ID   RFC3_SCHPO              Reviewed;         342 AA.
AC   O14003; Q9P547;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 2.
DT   02-SEP-2026, entry version 170.
DE   RecName: Full=Replication factor C subunit 3;
DE            Short=Replication factor C3;
GN   Name=rfc3; ORFNames=SPAC27E2.10c, SPAPJ698.01c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND MUTAGENESIS OF
RP   ARG-216.
RX   PubMed=10588638; DOI=10.1091/mbc.10.12.3991;
RA   Shimada M., Okuzaki D., Tanaka S., Tougan T., Tamai K.K., Shimoda C.,
RA   Nojima H.;
RT   "Replication factor C3 of Schizosaccharomyces pombe, a small subunit of
RT   replication factor C complex, plays a role in both replication and damage
RT   checkpoints.";
RL   Mol. Biol. Cell 10:3991-4003(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10794172; DOI=10.1007/s002940050514;
RA   Gray F.C., MacNeill S.A.;
RT   "The Schizosaccharomyces pombe rfc3+ gene encodes a homologue of the human
RT   hRFC36 and Saccharomyces cerevisiae Rfc3 subunits of replication factor
RT   C.";
RL   Curr. Genet. 37:159-167(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [4]
RP   PROTEIN SEQUENCE OF 10-41; 56-69; 79-98; 115-141; 163-170; 176-204; 255-272
RP   AND 301-332, FUNCTION, AND SUBUNIT.
RX   PubMed=16040599; DOI=10.1093/nar/gki728;
RA   Kim J., Robertson K., Mylonas K.J.L., Gray F.C., Charapitsa I.,
RA   MacNeill S.A.;
RT   "Contrasting effects of Elg1-RFC and Ctf18-RFC inactivation in the absence
RT   of fully functional RFC in fission yeast.";
RL   Nucleic Acids Res. 33:4078-4089(2005).
CC   -!- FUNCTION: The elongation of primed DNA templates by DNA polymerase
CC       delta and epsilon requires the action of the accessory proteins PCNA
CC       and activator 1. Subunit 3 binds ATP. Also involved in replication and
CC       DNA damage checkpoint controls, probably functioning as a checkpoint
CC       sensor. {ECO:0000269|PubMed:10588638, ECO:0000269|PubMed:16040599}.
CC   -!- SUBUNIT: Heteropentamer of subunits rfc1, rfc2, rfc3, rfc4 and rfc5
CC       that forms a complex (RFC) with PCNA in the presence of ATP. Two other
CC       complexes exist where rfc1 can be replaced by either ctf18 or elg1 to
CC       form the ctf18-RFC or the elg1-RFC complexes respectively.
CC       {ECO:0000269|PubMed:16040599}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC       {ECO:0000305}.
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DR   EMBL; AB017039; BAA82745.1; -; Genomic_DNA.
DR   EMBL; AB017040; BAA82746.1; -; mRNA.
DR   EMBL; AJ012839; CAB38106.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB39134.2; -; Genomic_DNA.
DR   PIR; T43410; T43410.
DR   AlphaFoldDB; O14003; -.
DR   SMR; O14003; -.
DR   BioGRID; 277995; 9.
DR   ComplexPortal; CPX-26444; DNA replication factor C complex, rad17 variant.
DR   ComplexPortal; CPX-26445; DNA replication factor C complex, ctf18 variant.
DR   ComplexPortal; CPX-26452; DNA replication factor C complex, elg1 variant.
DR   ComplexPortal; CPX-546; DNA replication factor C complex, RFC1 variant.
DR   FunCoup; O14003; 727.
DR   STRING; 284812.O14003; -.
DR   PaxDb; 284812-O14003; -.
DR   PomBase; SPAC27E2.10c; rfc3.
DR   VEuPathDB; FungiDB:SPAC27E2.10c; -.
DR   eggNOG; KOG0990; Eukaryota.
DR   HOGENOM; CLU_042324_2_1_1; -.
DR   InParanoid; O14003; -.
DR   OMA; AEDNLPW; -.
DR   PhylomeDB; O14003; -.
DR   Reactome; R-SPO-110312; Translesion synthesis by REV1.
DR   Reactome; R-SPO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR   Reactome; R-SPO-110320; Translesion Synthesis by POLH.
DR   Reactome; R-SPO-176187; Activation of ATR in response to replication stress.
DR   Reactome; R-SPO-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR   Reactome; R-SPO-5655862; Translesion synthesis by POLK.
DR   Reactome; R-SPO-5656121; Translesion synthesis by POLI.
DR   Reactome; R-SPO-5656169; Termination of translesion DNA synthesis.
DR   Reactome; R-SPO-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR   Reactome; R-SPO-5696400; Dual Incision in GG-NER.
DR   Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR   Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-SPO-69091; Polymerase switching.
DR   PRO; PR:O14003; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; IC:PomBase.
DR   GO; GO:0031390; C:Ctf18 RFC-like complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005663; C:DNA replication factor C complex; IBA:GO_Central.
DR   GO; GO:0031391; C:Elg1 RFC-like complex; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0031389; C:Rad17 RFC-like complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; NAS:PomBase.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0061860; F:DNA clamp unloader activity; IC:PomBase.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0006260; P:DNA replication; NAS:ComplexPortal.
DR   GO; GO:0000076; P:DNA replication checkpoint signaling; NAS:ComplexPortal.
DR   GO; GO:1902983; P:DNA strand elongation involved in mitotic DNA replication; IDA:PomBase.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR   GO; GO:1903460; P:mitotic DNA replication leading strand elongation; ISO:PomBase.
DR   GO; GO:0070914; P:UV-damage excision repair; IDA:PomBase.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd18140; HLD_clamp_RFC; 1.
DR   FunFam; 1.10.8.60:FF:000028; Replication factor C subunit 5; 1.
DR   FunFam; 1.20.272.10:FF:000004; Replication factor C subunit 5; 1.
DR   FunFam; 3.40.50.300:FF:000129; Replication factor C subunit 5; 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; IPR050238; DNA_Rep/Repair_Clamp_Loader.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013748; Rep_factorC_C.
DR   InterPro; IPR047854; RFC_lid.
DR   NCBIfam; NF001679; PRK00440.1; 1.
DR   PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR   PANTHER; PTHR11669:SF9; REPLICATION FACTOR C SUBUNIT 5; 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   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; DNA damage; DNA replication;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..342
FT                   /note="Replication factor C subunit 3"
FT                   /id="PRO_0000121755"
FT   BINDING         63..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         216
FT                   /note="R->W: Defective DNA replication."
FT                   /evidence="ECO:0000269|PubMed:10588638"
SQ   SEQUENCE   342 AA;  38440 MW;  FA179E0C9F3C6F96 CRC64;
     MSIEKGKGRA MDIDLPLGSE STLPWVEKYR PANLEDVVSH KDIISTLEKF ISSNRVPHML
     FYGPPGTGKT STILACARKI YGPNYRNQLM ELNASDDRGI DAVREQIKNF ASTRQIFAST
     FKMIILDEAD AMTLAAQNAL RRVIEKYTKN VRFCIICNYI NKISPAIQSR CTRFRFQPLP
     PKEIEKTVDH VIQSEHCNID PDAKMAVLRL SKGDMRKALN ILQACHAAYD HIDVSAIYNC
     VGHPHPSDID YFLKSIMNDE FVIAFNTISS IKQQKGLALQ DILTCIFEAL DELEIKPNAK
     IFILDQLATI EHRMSFGCSE KIQLSAMIAS IKTGVDLAAK VN
//