RFC1_SCHPO
ID RFC1_SCHPO Reviewed; 934 AA.
AC O60182; Q9US97;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Replication factor C subunit 1;
DE Short=Replication factor C1;
GN Name=rfc1; ORFNames=SPBC23E6.07c;
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], AND INTERACTION WITH CDC24.
RX PubMed=9891039; DOI=10.1128/mcb.19.2.1038;
RA Tanaka H., Tanaka K., Murakami H., Okayama H.;
RT "Fission yeast cdc24 is a replication factor C- and proliferating cell
RT nuclear antigen-interacting factor essential for S-phase completion.";
RL Mol. Cell. Biol. 19:1038-1048(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 461-645, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP FUNCTION.
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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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 1 is essential for cell cycle progression. It
CC may associate with components of the DNA replication machinery and
CC serve to enhance the efficiency of DNA replication.
CC {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. Interacts
CC with cdc24. {ECO:0000269|PubMed:9891039}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10759889}.
CC -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA18875.1; -; Genomic_DNA.
DR EMBL; AB027931; BAA87235.1; -; Genomic_DNA.
DR PIR; T39941; T39941.
DR RefSeq; NP_596607.1; NM_001022528.2.
DR AlphaFoldDB; O60182; -.
DR SMR; O60182; -.
DR BioGRID; 276954; 11.
DR ComplexPortal; CPX-546; DNA replication factor C complex.
DR IntAct; O60182; 1.
DR STRING; 4896.SPBC23E6.07c.1; -.
DR iPTMnet; O60182; -.
DR MaxQB; O60182; -.
DR PaxDb; O60182; -.
DR PRIDE; O60182; -.
DR EnsemblFungi; SPBC23E6.07c.1; SPBC23E6.07c.1:pep; SPBC23E6.07c.
DR GeneID; 2540426; -.
DR KEGG; spo:SPBC23E6.07c; -.
DR PomBase; SPBC23E6.07c; rfc1.
DR VEuPathDB; FungiDB:SPBC23E6.07c; -.
DR eggNOG; KOG1968; Eukaryota.
DR HOGENOM; CLU_003574_1_1_1; -.
DR InParanoid; O60182; -.
DR OMA; VKFPTWL; -.
DR PhylomeDB; O60182; -.
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-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:O60182; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IC:PomBase.
DR GO; GO:0043599; C:nuclear DNA replication factor C complex; ISO:PomBase.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; NAS:PomBase.
DR GO; GO:0003682; F:chromatin binding; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003689; F:DNA clamp loader activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IDA:PomBase.
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 Gene3D; 3.40.50.10190; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR013725; DNA_replication_fac_RFC1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012178; RFC1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF08519; RFC1; 1.
DR PIRSF; PIRSF036578; RFC1; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; DNA replication; DNA-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..934
FT /note="Replication factor C subunit 1"
FT /id="PRO_0000121775"
FT DOMAIN 236..326
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 1..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..891
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 416..423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 519
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 934 AA; 103489 MW; 4700EB0639C24F89 CRC64;
MSNSDIRSFF GGGNAQKKPK VSPTPTSPKP KRSLKKKRIV LSDDEDGTIE NSKVPASKSK
VQKRNESEDI SHSLPSIVHE DDKLVGSDGV STTPDEYFEQ QSTRSRSKPR IISNKETTTS
KDVVHPVKTE NFANDLDTTS DSKPVVHQTR ATRKPAQPKA EKSTTSKSKS HTTTATTHTS
RSSKSKGLPR FSDEVSQALK NVPLIDVDSM GVMAPGTFYE RAATTQTPGS KPVPEGNSDC
LSGISFVITG ILETLTRQEA TDLIKQYGGK VTGAPSVRTD FILLGENAGP RKVETIKQHK
IPAINEDGLF YLITHLPASG GTGAAAQAAQ QKKEQEEKKI LETVARMDDS NKKESQPSQI
WTSKYAPTSL KDICGNKGVV QKLQKWLQDY HKNRKSNFNK PGPDGLGLYK AVLLSGPPGI
GKTTAAHLVA KLEGYDVLEL NASDTRSKRL LDEQLFGVTD SQSLAGYFGT KANPVDMAKS
RLVLIMDEID GMSSGDRGGV GQLNMIIKKS MIPIICICND RAHPKLRPLD RTTFDLRFRR
PDANSMRSRI MSIAYREGLK LSPQAVDQLV QGTQSDMRQI INLLSTYKLS CSEMTPQNSQ
AVIKNSEKHI VMKPWDICSR YLHGGMFHPS SKSTINDKLE LYFNDHEFSY LMVQENYLNT
TPDRIRQEPP KMSHLKHLEL ISSAANSFSD SDLVDSMIHG PQQHWSLMPT HALMSCVRPA
SFVAGSGSRQ IRFTNWLGNN SKTNKLYRML REIQVHMRLK VSANKLDLRQ HYIPILYESL
PVKLSTGHSD VVPEIIELMD EYYLNREDFD SITELVLPAD AGEKLMKTIP TAAKSAFTRK
YNSSSHPIAF FGSSDVLPMK GSAQREVPDV EDAIEAEDEM LEEASDSEAA NEEDIDLSKD
KFISVPKKPK KRTKAKAEAS SSSSTSRRSR KKTA
