ID C5ME50_CANTT Unreviewed; 837 AA.
AC C5ME50;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Origin recognition complex subunit 1 {ECO:0000256|RuleBase:RU365058};
GN ORFNames=CTRG_04342 {ECO:0000313|EMBL:EER31560.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER31560.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER31560.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; GG692400; EER31560.1; -; Genomic_DNA.
DR RefSeq; XP_002550045.1; XM_002549999.1.
DR AlphaFoldDB; C5ME50; -.
DR STRING; 294747.C5ME50; -.
DR EnsemblFungi; CTRG_04342-t43_1; CTRG_04342-t43_1-p1; CTRG_04342.
DR GeneID; 8296763; -.
DR KEGG; ctp:CTRG_04342; -.
DR VEuPathDB; FungiDB:CTRG_04342; -.
DR eggNOG; KOG1514; Eukaryota.
DR HOGENOM; CLU_012774_1_1_1; -.
DR OrthoDB; 118994at2759; -.
DR Proteomes; UP000002037; 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 CDD; cd18139; HLD_clamp_RarA; 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; PF01426; BAH; 1.
DR Pfam; PF21312; ORC1_wHTH; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00439; BAH; 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:UP000002037}.
FT DOMAIN 60..180
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 205..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..322
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..346
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 94437 MW; 10F92B860B8EC232 CRC64;
MNCIKGWGYR IENVDSDDNK SLVDSTPVTR RGRISRSQAS TMAIKPASDK IVLIRQVDGV
EFKVGDAIEV TSRDKNFGSS SEICIIKQIQ WGTSEFILVH VVWLLRPIEV SGLQEGIAKE
NELFLTPYFN ELKYTEFIRH INVLSEDQFN DIVIDESNSN NTFLLRRLAD DYGNLSESFD
YSELHQLLLS NNEEFTKKIM NMSLSHAQNR KSSRRARQRE QPIKTEKGTN SNNSSTKLVN
VGMEKRSGTK TENKRIDLGA EEKQKKKQDE QESIEPSDSD LQSDYISDDH DPDVESEDEE
VVIESEEEVE DDEADLDEEE SDFEEYGKKR KKRTRSPRKN NTPSPKRKSV KSKTTGSELE
EFYSAVTPTK KIKFSTLDRS SLPVFLSPTK RVPDGFTDTT SQAFKEMKQK LHTSQKLNAL
PGREDEFAMI YMNLESAVNE GTGCCVYVSG VPGMGKTATI KDVVQQMTES QSLGEIKPFS
YVELNGLKLL NPNVAYEVLW EHISGHRVVA TNAALLLEEY FKTDQANRKP LIVLMDELDQ
IATKKQNVMY NFFNWPTYNT SKLIVIAVAN TMDLPERVLS NKISSRLGLR RIQFKGYTFQ
QLGDIISHRL EMITKNNRRK VTISPDAIGF ASRKVASVSG DARRALNICR RAVEIAEKQY
YDNHKNSEGA TTAGDDDKNK ETYEVLISHI LAAINETVNS PLAQFIAALP FASKLVLASM
LRTTRRTGLA ESKLGDIISE MKNSLVMSTD PKQKKPGQLD IMDMLYTDKL FGDENAGNHN
FNLRIHSFKH VVTSLVEAGI IALQTSAGER SKLVQLNVSE EEVVSVLKKD NQIAGFL
//