ID A7TNP8_VANPO Unreviewed; 920 AA.
AC A7TNP8;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Origin recognition complex subunit 1 {ECO:0000256|RuleBase:RU365058};
GN ORFNames=Kpol_1001p11 {ECO:0000313|EMBL:EDO16099.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO16099.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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: ORC is composed of six subunits.
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}.
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DR EMBL; DS480433; EDO16099.1; -; Genomic_DNA.
DR RefSeq; XP_001643957.1; XM_001643907.1.
DR AlphaFoldDB; A7TNP8; -.
DR STRING; 436907.A7TNP8; -.
DR GeneID; 5544229; -.
DR KEGG; vpo:Kpol_1001p11; -.
DR eggNOG; KOG1514; Eukaryota.
DR HOGENOM; CLU_012774_1_1_1; -.
DR InParanoid; A7TNP8; -.
DR OMA; IMYNFFN; -.
DR OrthoDB; 118994at2759; -.
DR PhylomeDB; A7TNP8; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032993; C:protein-DNA complex; IEA:UniProt.
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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 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; 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; IPR048867; ORC1_wHTH.
DR InterPro; IPR027417; P-loop_NTPase.
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; PF21312; ORC1_wHTH; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF82061; BAH domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51038; BAH; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU365058};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW 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:UP000000267}.
FT DOMAIN 48..187
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 218..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..303
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 104995 MW; F7A96E69EE4AE382 CRC64;
MAHSQKDLAG WKIVITDAEN NVLDGSKRRS RRNAPKEYIH LERESDELRF TRGDSIIMYD
EKVDSNIVYL VNEIRLNTMN NVVEILGMLY LGHDDLDPIK YLEQFDPDFV NDDRSDEEYV
ARIEQDVGKK RLFLTASLSE IWLMNFRGMA NILEEEEAKD LTDKIEGKDF VVNYVCDPDS
TNFVSIEFKG VRNKILECEP KEAEEFLKKV SLPKVNTNTI KSQEKEPKKI AKSMKSRKSV
VEDIKLESES ENNLASSSSD EEQDNSSDYA NDNGNHISTD EEDIDNEEEG SGNDDNNDNI
SIDTDEEEYG RKNKRKRRTT QTTSVKAPRT KRKATSTVVD DNPRSGTPKT TSNQQNGLFI
RKFTKRNVAR AKKKYTPFSK RFKSIKDIPD LTKLAEFNQA SADLEIARLE DKLRAPKGQK
VVETIFSKVK KRLYSSHGRE EIMKSTNFND YLPGRENEFA SIYLSLYSAV ESGSATTVYV
AGTPGVGKTL TVREVINEMQ NSVDNGELPK FQYVELNGLK MVKPTDSYEV LWNKVSGERL
TWGAAMESLE FYFNKVPREK KGIVVVLLDE LDALVTKAQD IMYNFFNWTT YENAKLIVVA
VANTMDLPER QLGNKVSSRI GFTRIMFAGY THDELKNIIN CKLQGLNDSY FYVNSKNGSA
HLINPEEESS IDDENLPKHI KKVQLRMSDD AIEIAARKVA SVSGDARRAL KICKRAAEIA
EQYYMSRHGY GYDGLPLEEI DDFDMENDED VIALRKERAN NKALEMTERD NDDSIQTVHI
SHIVKALNET VNSRTVKVIE RLPFTVKLFL YALLNLMKKT MKQEQHLGDI IDEIKLLVDV
NGKNKFIVEI SKTLFGQDSS PNEPSQLRMV SWNFVLNQLI DSGIIIRQTL KNERKSTVKL
NISTEDIKNA IEREDSLKGL
//
