ORC1_CRIGR
ID ORC1_CRIGR Reviewed; 850 AA.
AC Q9JI69;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Origin recognition complex subunit 1;
GN Name=ORC1; Synonyms=ORC1L;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10835370; DOI=10.1093/emboj/19.11.2728;
RA Natale D.A., Li C.-J., Sun W.-H., DePamphilis M.L.;
RT "Selective instability of Orc1 protein accounts for the absence of
RT functional origin recognition complexes during the M-G1 transition in
RT mammals.";
RL EMBO J. 19:2728-2738(2000).
CC -!- FUNCTION: Component of the origin recognition complex (ORC) that binds
CC origins of replication. DNA-binding is ATP-dependent. The specific DNA
CC sequences that define origins of replication have not been identified
CC yet. ORC is required to assemble the pre-replication complex necessary
CC to initiate DNA replication (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of ORC, a complex composed of at least 6 subunits:
CC ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle
CC dependent manner. It is sequentially assembled at the exit from
CC anaphase of mitosis and disassembled as cells enter S phase (By
CC similarity). Interacts with CDC6 and KAT7/HBO1 (By similarity).
CC Interacts with LRWD1 predominantly during the G1 phase and with less
CC affinity during mitosis, when phosphorylated (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: The BAH domain mediates binding to dimethylated histone H4
CC 'Lys-20' (H4K20me2), which is enriched at replication origins.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ORC1 family. {ECO:0000305}.
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DR EMBL; AF254572; AAF66067.1; -; mRNA.
DR RefSeq; NP_001233617.1; NM_001246688.1.
DR AlphaFoldDB; Q9JI69; -.
DR SMR; Q9JI69; -.
DR STRING; 10029.NP_001233617.1; -.
DR GeneID; 100689425; -.
DR KEGG; cge:100689425; -.
DR CTD; 4998; -.
DR eggNOG; KOG1514; Eukaryota.
DR OrthoDB; 935804at2759; -.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; ISS: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:0006260; P:DNA replication; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW ATP-binding; DNA replication; DNA-binding; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein.
FT CHAIN 1..850
FT /note="Origin recognition complex subunit 1"
FT /id="PRO_0000127066"
FT DOMAIN 45..171
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT REGION 209..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..419
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 523..531
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 609
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 610
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 610
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 643
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 709
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT SITE 94
FT /note="Histone H4K20me2 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N2"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N2"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
SQ SEQUENCE 850 AA; 95954 MW; 6E7F858130F7E7E2 CRC64;
MPSYLTRQKT RKIFSWVGRP LPDRKHNHQI YKEMRMKVND CSTEIHIKVG QFVLIKGNNN
AKPYVAKLIE LFEDGSKFHS KKCARVQWCV RFSEIPISKR HLLGRKPAAQ EIFWYDDPDC
GNNICVETII GPVQVVALAP DEVIPMDQKS EDTLFVKLSW NTKNFEPLSP EVLAALKKLE
DSPKCQKPLE GKSKNVKNPS WNATEQMVKR IESSHSTSKS CQTSAHPVSP NARKPLELSD
SDIPRKPNMR LSQKILCDSL DSQKNSKRKT AFSETASPPK RCQPGEIKNL SPLKTLEKNG
QAHSFCDKGS MILRAQDPSF ITTKISMERA LDPVRSRLRP SVMLTSILTP KRTGREAGKQ
EAHTEPTRTS HRVHRRSSLL TLNRIRQQLW LLDDDKSDQE EEESISSAEV SDSTSEEEDD
SIPSLLKRNS QPQSRNRRMA SKPSLQTPSK TPKKTTHHPT PQIRGRNIAV QEPTSVLEEA
RLMLHVSAVP DSLPCREQEF QDIYSFVESK LLDGTGGCMY ISGVPGTGKT ATVNEVIRCL
QQAAQTNDVP PFEYVDVNGM KLTEPHQVYV QILQKLTGQK ATANHAAQLL AKRFCSQGSQ
QETTVLLVDE LDLLWTSKQD VMYNLFDWPT HKGARLIVLA IANTMDLPER IMMNRVSSRL
GLTRMSFQPY SHNQLKEILV SRLKHLKAFE DDAIQLVARK VAALSGDARR CLDICRRATE
ICELSHNHGN SLGPVTVSHL MEAIDEMFSS SYITAIKNCS LLEQGFLRAI IAEFRRSGLE
EATFQQIYSQ HVALCRMEGL PYPTMSETMA VCSNLGSCRL LLVEPSRNDL LLRVRLNVSQ
DDVLYALKEE
