ID I1MDB1_SOYBN Unreviewed; 854 AA.
AC I1MDB1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Origin recognition complex subunit 1 {ECO:0000256|RuleBase:RU365058};
GN Name=100814940 {ECO:0000313|EnsemblPlants:KRH10202};
GN ORFNames=GLYMA_15G034300 {ECO:0000313|EMBL:KRH10202.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH10202.1};
RN [1] {ECO:0000313|EMBL:KRH10202.1, ECO:0000313|EnsemblPlants:KRH10202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH10202};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH10202.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH10202}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH10202};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH10202.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH10202.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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, 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:0000256|RuleBase:RU365058}.
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. Binds unmodified and methylated histone H3.
CC {ECO:0000256|RuleBase:RU365058}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365058}.
CC -!- SIMILARITY: Belongs to the ORC1 family. {ECO:0000256|ARBA:ARBA00008398,
CC ECO:0000256|RuleBase:RU365058}.
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DR EMBL; CM000848; KRH10202.1; -; Genomic_DNA.
DR RefSeq; XP_006597259.1; XM_006597196.2.
DR AlphaFoldDB; I1MDB1; -.
DR SMR; I1MDB1; -.
DR STRING; 3847.I1MDB1; -.
DR PaxDb; 3847-GLYMA15G03900-1; -.
DR EnsemblPlants; KRH10202; KRH10202; GLYMA_15G034300.
DR GeneID; 100814940; -.
DR Gramene; KRH10202; KRH10202; GLYMA_15G034300.
DR KEGG; gmx:100814940; -.
DR eggNOG; KOG1514; Eukaryota.
DR HOGENOM; CLU_010923_0_0_1; -.
DR InParanoid; I1MDB1; -.
DR OMA; EGDWICH; -.
DR OrthoDB; 118994at2759; -.
DR Proteomes; UP000008827; Chromosome 15.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IBA:GO_Central.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; 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; CELL DIVISION CONTROL PROTEIN 6-RELATED; 1.
DR PANTHER; PTHR10763:SF23; ORIGIN RECOGNITION COMPLEX SUBUNIT 1; 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; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU365058};
KW DNA replication {ECO:0000256|RuleBase:RU365058};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU365058};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU365058};
KW Nucleus {ECO:0000256|RuleBase:RU365058};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 198..247
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 257..373
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..405
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 96986 MW; 913EFD07FFB2CAC8 CRC64;
MAATPSKFLQ TPSKPKLRSQ SNPKSSPVVT PDTPQTLYPR RSTRAKSLLF DAPKPPHTPL
EISLTTPKRR IRRSIDCVDQ DSGEDKATTS KISDKNKAPV VDASKKKKNG KNSIEVSFAP
VTPASSEKAS TRKREGEGGV VTRAKRRKSE NREKSAKLPQ RRVYYTKVVY DGGEFELGDD
VYVKRREDAS SDDEDPEMEE CRMCFSSNDE VMIECDDCLG GFHLKCLRPP LKDVPEGDWI
CGFCEARKMG MEVQLPKPPK GKKLVRTMRE KLLSSDLWSG RIKSIWREVD DNYWCRVRWY
TIPEETSVGR QPHNLRRELY RTNDFADIEM ESVLRHCHVM TPKEYAKASD EGDDVFLCEY
EYDIHWHSFK RLADIDNETE NGEEHDSDED WNVDKESDSD TDEDVEYEKE NIKNTQSKPS
TSHHLAANLQ KGQFFGLQKI GTKTIPQHVR SHKQTDLERA KATLLLASLP KSLPCRNKEM
EEITAFINGA LSDNQCLGRC LYIHGVPGTG KTMSVLSVMR SLKSEVDAGN IKPYTFVEIN
GLKLASPENI YKVIYEALNG HRVSWKKALH LLNERFVEGK KTRDEADRPC ILLIDELDLL
VTRNQSVLYN ILDWPTKPHS KLIVIGIANT MDLPEKLLPR ISSRMGIQRL CFGPYNYQQL
QEIISSRLKG IDVFEKQAVE FASRKVAAIS GDARRALEIC RRAAEIADYR MKKLISNPDC
VTAGKGLVGM VDVEAAIQEM FQAPHIQMMK SCSRVSKILL TAMVHELYNT GMGETTFEKL
AMRVSCFCTS NGEVFPGYDT LLQVGCRLGE CRIILCEAGA KHRWQKLQLN FPSDDVAFAL
RDCKDLPWLS KYLM
//