ORC1 origin recognition complex subunit 1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Gene symbol: ORC1
Gene description: origin recognition complex subunit 1
Primary source: FungiDB:YML065W
Locus tag: YML065W
See related: SGD:S000004530; AllianceGenome:SGD:S000004530; VEuPathDB:YML065W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables several functions, including ATP binding activity; ATP hydrolysis activity; and DNA replication origin binding activity. Involved in DNA-dependent DNA replication and chromosome organization. Located in nucleus. Part of DNA replication preinitiation complex; nuclear origin of replication recognition complex; and nuclear pre-replicative complex. Used to study Meier-Gorlin syndrome. Human ortholog(s) of this gene implicated in Meier-Gorlin syndrome 1. Orthologous to human ORC1 (origin recognition complex subunit 1). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See ORC1 in Genome Data Viewer

Location:: chromosome: XIII

Exon count:: 1

Sequence:: Chromosome: XIII; NC_001145.3 (142210..144954)

Chromosome XIII - NC_001145.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001145.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Biochemical and functional characterization of a meiosis-specific Pch2/ORC AAA+ assembly.
Title: Biochemical and functional characterization of a meiosis-specific Pch2/ORC AAA+ assembly.
Active transcription and Orc1 drive chromatin association of the AAA+ ATPase Pch2 during meiotic G2/prophase.
Title: Active transcription and Orc1 drive chromatin association of the AAA+ ATPase Pch2 during meiotic G2/prophase.
Direct interactions with nucleosomes are essential for Orc1 to maintain the integrity of rDNA borders during meiosis.
Title: Structure and function of the Orc1 BAH-nucleosome complex.
the diminished cell-cycle changes in nucleosome occupancy around origins in the orc1-161 mutant are associated with an abnormal global origin usage profile, suggesting that proper establishment of nucleosome occupancy around origins is a critical step for regulation of global origin activities. Our work thus establishes nucleosome occupancy as a novel and key chromatin parameter for proper origin regulation.
Title: Nucleosome occupancy as a novel chromatin parameter for replication origin functions.
Specific ORC1 to DNA replication origins depends on highly conserved basic residues.
Title: Specific binding of eukaryotic ORC to DNA replication origins depends on highly conserved basic residues.
Data indicate that Cdt1-MCM2-7 complex activates ORC/Cdc6 ATP-hydrolysis to promote helicase loading.
Title: An ORC/Cdc6/MCM2-7 complex is formed in a multistep reaction to serve as a platform for MCM double-hexamer assembly.
The functional specialization of Sir3,as a silencing protein was facilitated by the tandem duplication of the OIR domain in the Sir1 family, allowing distinct Sir1-Sir3 and Sir1-Orc1 interactions through OIR-BAH domain interactions.
Title: Elaboration, diversification and regulation of the Sir1 family of silencing proteins in Saccharomyces.
Coimmunoprecipitation assay confirmed that Cdt1p interacted with Orc6p, as well as with Orc1p and Orc2p.
Title: Interaction between ORC and Cdt1p of Saccharomyces cerevisiae.

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables ATP binding	IDA Inferred from Direct Assay more info	PubMed
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables ATP hydrolysis activity	IEA Inferred from Electronic Annotation more info
enables ATP hydrolysis activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables DNA binding	IEA Inferred from Electronic Annotation more info
enables DNA replication origin binding	IBA Inferred from Biological aspect of Ancestor more info
enables DNA replication origin binding	IDA Inferred from Direct Assay more info	PubMed
enables chromatin binding	IDA Inferred from Direct Assay more info	PubMed
enables chromatin binding	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables nucleosome binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in DNA replication	IEA Inferred from Electronic Annotation more info
involved_in DNA replication initiation	IBA Inferred from Biological aspect of Ancestor more info
involved_in DNA replication initiation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in maintenance of rDNA	IDA Inferred from Direct Assay more info	PubMed
involved_in mitotic DNA replication checkpoint signaling	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within nucleosome organization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in pre-replicative complex assembly involved in nuclear cell cycle DNA replication	IDA Inferred from Direct Assay more info	PubMed
involved_in pre-replicative complex assembly involved in nuclear cell cycle DNA replication	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in silent mating-type cassette heterochromatin formation	IDA Inferred from Direct Assay more info	PubMed
involved_in silent mating-type cassette heterochromatin formation	IGI Inferred from Genetic Interaction more info	PubMed

Component	Evidence Code	Pubs
part_of DNA replication preinitiation complex	IDA Inferred from Direct Assay more info	PubMed
located_in chromosome	IEA Inferred from Electronic Annotation more info
part_of nuclear origin of replication recognition complex	IBA Inferred from Biological aspect of Ancestor more info
part_of nuclear origin of replication recognition complex	IDA Inferred from Direct Assay more info	PubMed
part_of nuclear origin of replication recognition complex	IMP Inferred from Mutant Phenotype more info	PubMed
part_of nuclear pre-replicative complex	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info
part_of protein-DNA complex	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: origin recognition complex subunit 1

NP_013646.1

Largest subunit of the origin recognition complex; involved in directing DNA replication by binding to replication origins; also involved in transcriptional silencing; exhibits ATPase activity; role in chromatin organization at replication origins, along with chromatin remodellers; ORC1 has a paralog, SIR3, that arose from the whole genome duplication

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001145.3 Reference assembly

Range

142210..144954

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001182424.1 → NP_013646.1 TPA: origin recognition complex subunit 1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_013646.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VZA8, P54784

UniProtKB/TrEMBL

C7GW01

Conserved Domains (2) summary

COG1474
Location:426 → 890

CDC6; Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]

cd04720
Location:5 → 189

BAH_Orc1p_Yeast; BAH, or Bromo Adjacent Homology domain, as present in Orc1p, which again is part of the Saccharomyces cerevisiae Sir1-origin recognition complex, and as present in Sir3p. The Orc1p BAH doman functions in epigenetic silencing. BAH domains are found in a ...