ORC1_YEAST
ID ORC1_YEAST Reviewed; 914 AA.
AC P54784; D6VZA8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Origin recognition complex subunit 1;
DE AltName: Full=Origin recognition complex 120 kDa subunit;
GN Name=ORC1; OrderedLocusNames=YML065W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 381-408;
RP 532-550; 642-653 AND 726-732.
RX PubMed=7585959; DOI=10.1016/0092-8674(95)90096-9;
RA Bell S.P., Mitchell J., Leber J., Kobayashi R., Stillman B.;
RT "The multidomain structure of Orc1p reveals similarity to regulators of DNA
RT replication and transcriptional silencing.";
RL Cell 83:563-568(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7579692; DOI=10.1091/mbc.6.6.741;
RA Loo S., Fox C.A., Rine J., Kobayashi R., Stillman B., Bell S.P.;
RT "The origin recognition complex in silencing, cell cycle progression, and
RT DNA replication.";
RL Mol. Biol. Cell 6:741-756(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP INTERACTION MCM10.
RX PubMed=11168584; DOI=10.1046/j.1365-2443.2000.00387.x;
RA Kawasaki Y., Hiraga S., Sugino A.;
RT "Interactions between Mcm10p and other replication factors are required for
RT proper initiation and elongation of chromosomal DNA replication in
RT Saccharomyces cerevisiae.";
RL Genes Cells 5:975-989(2000).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH TAH11.
RX PubMed=17825064; DOI=10.1111/j.1567-1364.2007.00299.x;
RA Asano T., Makise M., Takehara M., Mizushima T.;
RT "Interaction between ORC and Cdt1p of Saccharomyces cerevisiae.";
RL FEMS Yeast Res. 7:1256-1262(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Component of the origin recognition complex (ORC) that binds
CC origins of replication. It has a role in both chromosomal replication
CC and mating type transcriptional silencing. Binds to the ARS consensus
CC sequence (ACS) of origins of replication.
CC {ECO:0000269|PubMed:17825064}.
CC -!- SUBUNIT: Component of the origin recognition complex (ORC) composed of
CC at least ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. Interacts with MCM10
CC and TAH11. {ECO:0000269|PubMed:11168584, ECO:0000269|PubMed:17825064}.
CC -!- INTERACTION:
CC P54784; P54791: ORC4; NbExp=6; IntAct=EBI-12568, EBI-12580;
CC P54784; P38826: ORC6; NbExp=4; IntAct=EBI-12568, EBI-12588;
CC P54784; P21691: SIR1; NbExp=3; IntAct=EBI-12568, EBI-17211;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: The N-terminus is dedicated to mating-type repression.
CC -!- MISCELLANEOUS: Present with 3930 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ORC1 family. {ECO:0000305}.
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DR EMBL; U34860; AAB38248.1; -; Genomic_DNA.
DR EMBL; Z38114; CAA86256.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09832.1; -; Genomic_DNA.
DR PIR; S48333; S48333.
DR RefSeq; NP_013646.1; NM_001182424.1.
DR PDB; 1M4Z; X-ray; 2.20 A; A/B=1-235.
DR PDB; 1ZBX; X-ray; 2.50 A; A=1-219.
DR PDB; 1ZHI; X-ray; 2.70 A; A=1-219.
DR PDB; 5V8F; EM; 3.90 A; A=1-913.
DR PDB; 5ZR1; EM; 3.00 A; A=1-914.
DR PDB; 6OM3; X-ray; 3.30 A; K/L/W/X=2-214.
DR PDB; 6RQC; EM; 4.40 A; A=1-914.
DR PDB; 6WGC; EM; 4.30 A; A=1-913.
DR PDB; 6WGG; EM; 8.10 A; A=1-913.
DR PDB; 6WGI; EM; 10.00 A; A=1-913.
DR PDB; 7MCA; EM; 3.60 A; A=1-914.
DR PDBsum; 1M4Z; -.
DR PDBsum; 1ZBX; -.
DR PDBsum; 1ZHI; -.
DR PDBsum; 5V8F; -.
DR PDBsum; 5ZR1; -.
DR PDBsum; 6OM3; -.
DR PDBsum; 6RQC; -.
DR PDBsum; 6WGC; -.
DR PDBsum; 6WGG; -.
DR PDBsum; 6WGI; -.
DR PDBsum; 7MCA; -.
DR AlphaFoldDB; P54784; -.
DR SMR; P54784; -.
DR BioGRID; 35101; 665.
DR ComplexPortal; CPX-768; Nuclear origin recognition complex.
DR DIP; DIP-2284N; -.
DR IntAct; P54784; 37.
DR MINT; P54784; -.
DR STRING; 4932.YML065W; -.
DR iPTMnet; P54784; -.
DR MaxQB; P54784; -.
DR PaxDb; P54784; -.
DR PRIDE; P54784; -.
DR EnsemblFungi; YML065W_mRNA; YML065W; YML065W.
DR GeneID; 854937; -.
DR KEGG; sce:YML065W; -.
DR SGD; S000004530; ORC1.
DR VEuPathDB; FungiDB:YML065W; -.
DR eggNOG; KOG1514; Eukaryota.
DR GeneTree; ENSGT00530000063498; -.
DR HOGENOM; CLU_012774_1_1_1; -.
DR InParanoid; P54784; -.
DR OMA; YMIHEIR; -.
DR BioCyc; YEAST:G3O-32660-MON; -.
DR Reactome; R-SCE-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-SCE-68689; CDC6 association with the ORC:origin complex.
DR Reactome; R-SCE-68949; Orc1 removal from chromatin.
DR Reactome; R-SCE-68962; Activation of the pre-replicative complex.
DR EvolutionaryTrace; P54784; -.
DR PRO; PR:P54784; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P54784; protein.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IDA:SGD.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; IDA:SGD.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IDA:SGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IDA:SGD.
DR GO; GO:0006270; P:DNA replication initiation; IMP:SGD.
DR GO; GO:0043007; P:maintenance of rDNA; IDA:SGD.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IDA:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IDA:SGD.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041083; AAA_lid_10.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR020793; ORC1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10763:SF23; PTHR10763:SF23; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17872; AAA_lid_10; 1.
DR Pfam; PF01426; BAH; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00439; BAH; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51038; BAH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; DNA replication;
KW DNA-binding; Magnesium; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..914
FT /note="Origin recognition complex subunit 1"
FT /id="PRO_0000127074"
FT DOMAIN 48..188
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT REGION 218..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..296
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 435
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 479..487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 566
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 567
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 600
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 704
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 726..733
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:1M4Z"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:1M4Z"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1M4Z"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:1M4Z"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1M4Z"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:6OM3"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:1M4Z"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:1M4Z"
FT STRAND 65..76
FT /evidence="ECO:0007829|PDB:1M4Z"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:1M4Z"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:1M4Z"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1M4Z"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:1M4Z"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:1M4Z"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:1M4Z"
FT STRAND 131..141
FT /evidence="ECO:0007829|PDB:1M4Z"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1M4Z"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:1M4Z"
FT HELIX 155..161
FT /evidence="ECO:0007829|PDB:1M4Z"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:1M4Z"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1M4Z"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:1M4Z"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:1ZBX"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:1ZBX"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:1M4Z"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:1M4Z"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:5ZR1"
FT TURN 392..396
FT /evidence="ECO:0007829|PDB:5ZR1"
FT TURN 399..404
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 422..429
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 456..468
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 473..480
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 485..501
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 508..514
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 523..533
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 539..551
FT /evidence="ECO:0007829|PDB:5ZR1"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 560..566
FT /evidence="ECO:0007829|PDB:5ZR1"
FT TURN 568..571
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 572..574
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 579..584
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 585..587
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 593..598
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 604..608
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 611..617
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 620..624
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 629..636
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 638..640
FT /evidence="ECO:0007829|PDB:5ZR1"
FT TURN 641..645
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 646..651
FT /evidence="ECO:0007829|PDB:5ZR1"
FT TURN 652..654
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 677..684
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 686..697
FT /evidence="ECO:0007829|PDB:5ZR1"
FT TURN 698..700
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 703..725
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 770..773
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 775..786
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 790..794
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 799..814
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 818..821
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 822..835
FT /evidence="ECO:0007829|PDB:5ZR1"
FT TURN 836..838
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 840..845
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 847..850
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 853..857
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 866..875
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 878..881
FT /evidence="ECO:0007829|PDB:5ZR1"
FT TURN 887..889
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 891..896
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 899..905
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 909..913
FT /evidence="ECO:0007829|PDB:5ZR1"
SQ SEQUENCE 914 AA; 104400 MW; BDAA9D3E40B4B76A CRC64;
MAKTLKDLQG WEIITTDEQG NIIDGGQKRL RRRGAKTEHY LKRSSDGIKL GRGDSVVMHN
EAAGTYSVYM IQELRLNTLN NVVELWALTY LRWFEVNPLA HYRQFNPDAN ILNRPLNYYN
KLFSETANKN ELYLTAELAE LQLFNFIRVA NVMDGSKWEV LKGNVDPERD FTVRYICEPT
GEKFVDINIE DVKAYIKKVE PREAQEYLKD LTLPSKKKEI KRGPQKKDKA TQTAQISDAE
TRATDITDNE DGNEDESSDY ESPSDIDVSE DMDSGEISAD ELEEEEDEEE DEDEEEKEAR
HTNSPRKRGR KIKLGKDDID ASVQPPPKKR GRKPKDPSKP RQMLLISSCR ANNTPVIRKF
TKKNVARAKK KYTPFSKRFK SIAAIPDLTS LPEFYGNSSE LMASRFENKL KTTQKHQIVE
TIFSKVKKQL NSSYVKEEIL KSANFQDYLP ARENEFASIY LSAYSAIESD SATTIYVAGT
PGVGKTLTVR EVVKELLSSS AQREIPDFLY VEINGLKMVK PTDCYETLWN KVSGERLTWA
ASMESLEFYF KRVPKNKKKT IVVLLDELDA MVTKSQDIMY NFFNWTTYEN AKLIVIAVAN
TMDLPERQLG NKITSRIGFT RIMFTGYTHE ELKNIIDLRL KGLNDSFFYV DTKTGNAILI
DAAGNDTTVK QTLPEDVRKV RLRMSADAIE IASRKVASVS GDARRALKVC KRAAEIAEKH
YMAKHGYGYD GKTVIEDENE EQIYDDEDKD LIESNKAKDD NDDDDDNDGV QTVHITHVMK
ALNETLNSHV ITFMTRLSFT AKLFIYALLN LMKKNGSQEQ ELGDIVDEIK LLIEVNGSNK
FVMEIAKTLF QQGSDNISEQ LRIISWDFVL NQLLDAGILF KQTMKNDRIC CVKLNISVEE
AKRAMNEDET LRNL
