ORC1_DEBHA
ID ORC1_DEBHA Reviewed; 810 AA.
AC Q6BSE2;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Origin recognition complex subunit 1;
GN Name=ORC1; OrderedLocusNames=DEHA2D09504g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Component of the origin recognition complex (ORC) that binds
CC origins of replication. It has a role in both chromosomal replication
CC and mating type transcriptional silencing. Binds to the ARS consensus
CC sequence (ACS) of origins of replication in an ATP-dependent manner (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: ORC is composed of six subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ORC1 family. {ECO:0000305}.
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; CR382136; CAG87030.2; -; Genomic_DNA.
DR RefSeq; XP_458878.2; XM_458878.1.
DR AlphaFoldDB; Q6BSE2; -.
DR SMR; Q6BSE2; -.
DR STRING; 4959.XP_458878.2; -.
DR EnsemblFungi; CAG87030; CAG87030; DEHA2D09504g.
DR GeneID; 2901345; -.
DR KEGG; dha:DEHA2D09504g; -.
DR VEuPathDB; FungiDB:DEHA2D09504g; -.
DR eggNOG; KOG1514; Eukaryota.
DR HOGENOM; CLU_012774_1_1_1; -.
DR InParanoid; Q6BSE2; -.
DR OMA; FFNWPTY; -.
DR OrthoDB; 935804at2759; -.
DR Proteomes; UP000000599; Chromosome D.
DR GO; GO:0005694; C:chromosome; IEA:UniProt.
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:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; 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 SMART; SM00382; AAA; 1.
DR SMART; SM00439; BAH; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51038; BAH; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-binding; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..810
FT /note="Origin recognition complex subunit 1"
FT /id="PRO_0000127071"
FT DOMAIN 57..183
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT REGION 21..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..278
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..303
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 423..431
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 508
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 509
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 509
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 542
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 615
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
SQ SEQUENCE 810 AA; 91895 MW; B4CD96B7F26696E4 CRC64;
MAKSQRDLKG WQYFLDDAEL NNTDSVNGEP TTPSRRSRRG KSTSSQKISL KREEDELEIK
EGDFLLVQQD NNSPEVAIVK EIKFGNDNFL DIIVSWFIRM RDIEEADLPK VEEYKERSQL
NENELFITSY LDEVKLGEII DKVNILSEEE FNNDIVIDDS NKASTFICRR GCDSAGELFT
DVFDFRDLCV LFEKNHHEFI EFIRRKTVPV AYNANKTHDK SKSIKDKLDE VETKKPKQKT
VSKQILDEEE ENNDSSDEFE SAIDLQDEPS SDELESDEDA SESKNKSPRK RKASSKPKAV
KEKQKRVKIP NNHSKFDDES RQFITSVVSP LNKRMKIKDS SKPSILALSP RKPKKGVSKG
ENGKNGSLGV DASSEAFKEL KEKLHTSTRL SSLPCREDEF TSIYLNLETA IQEQTGCCLY
VSGTPGVGKT ATVREVIAQL RELTEMGELN DFDYLEINGL KLLSPNVAYE KLWEKISGLK
VTASNAALLL ESYFSQDTPR KPLIVLMDEL DQIVTKKQNV MYNFFNWPTY SNSKLIVIAV
ANTMDLPERV LSNKISSRLG LRRIQFIGYT FEQLGSIIKH RLDMLTKQNK RKVIINSDAI
GFASRKVASV SGDARRALTI CRRAVEIAEK DFLSSKEDPG NEQEIENESY HVQISHISKA
INETVNSPIS QFLMSLPFAS KLVLAGVLLR MKRSGLAENS LGDIIDEMKN SLTMLTSRDG
DKVLEAIDSK MTLIDLLYGN GLLQNLDSTF NSKDTNIRIL RFKYIVNELV ENGILQQNVR
GERHSLINLN ISEEEIVSVL KRDKEISSIL