Please note: this site relies heavily on the use of javascript. Without a javascript-enabled browser, this site will not function correctly. Please enable javascript and reload the page, or switch to a different browser.
0  structures 261  species 0  interactions 327  sequences 12  architectures

Family: ORC5_C (PF14630)

Summary: Origin recognition complex (ORC) subunit 5 C-terminus

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "ORC5". More...

ORC5 Edit Wikipedia article

Origin recognition complex, subunit 5
Identifiers
Symbols ORC5; ORC5L; ORC5P; ORC5T
External IDs OMIM602331 MGI1347044 HomoloGene37636 GeneCards: ORC5 Gene
RNA expression pattern
PBB GE ORC5L 204957 at tn.png
PBB GE ORC5L 211212 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5001 26429
Ensembl ENSG00000164815 ENSMUSG00000029012
UniProt O43913 Q9WUV0
RefSeq (mRNA) NM_001197292 NM_011959
RefSeq (protein) NP_002544 NP_036089
Location (UCSC) Chr 7:
103.77 – 103.85 Mb
Chr 5:
22.49 – 22.55 Mb
PubMed search [1] [2]

Origin recognition complex subunit 5 is a protein that in humans is encoded by the ORC5 (ORC5L) gene.[1][2][3]

The origin recognition complex (ORC) is a highly conserved six subunit protein complex essential for the initiation of the DNA replication in eukaryotic cells. Studies in yeast demonstrated that ORC binds specifically to origins of replication and serves as a platform for the assembly of additional initiation factors such as Cdc6 and Mcm proteins. The protein encoded by this gene is a subunit of the ORC complex. It has been shown to form a core complex with ORC2L, -3L, and 4L. Alternatively spliced transcript variants encoding distinct isoforms have been described.[3]

Interactions[edit]

ORC5 has been shown to interact with ORC1,[4] ORC2,[4][5][6][7] MCM7,[4] ORC4,[4][5][6] ORC3,[4][6][7][8] MCM2,[4] MCM4[4] and MCM3.[4]

References[edit]

  1. ^ Ishiai M, Dean FB, Okumura K, Abe M, Moon KY, Amin AA, Kagotani K, Taguchi H, Murakami Y, Hanaoka F, O'Donnell M, Hurwitz J, Eki T (Feb 1998). "Isolation of human and fission yeast homologues of the budding yeast origin recognition complex subunit ORC5: human homologue (ORC5L) maps to 7q22". Genomics 46 (2): 294–8. doi:10.1006/geno.1997.5003. PMID 9417919. 
  2. ^ Tugal T, Zou-Yang XH, Gavin K, Pappin D, Canas B, Kobayashi R, Hunt T, Stillman B (Jan 1999). "The Orc4p and Orc5p subunits of the Xenopus and human origin recognition complex are related to Orc1p and Cdc6p". J Biol Chem 273 (49): 32421–9. doi:10.1074/jbc.273.49.32421. PMID 9829972. 
  3. ^ a b "Entrez Gene: ORC5L origin recognition complex, subunit 5-like (yeast)". 
  4. ^ a b c d e f g h Kneissl, Margot; Pütter Vera, Szalay Aladar A, Grummt Friedrich (Mar 2003). "Interaction and assembly of murine pre-replicative complex proteins in yeast and mouse cells". J. Mol. Biol. (England) 327 (1): 111–28. doi:10.1016/S0022-2836(03)00079-2. ISSN 0022-2836. PMID 12614612. 
  5. ^ a b Quintana, D G; Thome K C, Hou Z H, Ligon A H, Morton C C, Dutta A (Oct 1998). "ORC5L, a new member of the human origin recognition complex, is deleted in uterine leiomyomas and malignant myeloid diseases". J. Biol. Chem. (United States) 273 (42): 27137–45. doi:10.1074/jbc.273.42.27137. ISSN 0021-9258. PMID 9765232. 
  6. ^ a b c Dhar, S K; Delmolino L, Dutta A (Aug 2001). "Architecture of the human origin recognition complex". J. Biol. Chem. (United States) 276 (31): 29067–71. doi:10.1074/jbc.M103078200. ISSN 0021-9258. PMID 11395502. 
  7. ^ a b Vashee, S; Simancek P, Challberg M D, Kelly T J (Jul 2001). "Assembly of the human origin recognition complex". J. Biol. Chem. (United States) 276 (28): 26666–73. doi:10.1074/jbc.M102493200. ISSN 0021-9258. PMID 11323433. 
  8. ^ Pinto, S; Quintana D G, Smith P, Mihalek R M, Hou Z H, Boynton S, Jones C J, Hendricks M, Velinzon K, Wohlschlegel J A, Austin R J, Lane W S, Tully T, Dutta A (May 1999). "latheo encodes a subunit of the origin recognition complex and disrupts neuronal proliferation and adult olfactory memory when mutant". Neuron (United States) 23 (1): 45–54. doi:10.1016/S0896-6273(00)80752-7. ISSN 0896-6273. PMID 10402192. 

Further reading[edit]



This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This is the Wikipedia entry entitled "Origin recognition complex". More...

Origin recognition complex Edit Wikipedia article

Origin recognition complex subunit 2
Identifiers
Symbol ORC2
Pfam PF04084
InterPro IPR007220
Origin recognition complex (ORC) subunit 3 N-terminus
Identifiers
Symbol ORC3_N
Pfam PF07034
InterPro IPR010748
Origin recognition complex subunit 6 (ORC6)
Identifiers
Symbol ORC6
Pfam PF05460
InterPro IPR008721
Potential role of Cdc6 at the initiation of DNA replication.[1]

In molecular biology, ORC or origin recognition complex is a multi-subunit DNA binding complex (6 subunits) that binds in all eukaryotes in an ATP-dependent manner to origins of replication. The subunits of this complex are encoded by the ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6 genes.[2][3][4] ORC is a central component for eukaryotic DNA replication, and binds chromatin at replication origins throughout the cell cycle.[5] ORC directs DNA replication throughout the genome and is required for its initiation.[6][7][8] ORC bound at replication origins serves as the foundation for assembly of the pre-replication complex (pre-RC), which includes Cdc6, Tah11 (aka Cdt1), and the Mcm2-Mcm7 complex.[9][10][11] Pre-RC assembly during G1 is required for replication licensing of chromosomes prior to DNA synthesis during S phase.[12][13][14] Cell cycle-regulated phosphorylation of Orc2, Orc6, Cdc6, and MCM by the cyclin-dependent protein kinase Cdc28 regulates initiation of DNA replication, including blocking reinitiation in G2/M phase.[5][15][16][17]

In yeast, ORC also plays a role in the establishment of silencing at the mating-type loci Hidden MAT Left (HML) and Hidden MAT Right (HMR).[6][7][8] ORC participates in the assembly of transcriptionally silent chromatin at HML and HMR by recruiting the Sir1 silencing protein to the HML and HMR silencers.[8][18][19]

Both Orc1 and Orc5 bind ATP, though only Orc1 has ATPase activity.[20] The binding of ATP by Orc1 is required for ORC binding to DNA and is essential for cell viability.[11] The ATPase activity of Orc1 is involved in formation of the pre-RC.[21][22][23] ATP binding by Orc5 is crucial for the stability of ORC as a whole. Only the Orc1-5 subunits are required for origin binding; Orc6 is essential for maintenance of pre-RCs once formed.[24] Interactions within ORC suggest that Orc2-3-6 may form a core complex.[5]

References[edit]

  1. ^ Borlado LR, Méndez J (February 2008). "CDC6: from DNA replication to cell cycle checkpoints and oncogenesis". Carcinogenesis 29 (2): 237–43. doi:10.1093/carcin/bgm268. PMID 18048387. 
  2. ^ Origin Recognition Complex at the US National Library of Medicine Medical Subject Headings (MeSH)
  3. ^ Dutta A, Bell SP (1997). "Initiation of DNA replication in eukaryotic cells". Annu. Rev. Cell Dev. Biol. 13: 293–332. doi:10.1146/annurev.cellbio.13.1.293. PMID 9442876. 
  4. ^ Chesnokov IN (2007). "Multiple functions of the origin recognition complex". Int. Rev. Cytol. 256: 69–109. doi:10.1016/S0074-7696(07)56003-1. PMID 17241905. 
  5. ^ a b c Matsuda K, Makise M, Sueyasu Y, Takehara M, Asano T, Mizushima T (December 2007). "Yeast two-hybrid analysis of the origin recognition complex of Saccharomyces cerevisiae: interaction between subunits and identification of binding proteins". FEMS Yeast Res. 7 (8): 1263–9. doi:10.1111/j.1567-1364.2007.00298.x. PMID 17825065. 
  6. ^ a b Bell SP, Stillman B (May 1992). "ATP-dependent recognition of eukaryotic origins of DNA replication by a multiprotein complex". Nature 357 (6374): 128–34. doi:10.1038/357128a0. PMID 1579162. 
  7. ^ a b Bell SP, Mitchell J, Leber J, Kobayashi R, Stillman B (November 1995). "The multidomain structure of Orc1p reveals similarity to regulators of DNA replication and transcriptional silencing". Cell 83 (4): 563–8. doi:10.1016/0092-8674(95)90096-9. PMID 7585959. 
  8. ^ a b c Gibson DG, Bell SP, Aparicio OM (June 2006). "Cell cycle execution point analysis of ORC function and characterization of the checkpoint response to ORC inactivation in Saccharomyces cerevisiae". Genes Cells 11 (6): 557–73. doi:10.1111/j.1365-2443.2006.00967.x. PMID 16716188. 
  9. ^ Rao H, Stillman B (March 1995). "The origin recognition complex interacts with a bipartite DNA binding site within yeast replicators". Proc. Natl. Acad. Sci. U.S.A. 92 (6): 2224–8. doi:10.1073/pnas.92.6.2224. PMC 42456. PMID 7892251. 
  10. ^ Rowley A, Cocker JH, Harwood J, Diffley JF (June 1995). "Initiation complex assembly at budding yeast replication origins begins with the recognition of a bipartite sequence by limiting amounts of the initiator, ORC". EMBO J. 14 (11): 2631–41. PMC 398377. PMID 7781615. 
  11. ^ a b Speck C, Chen Z, Li H, Stillman B (November 2005). "ATPase-dependent cooperative binding of ORC and Cdc6 to origin DNA". Nat. Struct. Mol. Biol. 12 (11): 965–71. doi:10.1038/nsmb1002. PMC 2952294. PMID 16228006. 
  12. ^ Kelly TJ, Brown GW (2000). "Regulation of chromosome replication". Annu. Rev. Biochem. 69: 829–80. doi:10.1146/annurev.biochem.69.1.829. PMID 10966477. 
  13. ^ Bell SP, Dutta A (2002). "DNA replication in eukaryotic cells". Annu. Rev. Biochem. 71: 333–74. doi:10.1146/annurev.biochem.71.110601.135425. PMID 12045100. 
  14. ^ Stillman B (February 2005). "Origin recognition and the chromosome cycle". FEBS Lett. 579 (4): 877–84. doi:10.1016/j.febslet.2004.12.011. PMID 15680967. 
  15. ^ Weinreich M, Liang C, Chen HH, Stillman B (September 2001). "Binding of cyclin-dependent kinases to ORC and Cdc6p regulates the chromosome replication cycle". Proc. Natl. Acad. Sci. U.S.A. 98 (20): 11211–7. doi:10.1073/pnas.201387198. PMC 58709. PMID 11572976. 
  16. ^ Nguyen VQ, Co C, Li JJ (June 2001). "Cyclin-dependent kinases prevent DNA re-replication through multiple mechanisms". Nature 411 (6841): 1068–73. doi:10.1038/35082600. PMID 11429609. 
  17. ^ Archambault V, Ikui AE, Drapkin BJ, Cross FR (August 2005). "Disruption of mechanisms that prevent rereplication triggers a DNA damage response". Mol. Cell. Biol. 25 (15): 6707–21. doi:10.1128/MCB.25.15.6707-6721.2005. PMC 1190345. PMID 16024805. 
  18. ^ Triolo T, Sternglanz R (May 1996). "Role of interactions between the origin recognition complex and SIR1 in transcriptional silencing". Nature 381 (6579): 251–3. doi:10.1038/381251a0. PMID 8622770. 
  19. ^ Fox CA, Ehrenhofer-Murray AE, Loo S, Rine J (June 1997). "The origin recognition complex, SIR1, and the S phase requirement for silencing". Science 276 (5318): 1547–51. doi:10.1126/science.276.5318.1547. PMID 9171055. 
  20. ^ Klemm RD, Austin RJ, Bell SP (February 1997). "Coordinate binding of ATP and origin DNA regulates the ATPase activity of the origin recognition complex". Cell 88 (4): 493–502. doi:10.1016/S0092-8674(00)81889-9. PMID 9038340. 
  21. ^ Klemm RD, Bell SP (July 2001). "ATP bound to the origin recognition complex is important for preRC formation". Proc. Natl. Acad. Sci. U.S.A. 98 (15): 8361–7. doi:10.1073/pnas.131006898. PMC 37444. PMID 11459976. 
  22. ^ Bowers JL, Randell JC, Chen S, Bell SP (December 2004). "ATP hydrolysis by ORC catalyzes reiterative Mcm2-7 assembly at a defined origin of replication". Mol. Cell 16 (6): 967–78. doi:10.1016/j.molcel.2004.11.038. PMID 15610739. 
  23. ^ Randell JC, Bowers JL, Rodri­guez HK, Bell SP (January 2006). "Sequential ATP hydrolysis by Cdc6 and ORC directs loading of the Mcm2-7 helicase". Mol. Cell 21 (1): 29–39. doi:10.1016/j.molcel.2005.11.023. PMID 16387651. 
  24. ^ Semple JW, Da-Silva LF, Jervis EJ, Ah-Kee J, Al-Attar H, Kummer L, Heikkila JJ, Pasero P, Duncker BP (November 2006). "An essential role for Orc6 in DNA replication through maintenance of pre-replicative complexes". EMBO J. 25 (21): 5150–8. doi:10.1038/sj.emboj.7601391. PMC 1630405. PMID 17053779. 

Further reading[edit]

This article incorporates text from the public domain Pfam and InterPro IPR007220

This article incorporates text from the public domain Pfam and InterPro IPR010748

This article incorporates text from the public domain Pfam and InterPro IPR008721

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Origin recognition complex (ORC) subunit 5 C-terminus Provide feedback

This entry represents the C-terminus of origin recognition complex subunit 5 [1].

Literature references

  1. Ishiai M, Dean FB, Okumura K, Abe M, Moon KY, Amin AA, Kagotani K, Taguchi H, Murakami Y, Hanaoka F, O'Donnell M, Hurwitz J, Eki T;, Genomics. 1997;46:294-298.: Isolation of human and fission yeast homologues of the budding yeast origin recognition complex subunit ORC5: human homologue (ORC5L) maps to 7q22. PUBMED:9417919 EPMC:9417919


External database links

This tab holds annotation information from the InterPro database.

No InterPro data for this Pfam family.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

Loading domain graphics...

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(68)
Full
(327)
Representative proteomes NCBI
(309)
Meta
(2)
RP15
(72)
RP35
(122)
RP55
(203)
RP75
(243)
Jalview View  View  View  View  View  View  View  View 
HTML View  View  View  View  View  View     
PP/heatmap 1 View  View  View  View  View     
Pfam viewer View  View             

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(68)
Full
(327)
Representative proteomes NCBI
(309)
Meta
(2)
RP15
(72)
RP35
(122)
RP55
(203)
RP75
(243)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(68)
Full
(327)
Representative proteomes NCBI
(309)
Meta
(2)
RP15
(72)
RP35
(122)
RP55
(203)
RP75
(243)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

This family is new in this Pfam release.

Seed source: Jackhmmer:O43913
Previous IDs: none
Type: Family
Author: Eberhardt R
Number in seed: 68
Number in full: 327
Average length of the domain: 262.10 aa
Average identity of full alignment: 25 %
Average coverage of the sequence by the domain: 53.50 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 30.8 27.8
Noise cut-off 23.8 23.0
Model length: 271
Family (HMM) version: 1
Download: download the raw HMM for this family

Species distribution

Sunburst controls

Show

This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

Loading sunburst data...

Tree controls

Hide

The tree shows the occurrence of this domain across different species. More...

Loading...

Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.