GenomeNet

Database: UniProt
Entry: C5DS67_ZYGRC
LinkDB: C5DS67_ZYGRC
Original site: C5DS67_ZYGRC 
ID   C5DS67_ZYGRC            Unreviewed;      1029 AA.
AC   C5DS67;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Origin recognition complex subunit 1 {ECO:0000256|RuleBase:RU365058};
GN   OrderedLocusNames=ZYRO0B14278g {ECO:0000313|EMBL:CAR26628.1};
OS   Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS   / NRRL Y-229) (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR26628.1, ECO:0000313|Proteomes:UP000008536};
RN   [1] {ECO:0000313|Proteomes:UP000008536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC   Y-229 {ECO:0000313|Proteomes:UP000008536};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(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}.
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; CU928174; CAR26628.1; -; Genomic_DNA.
DR   RefSeq; XP_002495561.1; XM_002495516.1.
DR   AlphaFoldDB; C5DS67; -.
DR   STRING; 559307.C5DS67; -.
DR   GeneID; 8202727; -.
DR   KEGG; zro:ZYRO0B14278g; -.
DR   HOGENOM; CLU_012774_1_1_1; -.
DR   InParanoid; C5DS67; -.
DR   Proteomes; UP000008536; Chromosome B.
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; cd04720; BAH_Orc1p_Yeast; 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:UP000008536}.
FT   DOMAIN          48..186
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   REGION          201..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..288
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..316
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..407
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..448
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1029 AA;  117838 MW;  93EC664B18F76971 CRC64;
     MAETLKDIQG WEVITTDEKG NIINDNRRRS RKRGGSENTF LIRLKDGLKF GRGDSVIMHD
     EATKTYSVYL IHEIRLNTLN NLVEIWAFSY LRWFELKPLL YYAHFDPGYA AENRPIEEYR
     NRFIEDVNKS EIYLTAELSE IWLKDFVEVA RIMPEVDWKR SSQLEDKDFF VRFICEPTAE
     SYVPIDIIKE QRLLQNTEPK SYEEHLKRMS VPPTLGRSKS GSTRRTNQVT SPSVNKIEDE
     PETEDEEEDE TQEEEEETQE GEEEEYNEEG EEGEEEEEEE EEEEEEEVGK KNEGSSSEEK
     EGFTGESRDS SRKDTTASKS QDFSTSQSPE AYSDAQETPS IASKTNPSGP QQAPAKENLL
     GKLKAQKEDE GQNRASSAGK EDDVTVDESE ANKSETENNK DDKHEDSNAE EYVDEEEEDE
     YAEQEEEEEE EEEEEEEEEE DEDEDEDYDQ KSSSKRGKSQ SPAKKSRKLA PLSTPVTPSK
     PPNHNNNNTV SSPAIRKFTK RNVVRAKKKY TPFSKRFKSV DEIPDLTQLA ELNQSSNKLD
     VAALENKLRT PKKHEIVETI FSRIKKQLYS SHEKEEIVKS TNFQDYLPAR ENEFASIYLS
     LYSAIESGSA TTVYVAGTPG VGKTLTVREV VKELQRSADQ NELPLFQYVE INGLKMVKPT
     DSYEVLWNKI MGERLTWGAA MESLEFYFNK VPQNKKRPVV VLLDELDALL TKTQDIMYNF
     FNWTTYENAK LIVIAVANTM DLPERQLGNK VSSRIGLTRI MFTGYTHEEL RKIIDFRLKG
     FNNSYFYVDT QSGSAHMLTP EEDTNTSELP PHTKKVQLRM SDDAIEIASR KVASVSGDAR
     RALKVCKRAA EIAEQHYMSR HGYGYDGQAV LTPNEGEDAN DGDGLQTVHI THVLKALNET
     VSSQGTQFIS NLSFTAKIFL YALLNLIKKT ELQEQQLGDI IDEIRLLIDV NGNNKFILEI
     SRVLFQQGSE STPEQLKIIS WDFLLNQLVE AGIIFRQSMK NERLTCIKLN ISQEEVRKGL
     EQDENLKSL
//
DBGET integrated database retrieval system