ORC1_ORYSJ
ID ORC1_ORYSJ Reviewed; 814 AA.
AC Q5SMU7; Q0DDZ5; Q9MB44;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Origin of replication complex subunit 1 {ECO:0000303|PubMed:10996242};
DE Short=OsORC1 {ECO:0000303|PubMed:10996242};
GN Name=ORC1 {ECO:0000303|PubMed:10996242};
GN OrderedLocusNames=Os06g0187000 {ECO:0000312|EMBL:BAF18928.1},
GN LOC_Os06g08790 {ECO:0000305};
GN ORFNames=OsJ_20389 {ECO:0000312|EMBL:EEE65230.1},
GN P0470C02.11 {ECO:0000312|EMBL:BAD72454.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY
RP SUCROSE.
RC STRAIN=cv. Nipponbare;
RX PubMed=10996242; DOI=10.1016/s0168-9452(00)00297-1;
RA Kimura S., Ishibashi T., Hatanaka M., Sakakibara Y., Hashimoto J.,
RA Sakaguchi K.;
RT "Molecular cloning and characterization of a plant homologue of the origin
RT recognition complex 1 (ORC1).";
RL Plant Sci. 158:33-39(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY SUCROSE, GENE
RP FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Nipponbare;
RX PubMed=15939553; DOI=10.1016/j.gene.2005.03.047;
RA Mori Y., Yamamoto T., Sakaguchi N., Ishibashi T., Furukawa T., Kadota Y.,
RA Kuchitsu K., Hashimoto J., Kimura S., Sakaguchi K.;
RT "Characterization of the origin recognition complex (ORC) from a higher
RT plant, rice (Oryza sativa L.).";
RL Gene 353:23-30(2005).
RN [8]
RP REVIEW ON THE CORE DNA REPLICATION MACHINERY.
RX PubMed=17556508; DOI=10.1104/pp.107.101105;
RA Shultz R.W., Tatineni V.M., Hanley-Bowdoin L., Thompson W.F.;
RT "Genome-wide analysis of the core DNA replication machinery in the higher
RT plants Arabidopsis and rice.";
RL Plant Physiol. 144:1697-1714(2007).
RN [9]
RP INDUCTION BY GAMMA IRRADIATION.
RX PubMed=25124817; DOI=10.1093/jhered/esu025;
RA Hayashi G., Shibato J., Imanaka T., Cho K., Kubo A., Kikuchi S., Satoh K.,
RA Kimura S., Ozawa S., Fukutani S., Endo S., Ichikawa K., Agrawal G.K.,
RA Shioda S., Fukumoto M., Rakwal R.;
RT "Unraveling low-level gamma radiation--responsive changes in expression of
RT early and late genes in leaves of rice seedlings at Iitate Village,
RT Fukushima.";
RL J. Hered. 105:723-738(2014).
CC -!- FUNCTION: Essential protein (By similarity). Component of the origin
CC recognition complex (ORC) that binds origins of replication. It has a
CC role in both chromosomal replication and mating type transcriptional
CC silencing. Binds to the ARS consensus sequence (ACS) of origins of
CC replication (By similarity). H3K4me3 effector that regulates positively
CC the transcription of a subset of genes (By similarity). Required for
CC cell proliferation (PubMed:10996242). {ECO:0000250|UniProtKB:P54784,
CC ECO:0000250|UniProtKB:Q710E8, ECO:0000303|PubMed:10996242}.
CC -!- SUBUNIT: Component of the origin recognition complex (ORC) composed of
CC at least ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a
CC cell-cycle and development dependent manner. It is sequentially
CC assembled at the exit from anaphase of mitosis and disassembled as
CC cells enter S phase (By similarity). Binds unmodified and methylated
CC histone H3 (By similarity). {ECO:0000250|UniProtKB:Q710E8,
CC ECO:0000250|UniProtKB:Q9SU24}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15939553}.
CC -!- TISSUE SPECIFICITY: Expressed strongly in root tips and shoot apical
CC meristem (SAM), and weakly in young leaves. Not detected in mature
CC leaves. {ECO:0000269|PubMed:10996242, ECO:0000269|PubMed:15939553}.
CC -!- INDUCTION: Reduced expression upon sucrose depletion-mediated cell
CC proliferation arrest, and accumulates after sucrose treatment
CC (PubMed:10996242, PubMed:15939553). Induced by gamma irradiation
CC (PubMed:25124817). {ECO:0000269|PubMed:10996242,
CC ECO:0000269|PubMed:15939553, ECO:0000269|PubMed:25124817}.
CC -!- SIMILARITY: Belongs to the ORC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA89785.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAF18928.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB037135; BAA89785.2; ALT_FRAME; mRNA.
DR EMBL; AP003508; BAD72454.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF18928.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000143; EEE65230.1; -; Genomic_DNA.
DR EMBL; AK103068; BAG95868.1; -; mRNA.
DR RefSeq; XP_015641584.1; XM_015786098.1.
DR AlphaFoldDB; Q5SMU7; -.
DR SMR; Q5SMU7; -.
DR STRING; 39947.Q5SMU7; -.
DR PaxDb; Q5SMU7; -.
DR PRIDE; Q5SMU7; -.
DR GeneID; 4340349; -.
DR KEGG; osa:4340349; -.
DR InParanoid; Q5SMU7; -.
DR OrthoDB; 935804at2759; -.
DR PlantReactome; R-OSA-9640882; Assembly of pre-replication complex.
DR PlantReactome; R-OSA-9645850; Activation of pre-replication complex.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:0009744; P:response to sucrose; IDA:UniProtKB.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.30.40.10; -; 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 InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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 Pfam; PF00628; PHD; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
KW Activator; ATP-binding; DNA replication; DNA-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..814
FT /note="Origin of replication complex subunit 1"
FT /id="PRO_0000431428"
FT DOMAIN 218..335
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT ZN_FING 160..209
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..181
FT /note="Histone H3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT REGION 197..201
FT /note="Histone H3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT REGION 310..315
FT /note="Histone H3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT REGION 339..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..804
FT /note="Necessary and sufficient for ORC complex assembly"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOTIF 105..112
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT BINDING 468..476
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 468..475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 558
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 559
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 559
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 592
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 657
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT CONFLICT 107..108
FT /note="Missing (in Ref. 1; BAA89785)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="T -> N (in Ref. 1; BAA89785)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="L -> I (in Ref. 1; BAA89785)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="P -> L (in Ref. 1; BAA89785)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="T -> N (in Ref. 1; BAA89785)"
FT /evidence="ECO:0000305"
FT CONFLICT 776
FT /note="L -> F (in Ref. 1; BAA89785)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 814 AA; 92054 MW; F3E4B562A04F13B0 CRC64;
MDLSATPSRS KSGLRSSPRK PVAAPAVAQM DLSTPSKPTP RRKPKAPPVA APMSPVTPSS
VRRSSRLLET PTKVTSETPV KPTPTPKRKR AAPSPSPKTP TQSEPKRQRQ RQRQRQQPKK
PKKRAYYRKV VYDGGEFAAG DDVYVKRRDG AESDAEDPEA EECRVCFRAG AAVMVECDVC
LGGFHLRCVR PPLRRVPEGD WACPYCEAER AGKAIERPKP PEGKRIVRTA KEKLLSSDLW
AARIESLWRE PDGIFWAKVR WYIIPEETAA GRQPHNLRRE LYRTNDLADI EMETILRHCY
VMSPKEFKDA SDQGDDVFYC EYEYDIHWHN FKRLADIDDE PETKEDPGDE PYNAGNDYVS
DSDEDSEYDE EEEPTKCSSA RTHQSHALAA NLRKGRTYGL QKIGIRKIPE HVRCHQKTNL
EKAKATLLLA TLPKSLPCRD KEMEEISAFV KDAICNDQCL GRCLYIHGVP GTGKTMSVLA
VMRRLRSELD SGNLRPYSFI EINGLKLASP ENIYKVIYEQ LSGHRVGWKK ALHYLTEHFS
GGTKIGKQAN QPIILLIDEL DLLLTRNQSV LYNILDWPTR PNSNLVVIGI ANTMDLPEKL
LPRISSRMGI QRLCFGPYNY RQLQEIITSR LKGIDAFEDQ AIEFASRKVA AMSGDARRAL
EICRRAAEFA DYRVKQSGHT SVNRGKNVVC MGDIEAAIQE VFQAPHIQVM KNCPKFGKII
LVAMVHELYR SGLGEVMFDK LAATVLSWCH VNRELLPGYD TLLKICCKLG EGKIILCEEG
TKHKLQKLQL NYPSDDVTFA LKESPDIPWL SKYL
