Origin recognition complex subunit 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P54784 (ORC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 129. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Origin recognition complex subunit 1

Alternative name(s):
Origin recognition complex 120 kDa subunit

Gene names

Name:	ORC1
Ordered Locus Names:	YML065W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	914 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication. Ref.7
Subunit structure	Component of the origin recognition complex (ORC) composed of at least ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. Interacts with MCM10 and TAH11. Ref.5 Ref.7
Subcellular location	Nucleus.
Domain	The N-terminus is dedicated to mating-type repression.
Miscellaneous	Present with 3930 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the ORC1 family. Contains 1 BAH domain.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
Ligand	ATP-binding DNA-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication initiation Inferred from mutant phenotype PubMed 16716188. Source: SGD chromatin silencing at silent mating-type cassette Inferred from direct assay PubMed 12897051 PubMed 16581798. Source: SGD pre-replicative complex assembly Inferred from direct assay PubMed 16824194. Source: SGD
Cellular_component	DNA replication preinitiation complex Inferred from direct assay PubMed 9554851. Source: SGD nuclear origin of replication recognition complex Inferred from direct assay PubMed 9372948. Source: SGD pre-replicative complex Inferred from direct assay PubMed 16824194 PubMed 9335335. Source: SGD
Molecular_function	ATP binding Inferred from direct assay Ref.7. Source: SGD ATPase activity Inferred from mutant phenotype PubMed 9038340. Source: SGD DNA replication origin binding Inferred from direct assay PubMed 16824194. Source: SGD chromatin binding Inferred from direct assay Ref.5. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ORC4	P54791	4	EBI-12568,EBI-12580

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 914

914

Origin recognition complex subunit 1

PRO_0000127074

Regions

Domain

48 – 188

141

BAH

Nucleotide binding

479 – 486

ATP Potential

Nucleotide binding

726 – 733

ATP Potential

Compositional bias

281 – 292

Poly-Glu

Compositional bias

759 – 768

Poly-Asp

Amino acid modifications

Modified residue

237

Phosphoserine Ref.8 Ref.9 Ref.10

Secondary structure

914

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P54784 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: BDAA9D3E40B4B76A
Show »

FASTA

914

104,400

        10         20         30         40         50         60 
MAKTLKDLQG WEIITTDEQG NIIDGGQKRL RRRGAKTEHY LKRSSDGIKL GRGDSVVMHN 

        70         80         90        100        110        120 
EAAGTYSVYM IQELRLNTLN NVVELWALTY LRWFEVNPLA HYRQFNPDAN ILNRPLNYYN 

       130        140        150        160        170        180 
KLFSETANKN ELYLTAELAE LQLFNFIRVA NVMDGSKWEV LKGNVDPERD FTVRYICEPT 

       190        200        210        220        230        240 
GEKFVDINIE DVKAYIKKVE PREAQEYLKD LTLPSKKKEI KRGPQKKDKA TQTAQISDAE 

       250        260        270        280        290        300 
TRATDITDNE DGNEDESSDY ESPSDIDVSE DMDSGEISAD ELEEEEDEEE DEDEEEKEAR 

       310        320        330        340        350        360 
HTNSPRKRGR KIKLGKDDID ASVQPPPKKR GRKPKDPSKP RQMLLISSCR ANNTPVIRKF 

       370        380        390        400        410        420 
TKKNVARAKK KYTPFSKRFK SIAAIPDLTS LPEFYGNSSE LMASRFENKL KTTQKHQIVE 

       430        440        450        460        470        480 
TIFSKVKKQL NSSYVKEEIL KSANFQDYLP ARENEFASIY LSAYSAIESD SATTIYVAGT 

       490        500        510        520        530        540 
PGVGKTLTVR EVVKELLSSS AQREIPDFLY VEINGLKMVK PTDCYETLWN KVSGERLTWA 

       550        560        570        580        590        600 
ASMESLEFYF KRVPKNKKKT IVVLLDELDA MVTKSQDIMY NFFNWTTYEN AKLIVIAVAN 

       610        620        630        640        650        660 
TMDLPERQLG NKITSRIGFT RIMFTGYTHE ELKNIIDLRL KGLNDSFFYV DTKTGNAILI 

       670        680        690        700        710        720 
DAAGNDTTVK QTLPEDVRKV RLRMSADAIE IASRKVASVS GDARRALKVC KRAAEIAEKH 

       730        740        750        760        770        780 
YMAKHGYGYD GKTVIEDENE EQIYDDEDKD LIESNKAKDD NDDDDDNDGV QTVHITHVMK 

       790        800        810        820        830        840 
ALNETLNSHV ITFMTRLSFT AKLFIYALLN LMKKNGSQEQ ELGDIVDEIK LLIEVNGSNK 

       850        860        870        880        890        900 
FVMEIAKTLF QQGSDNISEQ LRIISWDFVL NQLLDAGILF KQTMKNDRIC CVKLNISVEE 

       910 
AKRAMNEDET LRNL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The multidomain structure of Orc1p reveals similarity to regulators of DNA replication and transcriptional silencing." Bell S.P., Mitchell J., Leber J., Kobayashi R., Stillman B. Cell 83:563-568(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 381-408; 532-550; 642-653 AND 726-732.
[2]	"The origin recognition complex in silencing, cell cycle progression, and DNA replication." Loo S., Fox C.A., Rine J., Kobayashi R., Stillman B., Bell S.P. Mol. Biol. Cell 6:741-756(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Interactions between Mcm10p and other replication factors are required for proper initiation and elongation of chromosomal DNA replication in Saccharomyces cerevisiae." Kawasaki Y., Hiraga S., Sugino A. Genes Cells 5:975-989(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION MCM10.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Interaction between ORC and Cdt1p of Saccharomyces cerevisiae." Asano T., Makise M., Takehara M., Mizushima T. FEMS Yeast Res. 7:1256-1262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TAH11.
[8]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, MASS SPECTROMETRY. Strain: ADR376.
[9]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, MASS SPECTROMETRY.
[10]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U34860 Genomic DNA. Translation: AAB38248.1.
Z38114 Genomic DNA. Translation: CAA86256.1.
BK006946 Genomic DNA. Translation: DAA09832.1.

PIR

S48333.

RefSeq

NP_013646.1. NM_001182424.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M4Z	X-ray	2.20	A/B	1-235	[»]
1ZBX	X-ray	2.50	A	1-219	[»]
1ZHI	X-ray	2.70	A	1-219	[»]

ProteinModelPortal

P54784.

SMR

P54784. Positions 10-214, 435-738.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2284N.

IntAct

P54784. 34 interactions.

MINT

MINT-616045.

STRING

4932.YML065W.

Proteomic databases

PaxDb

P54784.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YML065W; YML065W; YML065W.

GeneID

854937.

KEGG

sce:YML065W.

Organism-specific databases

CYGD

YML065w.

SGD

S000004530. ORC1.

Phylogenomic databases

eggNOG

COG1474.

GeneTree

ENSGT00550000076094.

HOGENOM

HOG000115288.

K02603.

OMA

FTGYTHE.

OrthoDB

EOG4GQTF8.

Gene expression databases

Genevestigator

P54784.

GermOnline

YML065W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR001025. BAH_dom.
IPR020793. ORC1.
[Graphical view]

PANTHER

PTHR10763:SF6. PTHR10763:SF6. 1 hit.

Pfam

PF00004. AAA. 1 hit.
PF01426. BAH. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 1 hit.
SM00439. BAH. 1 hit.
[Graphical view]

PROSITE

PS51038. BAH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P54784.

NextBio

977980.

Entry information

Entry name

ORC1_YEAST

Accession

Primary (citable) accession number: P54784
Secondary accession number(s): D6VZA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents