GenomeNet

Database: UniProt
Entry: I1MDB1_SOYBN
LinkDB: I1MDB1_SOYBN
Original site: I1MDB1_SOYBN 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system