ORC1_SCHPO
ID ORC1_SCHPO Reviewed; 707 AA.
AC P54789;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Origin recognition complex subunit 1;
GN Name=orc1; Synonyms=orp1 {ECO:0000303|PubMed:15314153};
GN ORFNames=SPBC29A10.15;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7502077; DOI=10.1126/science.270.5242.1667;
RA Gavin K.A., Hidaka M., Stillman B.D.;
RT "Conserved initiator proteins in eukaryotes.";
RL Science 270:1667-1671(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=8618924; DOI=10.1073/pnas.92.26.12475;
RA Muzi-Falconi M., Kelly T.J.;
RT "Orp1, a member of the Cdc18/Cdc6 family of S-phase regulators, is
RT homologous to a component of the origin recognition complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:12475-12479(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP SUBUNIT.
RX PubMed=10535928; DOI=10.1073/pnas.96.22.12367;
RA Moon K.-Y., Kong D., Lee J.-K., Raychaudhuri S., Hurwitz J.;
RT "Identification and reconstitution of the origin recognition complex from
RT Schizosaccharomyces pombe.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:12367-12372(1999).
RN [5]
RP CHARACTERIZATION OF ORC, AND INTERACTION WITH CDC18.
RX PubMed=11850415; DOI=10.1074/jbc.m107710200;
RA Chuang R.-Y., Chretien L., Dai J., Kelly T.J.;
RT "Purification and characterization of the Schizosaccharomyces pombe origin
RT recognition complex: interaction with origin DNA and Cdc18 protein.";
RL J. Biol. Chem. 277:16920-16927(2002).
RN [6]
RP INTERACTION WITH SPB70, AND SUBCELLULAR LOCATION.
RX PubMed=15314153; DOI=10.1128/mcb.24.17.7419-7434.2004;
RA Uchiyama M., Wang T.S.;
RT "The B-subunit of DNA polymerase alpha-primase associates with the origin
RT recognition complex for initiation of DNA replication.";
RL Mol. Cell. Biol. 24:7419-7434(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291; THR-292 AND SER-320, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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. ORC binds to multiple sites
CC within the ars1 origin of DNA replication in an ATP-independent manner.
CC -!- SUBUNIT: ORC is composed of six subunits. ORC interacts with cdc18,
CC recruiting it to the ars1 origin of replication (PubMed:10535928,
CC PubMed:11850415). Interacts with sbp70 (PubMed:15314153).
CC {ECO:0000269|PubMed:10535928, ECO:0000269|PubMed:11850415,
CC ECO:0000269|PubMed:15314153}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15314153}. Chromosome
CC {ECO:0000269|PubMed:15314153}.
CC -!- DEVELOPMENTAL STAGE: Expressed constitutively during the cell cycle.
CC -!- SIMILARITY: Belongs to the ORC1 family. {ECO:0000305}.
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DR EMBL; U40378; AAC49141.1; -; mRNA.
DR EMBL; U43392; AAB38247.1; -; Genomic_DNA.
DR EMBL; U38522; AAC49129.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA22443.1; -; Genomic_DNA.
DR PIR; T40070; T40070.
DR RefSeq; NP_596060.1; NM_001021971.2.
DR AlphaFoldDB; P54789; -.
DR SMR; P54789; -.
DR BioGRID; 276998; 38.
DR STRING; 4896.SPBC29A10.15.1; -.
DR iPTMnet; P54789; -.
DR MaxQB; P54789; -.
DR PaxDb; P54789; -.
DR PRIDE; P54789; -.
DR EnsemblFungi; SPBC29A10.15.1; SPBC29A10.15.1:pep; SPBC29A10.15.
DR GeneID; 2540470; -.
DR KEGG; spo:SPBC29A10.15; -.
DR PomBase; SPBC29A10.15; orc1.
DR VEuPathDB; FungiDB:SPBC29A10.15; -.
DR eggNOG; KOG1514; Eukaryota.
DR HOGENOM; CLU_012774_1_1_1; -.
DR InParanoid; P54789; -.
DR OMA; PWEWIYE; -.
DR PhylomeDB; P54789; -.
DR Reactome; R-SPO-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SPO-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-SPO-68689; CDC6 association with the ORC:origin complex.
DR Reactome; R-SPO-68949; Orc1 removal from chromatin.
DR Reactome; R-SPO-68962; Activation of the pre-replicative complex.
DR PRO; PR:P54789; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IC:PomBase.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; IDA:UniProtKB.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IC:PomBase.
DR GO; GO:0043596; C:nuclear replication fork; IC:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:UniProtKB.
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:1902969; P:mitotic DNA replication; IMP:PomBase.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IGI:PomBase.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IC:PomBase.
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 ATP-binding; Chromosome; DNA replication; DNA-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..707
FT /note="Origin recognition complex subunit 1"
FT /id="PRO_0000127073"
FT DOMAIN 62..193
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT REGION 216..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 334
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 368..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 454
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 455
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 488
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 292
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 707 AA; 80514 MW; D056018159A40A44 CRC64;
MPRRKSLRSQ LLINGIDKSL LSDDSADSSD IDEEEVYGVW TEEPFQKEAG RSYYRSLKKN
DVIYRVGDDI TVHDGDSSFY LGVICKLYEK AIDKHSGKKY VEAIWYSRAY AKRMEIKPEY
LLPDRHINEV YVSCGRDENL TSCIIEHCNV YSEAEFFSKF PAGIPTKRKD LFPCNFFIRR
GVHLKVNKYT EPLDWSYYAH NLERIEDLLV EMEENLRPTK KKSGSRGRGR PRKYPLPNVE
SKESSSKVNS KDENFDLQDD SESSEDNLTI QPQTPRRRHK RSRHNSSNLA STPKRNGYKQ
PLQITPLPIR MLSLEEFQGS PHRKARAMLH VASVPSTLQC RDNEFSTIFS NLESAIEEET
GACLYISGTP GTGKTATVHE VIWNLQELSR EGQLPEFSFC EINGMRVTSA NQAYSILWES
LTGERVTPIH AMDLLDNRFT HASPNRSSCV VLMDELDQLV THNQKVLYNF FNWPSLPHSR
LIVVAVANTM DLPERILSNR ISSRLGLSRV PFEPYTHTQL EIIIAARLEA VRDDDVFSSD
AIRFAARKVA AVSGDARRAL DICRRASELA ENKNGKVTPG LIHQAISEMT ASPLQKVLRN
LSFMQKVFLC AIVNRMRRSG FAESYVYEVL EEAERLLRVM TTPDAEAKFG ELILRRPEFG
YVLSSLSENG VLYLENKSSR NARVRLAIAD DEIKLAFRGD SELAGIA
