Tag | Content |
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CPLM ID | CPLM-006889 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Replication factor C subunit 5 |
Protein Synonyms/Alias | Replication factor C5; Activator 1 40 kDa subunit |
Gene Name | RFC5 |
Gene Synonyms/Alias | YBR087W; YBR0810 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
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256 | KSSSPIIKPDWIIVI | acetylation | [1] |
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Reference | [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] |
Functional Description | Component of ATP-dependent clamp loader (RFC and RFC- like) complexes for DNA clamps, such as the POL30/PCNA homotrimer and the checkpoint clamp DDC1:MEC3:RAD17 complex. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA. Component of the replication factor C (RFC or activator 1) complex which loads POL30/PCNA and acts during elongation of primed DNA templates by DNA polymerase delta and epsilon. RFC has an essential but redundant activity in sister chromatid cohesion establishment. Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. Component of the RFC-like RAD24-RFC complex which loads the checkpoint clamp DDC1:MEC3:RAD17 complex and is involved in DNA repair pathways. Component of the RFC-like ELG1-RFC complex which appears to have a role in DNA replication, replication fork re-start, recombination and repair. |
Sequence Annotation | NP_BIND 43 51 ATP. BINDING 5 5 ATP; via carbonyl oxygen. BINDING 17 17 ATP. BINDING 231 231 ATP. |
Keyword | 3D-structure; ATP-binding; Cell cycle; Complete proteome; DNA replication; DNA-binding; Nucleotide-binding; Nucleus; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 354 AA |
Protein Sequence | MSLWVDKYRP KSLNALSHNE ELTNFLKSLS DQPRDLPHLL LYGPNGTGKK TRCMALLESI 60 FGPGVYRLKI DVRQFVTASN RKLELNVVSS PYHLEITPSD MGNNDRIVIQ ELLKEVAQME 120 QVDFQDSKDG LAHRYKCVII NEANSLTKDA QAALRRTMEK YSKNIRLIMV CDSMSPIIAP 180 IKSRCLLIRC PAPSDSEIST ILSDVVTNER IQLETKDILK RIAQASNGNL RVSLLMLESM 240 ALNNELALKS SSPIIKPDWI IVIHKLTRKI VKERSVNSLI ECRAVLYDLL AHCIPANIIL 300 KELTFSLLDV ETLNTTNKSS IIEYSSVFDE RLSLGNKAIF HLEGFIAKVM CCLD 354 |
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