ORC1_KLULA
ID ORC1_KLULA Reviewed; 886 AA.
AC P54788; Q6CWD2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Origin recognition complex subunit 1;
GN Name=ORC1; OrderedLocusNames=KLLA0B05016g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7502077; DOI=10.1126/science.270.5242.1667;
RA Gavin K.A., Hidaka M., Stillman B.D.;
RT "Conserved initiator proteins in eukaryotes.";
RL Science 270:1667-1671(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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.
CC -!- SIMILARITY: Belongs to the ORC1 family. {ECO:0000305}.
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DR EMBL; U40151; AAC49130.1; -; Genomic_DNA.
DR EMBL; CR382122; CAH02150.1; -; Genomic_DNA.
DR RefSeq; XP_451757.1; XM_451757.1.
DR AlphaFoldDB; P54788; -.
DR SMR; P54788; -.
DR STRING; 28985.XP_451757.1; -.
DR PRIDE; P54788; -.
DR EnsemblFungi; CAH02150; CAH02150; KLLA0_B05016g.
DR GeneID; 2897110; -.
DR KEGG; kla:KLLA0_B05016g; -.
DR eggNOG; KOG1514; Eukaryota.
DR HOGENOM; CLU_012774_1_1_1; -.
DR InParanoid; P54788; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IEA:EnsemblFungi.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; IEA:EnsemblFungi.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:EnsemblFungi.
DR GO; GO:0006270; P:DNA replication initiation; IEA:EnsemblFungi.
DR GO; GO:0043007; P:maintenance of rDNA; IEA:EnsemblFungi.
DR GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IEA:EnsemblFungi.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IEA:EnsemblFungi.
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 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..886
FT /note="Origin recognition complex subunit 1"
FT /id="PRO_0000127072"
FT DOMAIN 50..192
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT REGION 276..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 471..479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 558
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 559
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 559
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 592
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 700
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT SITE 101
FT /note="Histone H4K20me2 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N2"
FT CONFLICT 856
FT /note="L -> F (in Ref. 1; AAC49130)"
FT /evidence="ECO:0000305"
FT CONFLICT 874..875
FT /note="EQ -> DE (in Ref. 1; AAC49130)"
FT /evidence="ECO:0000305"
FT CONFLICT 881
FT /note="E -> Q (in Ref. 1; AAC49130)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 886 AA; 101374 MW; CD4665FD6C47D28F CRC64;
MASTLAEFEV QWEIQKTDLK GNLIAETPRR RRRGDATEHE VINLVRYDGV RLYPGVTIVC
KVEGADELSA YMIHEVRLNT SNYVELWCLN YLSWYEINAA ERYKQLDGEF YETNKEKGDK
FFEETFASQS IKNELYLTAE LSEIYLRDLQ FVANIKNEKE YLDSVNEGKM DSNMFLCRSA
CLPSGTNLAD LDIHFFEEKI RSSNPKVSLE YLRDITLPKL PKPLNKSKVH AREKVVATKL
QSDNTPSKKS FQQTVSKTNA EVQRIASTIV NEKEAISDNE SDLSEYHESK EEFANASSSD
SDEEFEDYQS AEELAIVEPA KKKVRSIKPD IPISPVKSQT PLQPSAVHSS PRKFFKNNIV
RAKKAYTPFS KRYKNPKDIP DLNDIFQRHN NDLDIAALEE RFRTVSAKGK METIFSKVKK
QLNSRNSKEE IVKAADFDNY LPARENEFAS IYLSLYSAIE AGTSTSIYIA GTPGVGKTLT
VREVVKDLMT SADQKELPRF QYIEINGLKI VKASDSYEVF WQKISGEKLT SGAAMESLEF
YFNKVPATKK RPIVVLLDEL DALVSKSQDV MYNFFNWATY SNAKLIVVAV ANTLDLPERH
LGNKISSRIG FTRIMFTGYT HEELRTIINL RLKYLNESSF YVDPETGSSY MISPDSSTIE
TDEEEKRKDF SNYKRLKLRI NPDAIEIASR KIASVSGDVR RALKVVKRAV EYAENDYLKR
LRYERLVNSK KDTSGNGTGN EELQSVEIKH ITKALNESST SPEQQFISGL SFSGKLFLYA
LINLIKKKQT DVQLGDIVEE MRLLIDVNGN NKYILELKRI LFQNDSVDTK EQLRAVSWDY
ILLQLLDAGV VVRQYLKNER LSTIKLNISM EDAEQCLHED EMLKTF
