CDC63_SACS2
ID CDC63_SACS2 Reviewed; 394 AA.
AC Q97WM8;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=ORC1-type DNA replication protein 3 {ECO:0000255|HAMAP-Rule:MF_01407};
GN Name=cdc6-3; OrderedLocusNames=SSO2184;
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=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 [2]
RP FUNCTION, DNA-BINDING, SUBUNIT, INTERACTION WITH CDC6-1 AND CDC6-2, AND
RP LACK OF AUTOPHOSPHORYLATION.
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 [3]
RP FUNCTION, AND INTERACTION WITH MCM.
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 [4]
RP FUNCTION, AND INTERACTION WITH CDC6-1 AND CDC6-2.
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 [5]
RP INDUCTION BY VIRUS (MICROBIAL INFECTION).
RC STRAIN=2-2-12;
RX PubMed=18337566; DOI=10.1128/jvi.02583-07;
RA Ortmann A.C., Brumfield S.K., Walther J., McInnerney K., Brouns S.J.,
RA van de Werken H.J., Bothner B., Douglas T., van de Oost J., Young M.J.;
RT "Transcriptome analysis of infection of the archaeon Sulfolobus
RT solfataricus with Sulfolobus turreted icosahedral virus.";
RL J. Virol. 82:4874-4883(2008).
RN [6]
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).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 14-394 IN COMPLEX WITH CDC6-1 AND
RP DNA.
RX PubMed=17761879; DOI=10.1126/science.1143690;
RA Dueber E.L., Corn J.E., Bell S.D., Berger J.M.;
RT "Replication origin recognition and deformation by a heterodimeric archaeal
RT Orc1 complex.";
RL Science 317:1210-1213(2007).
CC -!- FUNCTION: Involved in regulation of DNA replication. May play essential
CC roles in origin recognition and cell cycle control of replication.
CC Binds to DNA, with a preference for molecules that contain a bubble, a
CC fork, or a tail. Inhibits the binding of the MCM helicase to the origin
CC DNA and inhibits its DNA helicase activity. Also regulates the DNA
CC polymerase and the nuclease activities of PolB1. Inhibits the DNA-
CC binding activity of Cdc6-1 and Cdc6-2. {ECO:0000255|HAMAP-
CC Rule:MF_01407, ECO:0000269|PubMed:16179962,
CC ECO:0000269|PubMed:17673179, ECO:0000269|PubMed:17825793,
CC ECO:0000269|PubMed:19416914}.
CC -!- SUBUNIT: Monomer. Interacts with Cdc6-1, Cdc6-2, MCM and PolB1.
CC {ECO:0000269|PubMed:16179962, ECO:0000269|PubMed:17673179,
CC ECO:0000269|PubMed:17761879, ECO:0000269|PubMed:17825793,
CC ECO:0000269|PubMed:19416914}.
CC -!- INTERACTION:
CC Q97WM8; P26811: dpo1; NbExp=3; IntAct=EBI-9026919, EBI-15778666;
CC -!- INDUCTION: (Microbial infection) At least 4-fold induced following
CC infection by Sulfolobus turreted icosahedral virus 1 (STIV-1) in strain
CC 2-2-12. {ECO:0000269|PubMed:18337566}.
CC -!- MISCELLANEOUS: Strain 2-2-12 is a substrain of P2 that is highly
CC susceptible to infection by Sulfolobus turreted icosahedral virus 1
CC (STIV-1). {ECO:0000269|PubMed:18337566}.
CC -!- SIMILARITY: Belongs to the CDC6/cdc18 family. {ECO:0000255|HAMAP-
CC Rule:MF_01407}.
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DR EMBL; AE006641; AAK42358.1; -; Genomic_DNA.
DR PIR; G90387; G90387.
DR RefSeq; WP_009992115.1; NC_002754.1.
DR PDB; 2QBY; X-ray; 3.35 A; B=14-394.
DR PDBsum; 2QBY; -.
DR AlphaFoldDB; Q97WM8; -.
DR SMR; Q97WM8; -.
DR DIP; DIP-48853N; -.
DR IntAct; Q97WM8; 1.
DR STRING; 273057.SSO2184; -.
DR EnsemblBacteria; AAK42358; AAK42358; SSO2184.
DR GeneID; 44127920; -.
DR KEGG; sso:SSO2184; -.
DR PATRIC; fig|273057.12.peg.2280; -.
DR eggNOG; arCOG00467; Archaea.
DR HOGENOM; CLU_025112_3_1_2; -.
DR InParanoid; Q97WM8; -.
DR OMA; REDAFQD; -.
DR PhylomeDB; Q97WM8; -.
DR EvolutionaryTrace; Q97WM8; -.
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; 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 3D-structure; ATP-binding; DNA replication; DNA-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..394
FT /note="ORC1-type DNA replication protein 3"
FT /id="PRO_0000151020"
FT BINDING 66..70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01407"
FT BINDING 207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01407"
FT TURN 19..23
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 36..50
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 68..85
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:2QBY"
FT TURN 184..189
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 209..222
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 232..242
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 270..290
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 294..304
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 309..322
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 330..342
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:2QBY"
FT TURN 354..357
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 360..368
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 369..381
FT /evidence="ECO:0007829|PDB:2QBY"
SQ SEQUENCE 394 AA; 44554 MW; 437E64B7E82B10B9 CRC64;
MHVIRETLKG GKGEVIKNPK VFIDPLSVFK EIPFREDILR DAAIAIRYFV KNEVKFSNLF
LGLTGTGKTF VSKYIFNEIE EVKKEDEEYK DVKQAYVNCR EVGGTPQAVL SSLAGKLTGF
SVPKHGINLG EYIDKIKNGT RNIRAIIYLD EVDTLVKRRG GDIVLYQLLR SDANISVIMI
SNDINVRDYM EPRVLSSLGP SVIFKPYDAE QLKFILSKYA EYGLIKGTYD DEILSYIAAI
SAKEHGDARK AVNLLFRAAQ LASGGGIIRK EHVDKAIVDY EQERLIEAVK ALPFHYKLAL
RSLIESEDVM SAHKMYTDLC NKFKQKPLSY RRFSDIISEL DMFGIVKIRI INRGRAGGVK
KYALVEDKEK VLRALNETFE DSISIGDFDD VGEN
