ORC1_BOVIN
ID ORC1_BOVIN Reviewed; 863 AA.
AC Q58DC8; A2VDN4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Origin recognition complex subunit 1;
GN Name=ORC1; Synonyms=ORC1L;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ORC1 family. {ECO:0000305}.
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DR EMBL; BT021669; AAX46516.1; -; mRNA.
DR EMBL; BC133326; AAI33327.1; -; mRNA.
DR RefSeq; NP_001014918.1; NM_001014918.1.
DR RefSeq; XP_015320898.1; XM_015465412.1.
DR AlphaFoldDB; Q58DC8; -.
DR SMR; Q58DC8; -.
DR DIP; DIP-59665N; -.
DR STRING; 9913.ENSBTAP00000003523; -.
DR PaxDb; Q58DC8; -.
DR PRIDE; Q58DC8; -.
DR GeneID; 513523; -.
DR KEGG; bta:513523; -.
DR CTD; 4998; -.
DR eggNOG; KOG1514; Eukaryota.
DR HOGENOM; CLU_012774_0_1_1; -.
DR InParanoid; Q58DC8; -.
DR OrthoDB; 935804at2759; -.
DR Proteomes; UP000009136; Unplaced.
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 Acetylation; ATP-binding; DNA replication; DNA-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..863
FT /note="Origin recognition complex subunit 1"
FT /id="PRO_0000245347"
FT DOMAIN 45..171
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT REGION 186..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..863
FT /note="Necessary and sufficient for ORC complex assembly"
FT /evidence="ECO:0000250"
FT COMPBIAS 192..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..427
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 502
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 536..544
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 622
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 623
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 623
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 656
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 722
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 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N2"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N2"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOD_RES 329
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT CONFLICT 40
FT /note="D -> G (in Ref. 2; AAI33327)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="D -> E (in Ref. 1; AAX46516)"
FT /evidence="ECO:0000305"
FT CONFLICT 774
FT /note="V -> F (in Ref. 2; AAI33327)"
FT /evidence="ECO:0000305"
FT CONFLICT 862..863
FT /note="EE -> RSEGLHKEG (in Ref. 1; AAX46516)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 863 AA; 97902 MW; 20A99FFE86AE1B47 CRC64;
MAYYSARLRT RQTYSWVGRP LLDQKLHYQT YKEMSMKRED YSTEIHIQVG QFVLIEGDDD
ENPYVAKLVE LFEDDSELYS KKRARVQWFI RFCEVPVCKQ HLLGRKPGTQ EIFWYDNPTC
NSNISVETII GSVRVVALAP DEVMPIDLKN KKTFFVKLSW NEKKFKPLPP EVFAQLNKLQ
EDNHRYQKPM QAKTKSAESP SWTTTEHAVK RIESRHSTSK SRHTASHPVT PRARKRLELS
SFPRTPNTRI SPAASCASLD SPGRMKRKVA FSEVMSPSKR SLPDGFQTSS PALKAPEKTG
EIQHSCTKDA KKTSPDHGMI LRARAPALKI TETSEERTLT PIGGGRKSSV VPSVILKPEY
IKRREGKEPE VQDEAPSTSR IRRKSSVLTL NRIRQQLRFL GNSKSDENDE EFLPAAEISD
CDSEEEEAST TPLPRRTPNS VSRNLRSSMK SSLQTPSKTP KKTPEPRTPR DATPRIRSRN
LTAQGPTNML EEARLRLHVA AVPESLPCRE QEFQDIYNFV ESKLLDQTGG CMYISGVPGT
GKTATVHEVI CCLQQAAQAN EVPPFQYIEV NGMKLTEPHQ VYVQILQKLT GKRATANHAA
ALLAKRFCTQ GSSQETTVLL VDELDLLWTQ KQDVMYNLFD WPTHKEARLV VLTIANTMDL
PERIMMNRVS SRLGLTRMCF QPYTHSQLRQ ILLSRLRHVK AFEDDAIQLV ARKVAALSGD
ARRCLDICRR ATEICEFSCQ KPDSPGLVTT AHLLEAIDEM FSSSYITAIK NSSVLEQSFL
RAILAEFRRS GLEEATFQQV YIQHVALCRM EGLPYPTMSE TMAVCSRLGA CRLLLVEPSR
NDVLRRVRLN VSQDDVLYAL KEE
