEAL
     DLVVELSDGD MRQSLNILQA CINSPGTVDQ DYIIKIIGLP SPKRIEKVLQ RLLKREVEEA
     LEMFDEIWEE KFDPLDLINS FFRAAKNMES YELLKVIGLA NLRISEGVNS RLQFYGMFWD
     ILDMGSKRL