CDC61_METTH
ID CDC61_METTH Reviewed; 382 AA.
AC O27463;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=ORC1-type DNA replication protein 1 {ECO:0000255|HAMAP-Rule:MF_01407};
GN Name=cdc6-1; OrderedLocusNames=MTH_1412;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP PHOSPHORYLATION, AND MUTAGENESIS OF ASP-149.
RX PubMed=11514535; DOI=10.1128/jb.183.18.5459-5464.2001;
RA Grabowski B., Kelman Z.;
RT "Autophosphorylation of archaeal Cdc6 homologues is regulated by DNA.";
RL J. Bacteriol. 183:5459-5464(2001).
RN [3]
RP FUNCTION, DNA-BINDING, SUBUNIT, AND MUTAGENESIS OF ARG-334.
RX PubMed=15358831; DOI=10.1093/nar/gkh819;
RA Capaldi S.A., Berger J.M.;
RT "Biochemical characterization of Cdc6/Orc1 binding to the replication
RT origin of the euryarchaeon Methanothermobacter thermoautotrophicus.";
RL Nucleic Acids Res. 32:4821-4832(2004).
RN [4]
RP FUNCTION, DNA-BINDING, INTERACTION WITH MCM, AND PHOSPHORYLATION.
RX PubMed=16150924; DOI=10.1093/nar/gki807;
RA Kasiviswanathan R., Shin J.H., Kelman Z.;
RT "Interactions between the archaeal Cdc6 and MCM proteins modulate their
RT biochemical properties.";
RL Nucleic Acids Res. 33:4940-4950(2005).
RN [5]
RP FUNCTION, DNA-BINDING, INTERACTION WITH MCM, AND DOMAIN.
RX PubMed=16740965; DOI=10.1128/jb.00168-06;
RA Kasiviswanathan R., Shin J.H., Kelman Z.;
RT "DNA binding by the Methanothermobacter thermautotrophicus Cdc6 protein is
RT inhibited by the minichromosome maintenance helicase.";
RL J. Bacteriol. 188:4577-4580(2006).
RN [6]
RP FUNCTION.
RX PubMed=18390662; DOI=10.1128/jb.00233-08;
RA Shin J.H., Heo G.Y., Kelman Z.;
RT "The Methanothermobacter thermautotrophicus Cdc6-2 protein, the putative
RT helicase loader, dissociates the minichromosome maintenance helicase.";
RL J. Bacteriol. 190:4091-4094(2008).
CC -!- FUNCTION: Involved in regulation of DNA replication. May play an
CC essential role in origin recognition. Binds to DNA, with a preference
CC for origin-specific double-stranded sequences. Does not bind single-
CC stranded DNA. Inhibits MCM helicase activity but does not affect its
CC oligomeric state. {ECO:0000255|HAMAP-Rule:MF_01407,
CC ECO:0000269|PubMed:15358831, ECO:0000269|PubMed:16150924,
CC ECO:0000269|PubMed:16740965, ECO:0000269|PubMed:18390662}.
CC -!- SUBUNIT: Monomer. Interacts with MCM via the WH domain.
CC {ECO:0000269|PubMed:15358831, ECO:0000269|PubMed:16150924,
CC ECO:0000269|PubMed:16740965}.
CC -!- DOMAIN: The N-terminal AAA+ ATPase domain and the C-terminal winged-
CC helix (WH) domain are both required for DNA binding.
CC {ECO:0000269|PubMed:16740965}.
CC -!- PTM: Autophosphorylated on a serine. Phosphorylation is stimulated by
CC binding to MCM. Both single-stranded DNA and double-stranded DNA
CC inhibit the phosphorylation reaction. {ECO:0000269|PubMed:11514535,
CC ECO:0000269|PubMed:16150924}.
CC -!- SIMILARITY: Belongs to the CDC6/cdc18 family. {ECO:0000255|HAMAP-
CC Rule:MF_01407}.
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DR EMBL; AE000666; AAB85889.1; -; Genomic_DNA.
DR PIR; B69055; B69055.
DR RefSeq; WP_010877024.1; NC_000916.1.
DR AlphaFoldDB; O27463; -.
DR SMR; O27463; -.
DR STRING; 187420.MTH_1412; -.
DR EnsemblBacteria; AAB85889; AAB85889; MTH_1412.
DR GeneID; 24854525; -.
DR KEGG; mth:MTH_1412; -.
DR PATRIC; fig|187420.15.peg.1376; -.
DR HOGENOM; CLU_025112_3_1_2; -.
DR OMA; DMLGIIN; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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..382
FT /note="ORC1-type DNA replication protein 1"
FT /id="PRO_0000151008"
FT BINDING 63..67
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 149
FT /note="D->N: No labeling with ATP."
FT /evidence="ECO:0000269|PubMed:11514535"
FT MUTAGEN 334
FT /note="R->A: Abolishes DNA binding."
FT /evidence="ECO:0000269|PubMed:15358831"
SQ SEQUENCE 382 AA; 43875 MW; FE81374BE134961C CRC64;
MNIFDEIGDK ESVFKDKKYL DHRFLPDRLP HREEQIRSIA KYWVEALNGV TPPDITIYGK
TGTGKTAVAK FAMKQLKEAS KDCDVNIRTE YIRCTDYTTE YQVIARLCQQ LGRDVPYRGW
TKAEIVNTFR NMFKKNAFGQ DMILMVVLDE IDILLRNDGD GLLYTLTRTD NVSILSISNY
VEFKKFIKPR VRSSLRDREI VFPPYGAQQL VDILEERSKM SFKEGALDDD VIPLCAALAA
KEEGDARYAL DLLRTAGEIA DERDSDKVLG DFVREAKDYI EHNKITDIIL TLPSQQQRVL
EAILYLTKRK EEITSGRLYE VYKEIAKGDS VSYRRIFDFI NELEMLGLIS TNTVSRGRGK
GRTNIIDLQC ETSLLEDSLW GV
