CDC61_SACS2
ID CDC61_SACS2 Reviewed; 397 AA.
AC Q980N4;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=ORC1-type DNA replication protein 1 {ECO:0000255|HAMAP-Rule:MF_01407};
GN Name=cdc6-1; OrderedLocusNames=SSO0257;
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 CDC6-3, AND
RP 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 CDC6-3.
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 [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 15-397 IN COMPLEX WITH CDC6-3 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 strongly inhibits its DNA helicase activity. Also regulates the
CC DNA polymerase and the nuclease activities of PolB1. Stimulates the
CC DNA-binding activity of Cdc6-3. {ECO:0000255|HAMAP-Rule:MF_01407,
CC ECO:0000269|PubMed:16179962, 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:16179962, ECO:0000269|PubMed:17673179,
CC ECO:0000269|PubMed:17761879, ECO:0000269|PubMed:17825793,
CC ECO:0000269|PubMed:19416914}.
CC -!- INTERACTION:
CC Q980N4; P26811: dpo1; NbExp=4; IntAct=EBI-9026921, 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 -!- PTM: Autophosphorylated in vitro. {ECO:0000269|PubMed:16179962}.
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; AAK40596.1; -; Genomic_DNA.
DR PIR; E90167; E90167.
DR RefSeq; WP_009990521.1; NC_002754.1.
DR PDB; 2QBY; X-ray; 3.35 A; A=15-397.
DR PDBsum; 2QBY; -.
DR AlphaFoldDB; Q980N4; -.
DR SMR; Q980N4; -.
DR DIP; DIP-48851N; -.
DR IntAct; Q980N4; 1.
DR STRING; 273057.SSO0257; -.
DR EnsemblBacteria; AAK40596; AAK40596; SSO0257.
DR GeneID; 44129226; -.
DR KEGG; sso:SSO0257; -.
DR PATRIC; fig|273057.12.peg.251; -.
DR eggNOG; arCOG00467; Archaea.
DR HOGENOM; CLU_025112_3_1_2; -.
DR InParanoid; Q980N4; -.
DR OMA; DMLGIIN; -.
DR PhylomeDB; Q980N4; -.
DR EvolutionaryTrace; Q980N4; -.
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 3D-structure; ATP-binding; DNA replication; DNA-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..397
FT /note="ORC1-type DNA replication protein 1"
FT /id="PRO_0000151018"
FT BINDING 67..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01407"
FT BINDING 208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01407"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01407"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 69..83
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:2QBY"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 123..135
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:2QBY"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 210..224
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 232..244
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 249..265
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 273..293
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 297..309
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 319..333
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 340..352
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 355..360
FT /evidence="ECO:0007829|PDB:2QBY"
FT STRAND 370..376
FT /evidence="ECO:0007829|PDB:2QBY"
FT HELIX 379..388
FT /evidence="ECO:0007829|PDB:2QBY"
SQ SEQUENCE 397 AA; 45167 MW; A2A32A355A3ADD74 CRC64;
MSDIIDEVIS SFKTSSIFIN REYLLPDYIP DELPHREDQI RKIASILAPL YREEKPNNIF
IYGLTGTGKT AVVKFVLSKL HKKFLGKFKH VYINTRQIDT PYRVLADLLE SLDVKVPFTG
LSIAELYRRL VKAVRDYGSQ VVIVLDEIDA FVKKYNDDIL YKLSRINSEV NKSKISFIGI
TNDVKFVDLL DPRVKSSLSE EEIIFPPYNA EELEDILTKR AQMAFKPGVL PDNVIKLCAA
LAAREHGDAR RALDLLRVSG EIAERMKDTK VKEEYVYMAK EEIERDRVRD IILTLPFHSK
LVLMAVVSIS SEENVVSTTG AVYETYLNIC KKLGVEAVTQ RRVSDIINEL DMVGILTAKV
VNRGRYGKTK EIGLAVDKNI IVRSLIESDS RFADLWS
