ID   ORC1_CANAX              Reviewed;         805 AA.
AC   O74270;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Origin recognition complex subunit 1;
GN   Name=ORC1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 10261 / CBS 2718 / NBRC 1061 / FMJ 1011;
RA   Vinz K., Eck R.;
RT   "Molecular cloning and characterization of Orc1 from Candida albicans.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; Y17395; CAA76762.1; -; mRNA.
DR   AlphaFoldDB; O74270; -.
DR   SMR; O74270; -.
DR   PRIDE; O74270; -.
DR   VEuPathDB; FungiDB:C1_03070C_A; -.
DR   VEuPathDB; FungiDB:CAWG_01077; -.
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; 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; SM00439; BAH; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51038; BAH; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; DNA replication; DNA-binding; Magnesium; Metal-binding;
KW   Nucleotide-binding; Nucleus.
FT   CHAIN           1..805
FT                   /note="Origin recognition complex subunit 1"
FT                   /id="PRO_0000127070"
FT   DOMAIN          60..180
FT                   /note="BAH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..299
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         428..436
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q13415"
FT   BINDING         514
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q13415"
FT   BINDING         515
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q13415"
FT   BINDING         515
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q13415"
FT   BINDING         548
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q13415"
FT   BINDING         621
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q13415"
SQ   SEQUENCE   805 AA;  91249 MW;  D0335DE26E41262E CRC64;
     MNKLPKGWNF TIVDDNADST NSENIQGKRP RRSRTSVQRS DGASPIIRDN IVLIRTDDNE
     EFKVGDTIEI TQGKGPEDPT TEYGLITEIK FGNSEFIEVI VDWFIRSSEI VGMPNDFFAD
     NELLLTPFRS EVKFIDFIRP INVLSESQFA DVVIDESNSH STFLVKRATD NEGNFSDIFD
     YKDFSGKVLE NPKKCAIQVK ELISTTVQKE LLKEFSKEQR KKKANKVSTT GRVTRFNKRK
     ESVSTKAIKP ENKQVKIEID NDVLSDQSEE KQEESDYNEA EDANSALESD EENISQESED
     SEVEYSTKKK LKNKKLSRRS KAAATPSPKR KLQKKDIEDI YSVVTPTKRM KLGKDDRDSL
     PVFLSPTKSV PSEFTDPKSV AFKEVKQRLH TSQKLNALPG REDEFAMIYM NHESAVNEKT
     GCCVYVCGLP GMGKTATIKD VVEQMTYSSE RGEMEQFSYL ELNGLKLLSP TVAYEALWHH
     ISGDKVSASN AALLLEEYFK REDHKRKPLV ILMDEFDQIA TKKQNVMYNF FNWPTYSTSK
     LIVIAVANTM DLPERMLTNK IASRLGLRRI QFRGYTFQQL GDIITHRLEM ITKNNRRKVV
     ITSDAIGFAS RKVASVSGDA RRALTICRRA VEIAEKEYLE NKKGEDDSEP YQVLISHIST
     AINETVNSPL SKYIASLPFA SKLVLASLLR RSRRTGLAEN SLGDIIDEMR NSFAMATHSE
     EQGSDELNMQ DVLYSDKTFT ATNETVPILN LRIHFFKQIV TSLVEAGIII QQNSPGETSR
     LVKLDVPEEE VVSVFKKDNA ISQFL