CDC62_SACS2
ID CDC62_SACS2 Reviewed; 413 AA.
AC Q9UXF8;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=ORC1-type DNA replication protein 2 {ECO:0000255|HAMAP-Rule:MF_01407};
GN Name=cdc6-2; OrderedLocusNames=SSO0771;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=10701121; DOI=10.1139/g99-108;
RA Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT "Gene content and organization of a 281-kbp contig from the genome of the
RT extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL Genome 43:116-136(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP FUNCTION, SUBUNIT, AUTOPHOSPHORYLATION, DNA-BINDING, AND MUTAGENESIS OF
RP LYS-72.
RX PubMed=12966100; DOI=10.1074/jbc.m306075200;
RA De Felice M., Esposito L., Pucci B., Carpentieri F., De Falco M., Rossi M.,
RA Pisani F.M.;
RT "Biochemical characterization of a CDC6-like protein from the crenarchaeon
RT Sulfolobus solfataricus.";
RL J. Biol. Chem. 278:46424-46431(2003).
RN [4]
RP FUNCTION, DNA-BINDING, AND INTERACTION WITH MCM.
RX PubMed=15292191; DOI=10.1074/jbc.m406693200;
RA De Felice M., Esposito L., Pucci B., De Falco M., Rossi M., Pisani F.M.;
RT "A CDC6-like factor from the archaea Sulfolobus solfataricus promotes
RT binding of the mini-chromosome maintenance complex to DNA.";
RL J. Biol. Chem. 279:43008-43012(2004).
RN [5]
RP INTERACTION WITH CDC6-3.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=16179962; DOI=10.1007/s00792-005-0473-0;
RA De Felice M., Esposito L., Rossi M., Pisani F.M.;
RT "Biochemical characterization of two Cdc6/ORC1-like proteins from the
RT crenarchaeon Sulfolobus solfataricus.";
RL Extremophiles 10:61-70(2006).
RN [6]
RP FUNCTION, INTERACTION WITH MCM, AND DOMAIN.
RX PubMed=17673179; DOI=10.1016/j.bbrc.2007.07.073;
RA Jiang P.X., Wang J., Feng Y., He Z.G.;
RT "Divergent functions of multiple eukaryote-like Orc1/Cdc6 proteins on
RT modulating the loading of the MCM helicase onto the origins of the
RT hyperthermophilic archaeon Sulfolobus solfataricus P2.";
RL Biochem. Biophys. Res. Commun. 361:651-658(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH CDC6-3.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=17825793; DOI=10.1016/j.bbrc.2007.08.125;
RA Wang J., Jiang P.X., Feng H., Feng Y., He Z.G.;
RT "Three eukaryote-like Orc1/Cdc6 proteins functionally interact and mutually
RT regulate their activities of binding to the replication origin in the
RT hyperthermophilic archaeon Sulfolobus solfataricus P2.";
RL Biochem. Biophys. Res. Commun. 363:63-70(2007).
RN [8]
RP FUNCTION, AND INTERACTION WITH POLB1.
RX PubMed=19416914; DOI=10.1073/pnas.0813056106;
RA Zhang L., Zhang L., Liu Y., Yang S., Gao C., Gong H., Feng Y., He Z.G.;
RT "Archaeal eukaryote-like Orc1/Cdc6 initiators physically interact with DNA
RT polymerase B1 and regulate its functions.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:7792-7797(2009).
CC -!- FUNCTION: Involved in regulation of DNA replication. May play essential
CC roles in origin recognition and cell cycle control of replication.
CC Binds both single-stranded and double-stranded DNA, with a preference
CC for molecules that contain a bubble, a fork, or a tail. Has a weak
CC ATPase activity. Stimulates the binding of the MCM helicase to the
CC origin DNA, but strongly inhibits ATPase and DNA helicase activities of
CC MCM. Also regulates the DNA polymerase and the nuclease activities of
CC PolB1. {ECO:0000255|HAMAP-Rule:MF_01407, ECO:0000269|PubMed:12966100,
CC ECO:0000269|PubMed:15292191, ECO:0000269|PubMed:17673179,
CC ECO:0000269|PubMed:17825793, ECO:0000269|PubMed:19416914}.
CC -!- SUBUNIT: Monomer. Interacts with Cdc6-3, MCM and PolB1.
CC {ECO:0000269|PubMed:12966100, ECO:0000269|PubMed:15292191,
CC ECO:0000269|PubMed:16179962, ECO:0000269|PubMed:17673179,
CC ECO:0000269|PubMed:17825793, ECO:0000269|PubMed:19416914}.
CC -!- INTERACTION:
CC Q9UXF8; P26811: dpo1; NbExp=5; IntAct=EBI-15778726, EBI-15778666;
CC -!- DOMAIN: The C-terminal WH domain is essential for its stimulating
CC effect on the MCM-loading activity. {ECO:0000269|PubMed:17673179}.
CC -!- PTM: Autophosphorylated in vitro.
CC -!- SIMILARITY: Belongs to the CDC6/cdc18 family. {ECO:0000255|HAMAP-
CC Rule:MF_01407}.
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DR EMBL; Y18930; CAB57532.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK41068.1; -; Genomic_DNA.
DR PIR; E90226; E90226.
DR RefSeq; WP_009991361.1; NC_002754.1.
DR AlphaFoldDB; Q9UXF8; -.
DR SMR; Q9UXF8; -.
DR DIP; DIP-48852N; -.
DR IntAct; Q9UXF8; 1.
DR STRING; 273057.SSO0771; -.
DR PRIDE; Q9UXF8; -.
DR EnsemblBacteria; AAK41068; AAK41068; SSO0771.
DR GeneID; 44129777; -.
DR KEGG; sso:SSO0771; -.
DR PATRIC; fig|273057.12.peg.771; -.
DR eggNOG; arCOG00467; Archaea.
DR HOGENOM; CLU_025112_3_2_2; -.
DR InParanoid; Q9UXF8; -.
DR OMA; YLFYENE; -.
DR PhylomeDB; Q9UXF8; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd08768; Cdc6_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01407; ORC1_type_DNA_replic_protein; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR015163; Cdc6_C.
DR InterPro; IPR014277; Orc1/Cdc6_arc.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF13401; AAA_22; 1.
DR Pfam; PF09079; Cdc6_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01074; Cdc6_C; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02928; TIGR02928; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA replication; DNA-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..413
FT /note="ORC1-type DNA replication protein 2"
FT /id="PRO_0000151019"
FT BINDING 70..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01407"
FT BINDING 217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01407"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01407"
FT MUTAGEN 72
FT /note="K->A: Loss of ATPase activity. Loss of
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:12966100"
SQ SEQUENCE 413 AA; 47533 MW; 3CFFCFF405ACD01C CRC64;
MVSAKDILSD SLRSSVLIIK HKDKLSPDYV PENLPHREEK IKELGFIFKD LLAGDAKDSE
RVVILGRTGT GKTATVRLFG KNFEDIAERE YGVKVKYVHI NCYRHRTLYL ISQEIANALK
LPIPSRGLSA QEVFKMIHEY LDRRNIHLIV ALDEFGHFLN TANTEEIYFL VRLYDEISAI
IKRISYIFIV NESHSIYKLD RSIRDHIARR LIEFPPYKSM ELYDILKYRV DEAFNDNAVD
DEVLQFISNT YGYDKGGNGN ARIAIETLSL AGEIAEKEGS PVVLLDHAKK ANSTINPEIQ
EIIDSLSYLD LHQLILLKAL IRALNKTKAD EITMGTLEEE YISLSREFNE EPRRHTQVYE
YLRKLKVIGI INTRQSGKGM RGRTTLVSLS LPLDKRLDDY IMQQIMVRLK SRA
