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Database: UniProt
Entry: B8B3M1_ORYSI
LinkDB: B8B3M1_ORYSI
Original site: B8B3M1_ORYSI 
ID   B8B3M1_ORYSI            Unreviewed;      1043 AA.
AC   B8B3M1;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Origin recognition complex subunit 1 {ECO:0000256|RuleBase:RU365058};
GN   ORFNames=OsI_21955 {ECO:0000313|EMBL:EEC80150.1};
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946 {ECO:0000313|EMBL:EEC80150.1, ECO:0000313|Proteomes:UP000007015};
RN   [1] {ECO:0000313|EMBL:EEC80150.1, ECO:0000313|Proteomes:UP000007015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015};
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA   Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA   Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA   Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J.,
RA   Samudrala R., Wang J., Wong G.K., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(2),N(7)-dimethyl 5'-triphosphoguanosine)-
CC         ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end
CC         (N(2),N(2),N(7)-trimethyl 5'-triphosphoguanosine)-(ribonucleoside) in
CC         mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67624,
CC         Rhea:RHEA-COMP:17171, Rhea:RHEA-COMP:17315, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:167623,
CC         ChEBI:CHEBI:172880; Evidence={ECO:0000256|ARBA:ARBA00024488};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67625;
CC         Evidence={ECO:0000256|ARBA:ARBA00024488};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC         in mRNA + S-adenosyl-L-methionine = a 5'-end (N(2),N(7)-dimethyl 5'-
CC         triphosphoguanosine)-ribonucleoside in mRNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:67620, Rhea:RHEA-COMP:17167, Rhea:RHEA-
CC         COMP:17315, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:156461, ChEBI:CHEBI:172880;
CC         Evidence={ECO:0000256|ARBA:ARBA00024618};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67621;
CC         Evidence={ECO:0000256|ARBA:ARBA00024618};
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.
CC       {ECO:0000256|RuleBase:RU365058}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       Trimethylguanosine synthase family. {ECO:0000256|ARBA:ARBA00025783}.
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DR   EMBL; CM000131; EEC80150.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8B3M1; -.
DR   STRING; 39946.B8B3M1; -.
DR   EnsemblPlants; BGIOSGA022441-TA; BGIOSGA022441-PA; BGIOSGA022441.
DR   Gramene; BGIOSGA022441-TA; BGIOSGA022441-PA; BGIOSGA022441.
DR   HOGENOM; CLU_010923_0_0_1; -.
DR   OMA; CPKFGKI; -.
DR   Proteomes; UP000007015; Chromosome 6.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009452; P:7-methylguanosine RNA capping; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
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; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR041083; AAA_lid_10.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR043151; BAH_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR019012; RNA_cap_Gua-N2-MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR10763; CELL DIVISION CONTROL PROTEIN 6-RELATED; 1.
DR   PANTHER; PTHR10763:SF23; ORIGIN RECOGNITION COMPLEX SUBUNIT 1; 1.
DR   Pfam; PF17872; AAA_lid_10; 1.
DR   Pfam; PF01426; BAH; 1.
DR   Pfam; PF09445; Methyltransf_15; 1.
DR   SMART; SM00439; BAH; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51038; BAH; 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   Nucleotide-binding {ECO:0000256|RuleBase:RU365058};
KW   Nucleus {ECO:0000256|RuleBase:RU365058};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007015}.
FT   DOMAIN          129..270
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   REGION          1..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          783..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..54
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        816..831
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1043 AA;  116672 MW;  B0928245C50E303E CRC64;
     MDLSATPSRS KSGLRSSPRK PAAAPAVAQM DLSTPSKPTP KRKPKAPPVA APMSPATPSS
     VRRSSRLLET PTKVTSEAPV KPTPTPKRKR AAPSPSPKTP TQSEPKRQRQ QPKKPKKRAH
     YRKVVYDGGE FAAGDDVYVK RRDGAESDAE DPEAEECRVC FRAGAAVMVE CDVCLGGFHL
     RLWREPDGIF WAKVRWYIIP EETAAGRQPH NLRRELYRTN DLADIEMETI LRHCYVMSPK
     EFKDASDQGD DVFYCEYEYD IHWHNFKRLA DIDDEPETKE DPGDEPYNAG NDYVSDSDED
     SEYDEEEEPT KCGSARTHQS HVLAANLRKG RTYGLQKIGI RKIPEHVRCH QKTNLEKAKA
     TLLLATLPKS LPCRDKEMEE ISAFVKDAIC NDQCLGRCLY IHGVPGTGKT MSVLAVMRRL
     RSELDSGNLR PYSFIEINGL KLASPENIYK VIYEQLSGHR VLYNILDWPT RPNSNLVVIG
     IANTMDLPEK LLPRISSRMG IQRLCFGPYN YRQLQEIITS RLKGIDAFED QAIEFASRKV
     AAMSGDARRA LEICRRAAEF ADYRVKQSGH TSVNRGKNVV CMGDIEAAIQ EVFQAPHIQV
     MKNCPKFGKI ILVAMVHELY RSGLGEVMFD KLAATVLSWC HVNRELLPGY DTLLKICCKL
     SESKIILCEE GTKHKLQKLQ LNYPSDDVTF ALKESPDIPW LSKTLPNSRG ILMFPSLRLE
     FTRALSFGPI AFLSPPASPL PMANASATRK THRRRRRRVT FLARTCHRLL RFLATRRLRR
     RGHGLNSISA GDSPPSGQPP RGRDAEEAEA TQSAAAAQRR HEERHGDDAA ATEEAAVAGK
     YWAQRRSLFS LYDRGVRMDA EGWYSATPEP IAAAQAARAP PGSLVLDAFA GVGGNSIQGC
     YVVAVEIDPR KVELAAHNAR IYGVDDMIEF VVADFFHLAP SLKADLVFLS PPWGGPSYSQ
     AQVYSLDMLK PRDGFTIFQA AQEISPNIIM FLPRNVDLSQ VEQLSWLSSP PLDFVSEENY
     IEHRFKGITA YFGGLAQEVL KQG
//
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