ORC1_DROME
ID ORC1_DROME Reviewed; 924 AA.
AC O16810; Q9V4N1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Origin recognition complex subunit 1;
DE Short=DmORC1;
GN Name=Orc1; ORFNames=CG10667;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=9363940; DOI=10.1016/s0092-8674(00)80415-8;
RA Pak D.T.S., Pflumm M., Chesnokov I., Huang D.W., Kellum R., Marr J.,
RA Romanowski P., Botchan M.R.;
RT "Association of the origin recognition complex with heterochromatin and HP1
RT in higher eukaryotes.";
RL Cell 91:311-323(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; THR-419; SER-426;
RP SER-430 AND SER-533, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Component of the origin recognition complex (ORC) that binds
CC origins of replication. DNA-binding is ATP-dependent, however specific
CC DNA sequences that define origins of replication have not been
CC identified so far. ORC is required to assemble the pre-replication
CC complex necessary to initiate DNA replication.
CC {ECO:0000269|PubMed:9363940}.
CC -!- SUBUNIT: ORC is composed of six subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ORC1 family. {ECO:0000305}.
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DR EMBL; AF017647; AAC47802.1; -; mRNA.
DR EMBL; AE013599; AAF59236.1; -; Genomic_DNA.
DR EMBL; AY094780; AAM11133.1; -; mRNA.
DR RefSeq; NP_477303.1; NM_057955.4.
DR PDB; 4XGC; X-ray; 3.50 A; A=533-924.
DR PDB; 7JGR; EM; 3.90 A; A=440-924.
DR PDB; 7JGS; EM; 3.20 A; A=440-924.
DR PDB; 7JK2; EM; 3.20 A; A=440-924.
DR PDB; 7JK3; EM; 3.40 A; A=440-924.
DR PDB; 7JK4; EM; 3.40 A; A=440-924.
DR PDB; 7JK5; EM; 3.90 A; A=440-924.
DR PDB; 7JK6; EM; 4.00 A; A=440-924.
DR PDBsum; 4XGC; -.
DR PDBsum; 7JGR; -.
DR PDBsum; 7JGS; -.
DR PDBsum; 7JK2; -.
DR PDBsum; 7JK3; -.
DR PDBsum; 7JK4; -.
DR PDBsum; 7JK5; -.
DR PDBsum; 7JK6; -.
DR AlphaFoldDB; O16810; -.
DR SMR; O16810; -.
DR BioGRID; 61562; 13.
DR DIP; DIP-59662N; -.
DR IntAct; O16810; 8.
DR MINT; O16810; -.
DR STRING; 7227.FBpp0088033; -.
DR iPTMnet; O16810; -.
DR PaxDb; O16810; -.
DR PRIDE; O16810; -.
DR DNASU; 35686; -.
DR EnsemblMetazoa; FBtr0088959; FBpp0088033; FBgn0286788.
DR GeneID; 35686; -.
DR KEGG; dme:Dmel_CG10667; -.
DR CTD; 4998; -.
DR FlyBase; FBgn0286788; Orc1.
DR VEuPathDB; VectorBase:FBgn0286788; -.
DR eggNOG; KOG1514; Eukaryota.
DR GeneTree; ENSGT00530000063498; -.
DR HOGENOM; CLU_012774_0_1_1; -.
DR InParanoid; O16810; -.
DR OMA; KTPSNDM; -.
DR OrthoDB; 935804at2759; -.
DR PhylomeDB; O16810; -.
DR Reactome; R-DME-176187; Activation of ATR in response to replication stress.
DR Reactome; R-DME-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-DME-68689; CDC6 association with the ORC:origin complex.
DR Reactome; R-DME-68949; Orc1 removal from chromatin.
DR Reactome; R-DME-68962; Activation of the pre-replicative complex.
DR SignaLink; O16810; -.
DR BioGRID-ORCS; 35686; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 35686; -.
DR PRO; PR:O16810; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0286788; Expressed in egg cell and 20 other tissues.
DR Genevisible; O16810; DM.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; IDA:FlyBase.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006277; P:DNA amplification; IMP:FlyBase.
DR GO; GO:0006270; P:DNA replication initiation; IDA:FlyBase.
DR CDD; cd08768; Cdc6_C; 1.
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; IPR015163; Cdc6_C.
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 Pfam; PF09079; Cdc6_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM01074; Cdc6_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51038; BAH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA replication; DNA-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..924
FT /note="Origin recognition complex subunit 1"
FT /id="PRO_0000127069"
FT DOMAIN 45..187
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT REGION 196..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 564
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 598..606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 684
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 685
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 685
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 718
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 784
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 419
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 159
FT /note="A -> S (in Ref. 1; AAC47802)"
FT /evidence="ECO:0000305"
FT HELIX 520..528
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 546..548
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 551..558
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 572..588
FT /evidence="ECO:0007829|PDB:7JGS"
FT STRAND 592..599
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 600..602
FT /evidence="ECO:0007829|PDB:4XGC"
FT HELIX 604..620
FT /evidence="ECO:0007829|PDB:7JGS"
FT STRAND 627..633
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 634..636
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 640..642
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 643..649
FT /evidence="ECO:0007829|PDB:7JGS"
FT TURN 650..652
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 658..669
FT /evidence="ECO:0007829|PDB:7JGS"
FT STRAND 678..684
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 686..689
FT /evidence="ECO:0007829|PDB:7JGS"
FT TURN 691..693
FT /evidence="ECO:0007829|PDB:7JK4"
FT HELIX 696..702
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 703..705
FT /evidence="ECO:0007829|PDB:7JGS"
FT STRAND 706..708
FT /evidence="ECO:0007829|PDB:7JK3"
FT STRAND 711..718
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 722..725
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 729..735
FT /evidence="ECO:0007829|PDB:7JGS"
FT STRAND 739..742
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 747..758
FT /evidence="ECO:0007829|PDB:7JGS"
FT STRAND 762..764
FT /evidence="ECO:0007829|PDB:7JK3"
FT HELIX 766..776
FT /evidence="ECO:0007829|PDB:7JGS"
FT TURN 777..780
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 783..799
FT /evidence="ECO:0007829|PDB:7JGS"
FT STRAND 803..805
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 807..817
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 823..827
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 831..847
FT /evidence="ECO:0007829|PDB:7JGS"
FT STRAND 848..850
FT /evidence="ECO:0007829|PDB:7JK3"
FT HELIX 854..868
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 875..887
FT /evidence="ECO:0007829|PDB:7JGS"
FT STRAND 890..892
FT /evidence="ECO:0007829|PDB:7JGS"
FT TURN 899..901
FT /evidence="ECO:0007829|PDB:7JGS"
FT STRAND 903..906
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 910..917
FT /evidence="ECO:0007829|PDB:7JGS"
SQ SEQUENCE 924 AA; 103281 MW; AACD002DEB10A136 CRC64;
MVNKENARSV GQQVKWIGSQ DELPPVKNLE HKNVYFYQKC IYGPLTLSVG DFILVSNADA
AEPDTVSGCD VARILHMYEL RELTDREPCR AIVQWYSWPK AIPHNKYDDD EVAIDFSLEV
IEEHRPYDND VALGAIYRKC IVLEGTSKTS AEEILKRHAN KLKSTACPMF VSRYRFVKVK
RSYRLIPLEI HLEQPEDNAR PTRSSRKSLT AHRESKRSIS ARHDDTAGNK GSSVEKRRRA
SMAASSSVEF IDVNSFICEN KVSPIKIVGG RSVVRLSEKK NAPEINANYL PASPLTEKNA
KVETPKSRAS AARRNLNLSL DRGADTTADS DCLNYSIVQQ TPDPKTPSND MKIKLRLSER
RRSVRLASMD VDPLSLEEAV QEPNAQGRKR LGVANGDIYH TPTKKSKEPL ESAAATEQTP
STRRKSILKS ATSRLAEGTP RRSIHLSNIV EQRVFEDDEI ISTPKRGRSK KTVQDNDEDY
SPKKSVQKTP TRTRRSSTTT KTATTPSKGI TTATATPMTP SQKMKKIRAG ELSPSMQQRT
DLPAKDSSKS ELQLAREQLH VSVVPKSLPC REREFENIYA FLEGKIQDQC GGCMYVSGVP
GTGKTATVTG VIRTLQRMAK QNELPAFEYL EINGMRLTEP RQAYVQIYKQ LTGKTVSWEQ
AHALLEKRFT TPAPRRVTTV LLVDELDILC NRRQDVVYNL LDWPTKSAAK LVVVTIANTM
DLPERLLMGK VTSRLGLTRL TFQPYSHKQL QEIVTARLGG SETFKGEAVQ LVARKVAAVS
GDARRALDIC RRATEIADTA AVKCVTMLHV QQALAEMIAS AKVQAIRNCS RMEQIFLQAI
AAEVTRTGVE ETTFMGVYQQ VETIAAFMGV TFPPPGRALR LCSKLGAERL IISEHSRNDL
FQKILLNVSA DDIHYALRVE EMVN
