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Protein

Replication factor C subunit 1

Gene

Gnf1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1. This subunit binds to the primer-template junction (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi487 – 4948ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: FlyBase
  • DNA clamp loader activity Source: InterPro

GO - Biological processi

  • dendrite morphogenesis Source: FlyBase
  • DNA repair Source: InterPro
  • DNA replication Source: FlyBase
  • lateral inhibition Source: FlyBase
  • neurogenesis Source: FlyBase
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • sensory perception of pain Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

DNA replication, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-110312. Translesion synthesis by REV1.
R-DME-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-DME-110320. Translesion Synthesis by POLH.
R-DME-174411. Polymerase switching on the C-strand of the telomere.
R-DME-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-DME-5655862. Translesion synthesis by POLK.
R-DME-5656121. Translesion synthesis by POLI.
R-DME-5656169. Termination of translesion DNA synthesis.
R-DME-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-DME-6782135. Dual incision in TC-NER.
R-DME-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-DME-69091. Polymerase switching.

Names & Taxonomyi

Protein namesi
Recommended name:
Replication factor C subunit 1
Alternative name(s):
Activator 1 140 kDa subunit
Activator 1 subunit 1
Germline transcription factor 1
Replication factor C large subunit
Gene namesi
Name:Gnf1
ORF Names:CG1119
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0004913. Gnf1.

Subcellular locationi

GO - Cellular componenti

  • DNA replication factor C complex Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • nucleus Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 986986Replication factor C subunit 1PRO_0000121774Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181Phosphoserine1 Publication
Modified residuei28 – 281Phosphoserine1 Publication
Modified residuei40 – 401Phosphoserine1 Publication
Modified residuei41 – 411Phosphoserine1 Publication
Modified residuei48 – 481Phosphoserine1 Publication
Modified residuei58 – 581Phosphoserine1 Publication
Modified residuei60 – 601Phosphothreonine1 Publication
Modified residuei62 – 621Phosphoserine1 Publication
Modified residuei63 – 631Phosphoserine1 Publication
Modified residuei71 – 711Phosphothreonine1 Publication
Modified residuei128 – 1281Phosphoserine1 Publication
Modified residuei137 – 1371Phosphoserine1 Publication
Modified residuei149 – 1491Phosphoserine1 Publication
Modified residuei154 – 1541Phosphoserine1 Publication
Modified residuei156 – 1561Phosphoserine1 Publication
Modified residuei164 – 1641Phosphoserine1 Publication
Modified residuei194 – 1941Phosphoserine1 Publication
Modified residuei197 – 1971Phosphothreonine1 Publication
Modified residuei938 – 9381Phosphoserine1 Publication
Modified residuei939 – 9391Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP35600.
PRIDEiP35600.

PTM databases

iPTMnetiP35600.

Expressioni

Gene expression databases

GenevisibleiP35600. DM.

Interactioni

Subunit structurei

Interacts with C-terminus of PCNA.1 Publication

Protein-protein interaction databases

BioGridi65822. 20 interactions.
DIPiDIP-18735N.
IntActiP35600. 9 interactions.
MINTiMINT-961959.
STRINGi7227.FBpp0099511.

Structurei

3D structure databases

ProteinModelPortaliP35600.
SMRiP35600. Positions 225-314, 421-651.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini232 – 32291BRCTPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi955 – 9595Nuclear localization signalSequence analysis

Sequence similaritiesi

Belongs to the activator 1 large subunit family.Curated
Contains 1 BRCT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IPR8. Eukaryota.
COG5275. LUCA.
GeneTreeiENSGT00730000111066.
InParanoidiP35600.
KOiK10754.
OrthoDBiEOG7N63M2.
PhylomeDBiP35600.

Family and domain databases

Gene3Di3.40.50.10190. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR001357. BRCT_dom.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR013725. DNA_replication_fac_RFC1_C.
IPR027417. P-loop_NTPase.
IPR012178. RFC1.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF00533. BRCT. 1 hit.
PF08519. RFC1. 1 hit.
[Graphical view]
PIRSFiPIRSF036578. RFC1. 1 hit.
SMARTiSM00382. AAA. 1 hit.
SM00292. BRCT. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52113. SSF52113. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35600-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRGIDSFFK RLPAKAKSAE AENGETPSKA PKRRKAVIIS SDEDEVVSPP
60 70 80 90 100
ETKKRKASKT ASSEDDVVAA TPEPIAKKAR NGQKPALSKL KRHVDPTELF
110 120 130 140 150
GGETKRVIVP KPKTKAVLEF ENEDIDRSLM EVDLDESIKE AAPEKKVHSI
160 170 180 190 200
TRSSPSPKRA KNSSPEPPKP KSTKSKATTP RVKKEKPAAD LESSVLTDEE
210 220 230 240 250
RHERKRASAV LYQKYKNRSS CLNPGSKEIP KGSPDCLSGL TFVVTGVLES
260 270 280 290 300
MEREEAESVI KEYGGKVMTV VGKKLKYLVV GEEAGPKKLA VAEELNIPIL
310 320 330 340 350
SEDGLFDLIR EKSGIAKQVK EEKKSPKKEH SSEEKGKKEV KTSRRSSDKK
360 370 380 390 400
EKEATKLKYG EKHDIAKHKV KEEHTSPKET KDKLNDVPAV TLKVKKEPSS
410 420 430 440 450
QKEHPPSPRT ADLKTLDVVG MAWVDKHKPT SIKEIVGQAG AASNVTKLMN
460 470 480 490 500
WLSKWYVNHD GNKKPQRPNP WAKNDDGSFY KAALLSGPPG IGKTTTATLV
510 520 530 540 550
VKELGFDAVE FNASDTRSKR LLKDEVSTLL SNKSLSGYFT GQGQAVSRKH
560 570 580 590 600
VLIMDEVDGM AGNEDRGGMQ ELIALIKDSS IPIICMCNDR NHPKIRSLVN
610 620 630 640 650
YCYDLRFQRP RLEQIKGKIM SICFKEKVKI SPAKVEEIIA ATNNDIRQSI
660 670 680 690 700
NHIALLSAKE DASQKSGQQV ATKDLKLGPW EVVRKVFTAD EHKHMSFADK
710 720 730 740 750
SDLFFHDYSL APLFVQQNYL QVLPQGNKKD VLAKVAATAD ALSLGDLVEK
760 770 780 790 800
RIRANSAWSL LPTQAFFSSV LPGEHMCGHF TGQINFPGWL GKNSKSGKRA
810 820 830 840 850
RLAQELHDHT RVCTSGSRLS VRLDYAPFLL DNIVRPLAKD GQEGVPAALD
860 870 880 890 900
VMKDYHLLRE DLDSLVELTS WPGKKSPLDA VDGRVKAALT RSYNKEVMAY
910 920 930 940 950
SYSAQAGIKK KKSEAAGADD DYLDEGPGEE DGAGGHLSSE EDEDKDNLEL
960 970 980
DSLIKAKKRT TTSKASGGSK KATSSTASKS KAKAKK
Length:986
Mass (Da):108,615
Last modified:December 1, 2000 - v2
Checksum:iA1E9C8EE0879545F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti447 – 4471K → NHNLKLKAKQERVKVLHYFN FPR in AAM52589 (Ref. 5) Curated
Sequence conflicti559 – 5591G → A in AAA28573 (PubMed:9705493).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L17340 Genomic DNA. Translation: AAA28573.1.
U97685 mRNA. Translation: AAB58311.1.
AE014297 Genomic DNA. Translation: AAF52082.1.
AE014297 Genomic DNA. Translation: AAX52937.1.
AY122077 mRNA. Translation: AAM52589.1.
BT003618 mRNA. Translation: AAO39621.1.
RefSeqiNP_001014605.1. NM_001014605.3.
NP_524229.1. NM_079505.3.
UniGeneiDm.2491.

Genome annotation databases

EnsemblMetazoaiFBtr0078837; FBpp0078478; FBgn0004913.
GeneIDi40607.
KEGGidme:Dmel_CG1119.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L17340 Genomic DNA. Translation: AAA28573.1.
U97685 mRNA. Translation: AAB58311.1.
AE014297 Genomic DNA. Translation: AAF52082.1.
AE014297 Genomic DNA. Translation: AAX52937.1.
AY122077 mRNA. Translation: AAM52589.1.
BT003618 mRNA. Translation: AAO39621.1.
RefSeqiNP_001014605.1. NM_001014605.3.
NP_524229.1. NM_079505.3.
UniGeneiDm.2491.

3D structure databases

ProteinModelPortaliP35600.
SMRiP35600. Positions 225-314, 421-651.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65822. 20 interactions.
DIPiDIP-18735N.
IntActiP35600. 9 interactions.
MINTiMINT-961959.
STRINGi7227.FBpp0099511.

PTM databases

iPTMnetiP35600.

Proteomic databases

PaxDbiP35600.
PRIDEiP35600.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078837; FBpp0078478; FBgn0004913.
GeneIDi40607.
KEGGidme:Dmel_CG1119.

Organism-specific databases

CTDi100035172.
FlyBaseiFBgn0004913. Gnf1.

Phylogenomic databases

eggNOGiENOG410IPR8. Eukaryota.
COG5275. LUCA.
GeneTreeiENSGT00730000111066.
InParanoidiP35600.
KOiK10754.
OrthoDBiEOG7N63M2.
PhylomeDBiP35600.

Enzyme and pathway databases

ReactomeiR-DME-110312. Translesion synthesis by REV1.
R-DME-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-DME-110320. Translesion Synthesis by POLH.
R-DME-174411. Polymerase switching on the C-strand of the telomere.
R-DME-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-DME-5655862. Translesion synthesis by POLK.
R-DME-5656121. Translesion synthesis by POLI.
R-DME-5656169. Termination of translesion DNA synthesis.
R-DME-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-DME-6782135. Dual incision in TC-NER.
R-DME-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-DME-69091. Polymerase switching.

Miscellaneous databases

GenomeRNAii40607.
PROiP35600.

Gene expression databases

GenevisibleiP35600. DM.

Family and domain databases

Gene3Di3.40.50.10190. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR001357. BRCT_dom.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR013725. DNA_replication_fac_RFC1_C.
IPR027417. P-loop_NTPase.
IPR012178. RFC1.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF00533. BRCT. 1 hit.
PF08519. RFC1. 1 hit.
[Graphical view]
PIRSFiPIRSF036578. RFC1. 1 hit.
SMARTiSM00382. AAA. 1 hit.
SM00292. BRCT. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52113. SSF52113. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a putative transcription factor active during oogenesis and embryogenesis."
    Frank L.H., Cohen R.S.
    Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "DNA recognition properties of the N-terminal DNA binding domain within the large subunit of replication factor C."
    Allen B.L., Uhlmann F., Gaur L.K., Mulder B.A., Posey K.L., Jones L.B., Hardin S.H.
    Nucleic Acids Res. 26:3877-3882(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DNA-BINDING ACTIVITY.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  6. "Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen."
    Mossi R., Jonsson Z.O., Allen B.L., Hardin S.H., Huebscher U.
    J. Biol. Chem. 272:1769-1776(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PCNA.
  7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-28; SER-40; SER-41; SER-48; SER-58; THR-60; SER-62; SER-63; THR-71; SER-128; SER-137; SER-149; SER-154; SER-156; SER-164; SER-194; THR-197; SER-938 AND SER-939, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiRFC1_DROME
AccessioniPrimary (citable) accession number: P35600
Secondary accession number(s): O02031, Q8MR76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 1, 2000
Last modified: June 8, 2016
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.