CDC62_THEAC
ID CDC62_THEAC Reviewed; 404 AA.
AC Q9HKG3;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=ORC1-type DNA replication protein 2 {ECO:0000255|HAMAP-Rule:MF_01407};
GN Name=cdc6-2; OrderedLocusNames=Ta0636;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP FUNCTION, INTERACTION WITH MCM, AND GENE NAME.
RX PubMed=17108356; DOI=10.1093/nar/gkl864;
RA Haugland G.T., Shin J.H., Birkeland N.K., Kelman Z.;
RT "Stimulation of MCM helicase activity by a Cdc6 protein in the archaeon
RT Thermoplasma acidophilum.";
RL Nucleic Acids Res. 34:6337-6344(2006).
RN [3]
RP FUNCTION, INTERACTION WITH MCM, DOMAIN, AND MUTAGENESIS OF LYS-66 AND
RP ASP-143.
RX PubMed=18757887; DOI=10.1093/nar/gkn548;
RA Haugland G.T., Sakakibara N., Pey A.L., Rollor C.R., Birkeland N.K.,
RA Kelman Z.;
RT "Thermoplasma acidophilum Cdc6 protein stimulates MCM helicase activity by
RT regulating its ATPase activity.";
RL Nucleic Acids Res. 36:5602-5609(2008).
CC -!- FUNCTION: Involved in regulation of DNA replication. Stimulates the
CC helicase activity of MCM via stimulation of its ATPase activity.
CC Binding to MCM may result in conformational changes in MCM, leading to
CC catalytic ATP hydrolysis by the helicase. Directly stimulates MCM
CC movement along single-stranded and double-stranded DNA. Does not bind
CC DNA. {ECO:0000255|HAMAP-Rule:MF_01407, ECO:0000269|PubMed:17108356,
CC ECO:0000269|PubMed:18757887}.
CC -!- SUBUNIT: Interacts with MCM. {ECO:0000269|PubMed:17108356,
CC ECO:0000269|PubMed:18757887}.
CC -!- DOMAIN: The N-terminal AAA+ ATPase domain and the C-terminal winged-
CC helix (WH) domain are both required for stimulation of MCM activity.
CC {ECO:0000269|PubMed:18757887}.
CC -!- SIMILARITY: Belongs to the CDC6/cdc18 family. {ECO:0000255|HAMAP-
CC Rule:MF_01407}.
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; AL445064; CAC11775.1; -; Genomic_DNA.
DR RefSeq; WP_010901059.1; NC_002578.1.
DR AlphaFoldDB; Q9HKG3; -.
DR SMR; Q9HKG3; -.
DR STRING; 273075.Ta0636; -.
DR EnsemblBacteria; CAC11775; CAC11775; CAC11775.
DR GeneID; 1456212; -.
DR KEGG; tac:Ta0636; -.
DR eggNOG; arCOG00467; Archaea.
DR HOGENOM; CLU_025112_3_1_2; -.
DR OMA; DMLGIIN; -.
DR OrthoDB; 58376at2157; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; Nucleotide-binding; Reference proteome.
FT CHAIN 1..404
FT /note="ORC1-type DNA replication protein 2"
FT /id="PRO_0000151024"
FT BINDING 64..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01407"
FT BINDING 205
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 MUTAGEN 66
FT /note="K->E: Does not affect stimulation of helicase
FT activity."
FT /evidence="ECO:0000269|PubMed:18757887"
FT MUTAGEN 143
FT /note="D->N: Does not affect stimulation of helicase
FT activity."
FT /evidence="ECO:0000269|PubMed:18757887"
SQ SEQUENCE 404 AA; 45639 MW; 803D810C6CE89378 CRC64;
MDNPFARFAG TRTIQANLSL LEENYVPDSF PHRENQINEM VTILSSIMRG SRPSNIIVYG
KTGTGKTSTT KYVTKMLVEA ASNVSVVYVN CEIYDSPYSI LVAIANSAGE EKIPELGWPI
DRIYRETVER VEKTGKFFII ILDEMDRLIK KNGGDSLYVL LKLMTDVDSV RVSMIGITND
TTVLENIDAR IKSRLNQESI VFPPYNASEI RDIISSRLDK VLGPGVVDDT AINLCAAIGA
QEHGDARKAI DLMRIAIEIA IRENRNKITE NEIYEARERY EMNVLREAIS TLPLHSKIVL
LSAVVTQEIE PNSVITGEIY ENYRRICDDL GFSPLSPRRI SDLLTELADY GLLVMDDRNM
GKYGRTRSFS VVHQAETIKK YLLEDENLSM FKSSKMPKQT RFDT
