RFC1_DROME
ID RFC1_DROME Reviewed; 986 AA.
AC P35600; O02031; Q8MR76;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Replication factor C subunit 1;
DE AltName: Full=Activator 1 140 kDa subunit;
DE AltName: Full=Activator 1 subunit 1;
DE AltName: Full=Germline transcription factor 1;
DE AltName: Full=Replication factor C large subunit;
GN Name=Gnf1; ORFNames=CG1119;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Frank L.H., Cohen R.S.;
RT "Cloning and characterization of a putative transcription factor active
RT during oogenesis and embryogenesis.";
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DNA-BINDING ACTIVITY.
RX PubMed=9705493; DOI=10.1093/nar/26.17.3877;
RA Allen B.L., Uhlmann F., Gaur L.K., Mulder B.A., Posey K.L., Jones L.B.,
RA Hardin S.H.;
RT "DNA recognition properties of the N-terminal DNA binding domain within the
RT large subunit of replication factor C.";
RL Nucleic Acids Res. 26:3877-3882(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH PCNA.
RX PubMed=8999859; DOI=10.1074/jbc.272.3.1769;
RA Mossi R., Jonsson Z.O., Allen B.L., Hardin S.H., Huebscher U.;
RT "Replication factor C interacts with the C-terminal side of proliferating
RT cell nuclear antigen.";
RL J. Biol. Chem. 272:1769-1776(1997).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-28; SER-40; SER-41;
RP SER-48; SER-58; THR-60; SER-62; SER-63; THR-71; SER-128; SER-137; SER-149;
RP SER-154; SER-156; SER-164; SER-194; THR-197; SER-938 AND SER-939, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: The elongation of primed DNA templates by DNA polymerase
CC delta and epsilon requires the action of the accessory proteins
CC proliferating cell nuclear antigen (PCNA) and activator 1. This subunit
CC binds to the primer-template junction (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with C-terminus of PCNA.
CC {ECO:0000269|PubMed:8999859}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC {ECO:0000305}.
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DR EMBL; L17340; AAA28573.1; -; Genomic_DNA.
DR EMBL; U97685; AAB58311.1; -; mRNA.
DR EMBL; AE014297; AAF52082.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52937.1; -; Genomic_DNA.
DR EMBL; AY122077; AAM52589.1; -; mRNA.
DR EMBL; BT003618; AAO39621.1; -; mRNA.
DR RefSeq; NP_001014605.1; NM_001014605.3.
DR RefSeq; NP_524229.1; NM_079505.3.
DR AlphaFoldDB; P35600; -.
DR SMR; P35600; -.
DR BioGRID; 65822; 28.
DR DIP; DIP-18735N; -.
DR IntAct; P35600; 9.
DR STRING; 7227.FBpp0099511; -.
DR iPTMnet; P35600; -.
DR PaxDb; P35600; -.
DR PRIDE; P35600; -.
DR EnsemblMetazoa; FBtr0078837; FBpp0078478; FBgn0004913.
DR GeneID; 40607; -.
DR KEGG; dme:Dmel_CG1119; -.
DR CTD; 100035172; -.
DR FlyBase; FBgn0004913; Gnf1.
DR VEuPathDB; VectorBase:FBgn0004913; -.
DR eggNOG; KOG1968; Eukaryota.
DR GeneTree; ENSGT00730000111066; -.
DR HOGENOM; CLU_003574_0_1_1; -.
DR InParanoid; P35600; -.
DR PhylomeDB; P35600; -.
DR Reactome; R-DME-110312; Translesion synthesis by REV1.
DR Reactome; R-DME-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-DME-110320; Translesion Synthesis by POLH.
DR Reactome; R-DME-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-DME-5655862; Translesion synthesis by POLK.
DR Reactome; R-DME-5656121; Translesion synthesis by POLI.
DR Reactome; R-DME-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-DME-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-DME-5696400; Dual Incision in GG-NER.
DR Reactome; R-DME-6782135; Dual incision in TC-NER.
DR Reactome; R-DME-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-DME-69091; Polymerase switching.
DR SignaLink; P35600; -.
DR BioGRID-ORCS; 40607; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 40607; -.
DR PRO; PR:P35600; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0004913; Expressed in ovary and 24 other tissues.
DR Genevisible; P35600; DM.
DR GO; GO:0005663; C:DNA replication factor C complex; NAS:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
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; IDA:FlyBase.
DR GO; GO:0003689; F:DNA clamp loader activity; IEA:InterPro.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; NAS:FlyBase.
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 Activator; ATP-binding; DNA replication; DNA-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..986
FT /note="Replication factor C subunit 1"
FT /id="PRO_0000121774"
FT DOMAIN 232..322
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 955..959
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 26..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..958
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 487..494
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 60
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 197
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 939
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 447
FT /note="K -> NHNLKLKAKQERVKVLHYFNFPR (in Ref. 5; AAM52589)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="G -> A (in Ref. 2; AAA28573)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 986 AA; 108615 MW; A1E9C8EE0879545F CRC64;
MQRGIDSFFK RLPAKAKSAE AENGETPSKA PKRRKAVIIS SDEDEVVSPP ETKKRKASKT
ASSEDDVVAA TPEPIAKKAR NGQKPALSKL KRHVDPTELF GGETKRVIVP KPKTKAVLEF
ENEDIDRSLM EVDLDESIKE AAPEKKVHSI TRSSPSPKRA KNSSPEPPKP KSTKSKATTP
RVKKEKPAAD LESSVLTDEE RHERKRASAV LYQKYKNRSS CLNPGSKEIP KGSPDCLSGL
TFVVTGVLES MEREEAESVI KEYGGKVMTV VGKKLKYLVV GEEAGPKKLA VAEELNIPIL
SEDGLFDLIR EKSGIAKQVK EEKKSPKKEH SSEEKGKKEV KTSRRSSDKK EKEATKLKYG
EKHDIAKHKV KEEHTSPKET KDKLNDVPAV TLKVKKEPSS QKEHPPSPRT ADLKTLDVVG
MAWVDKHKPT SIKEIVGQAG AASNVTKLMN WLSKWYVNHD GNKKPQRPNP WAKNDDGSFY
KAALLSGPPG IGKTTTATLV VKELGFDAVE FNASDTRSKR LLKDEVSTLL SNKSLSGYFT
GQGQAVSRKH VLIMDEVDGM AGNEDRGGMQ ELIALIKDSS IPIICMCNDR NHPKIRSLVN
YCYDLRFQRP RLEQIKGKIM SICFKEKVKI SPAKVEEIIA ATNNDIRQSI NHIALLSAKE
DASQKSGQQV ATKDLKLGPW EVVRKVFTAD EHKHMSFADK SDLFFHDYSL APLFVQQNYL
QVLPQGNKKD VLAKVAATAD ALSLGDLVEK RIRANSAWSL LPTQAFFSSV LPGEHMCGHF
TGQINFPGWL GKNSKSGKRA RLAQELHDHT RVCTSGSRLS VRLDYAPFLL DNIVRPLAKD
GQEGVPAALD VMKDYHLLRE DLDSLVELTS WPGKKSPLDA VDGRVKAALT RSYNKEVMAY
SYSAQAGIKK KKSEAAGADD DYLDEGPGEE DGAGGHLSSE EDEDKDNLEL DSLIKAKKRT
TTSKASGGSK KATSSTASKS KAKAKK
