CDC62_METTH
ID CDC62_METTH Reviewed; 379 AA.
AC O27636;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, 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=MTH_1599;
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 LYS-71 AND ASP-148.
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, AND DNA-BINDING.
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. Dissociates the
CC MCM complex and inhibits the MCM helicase activity, suggesting that it
CC may function as a helicase loader. Binds to both specific and random
CC double-stranded or single-stranded DNA. {ECO:0000255|HAMAP-
CC Rule:MF_01407, ECO:0000269|PubMed:15358831,
CC ECO:0000269|PubMed:16150924, ECO:0000269|PubMed:16740965,
CC ECO:0000269|PubMed:18390662}.
CC -!- SUBUNIT: Interacts with MCM. {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 inhibited 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; AAB86072.1; -; Genomic_DNA.
DR PIR; D69080; D69080.
DR RefSeq; WP_010877207.1; NC_000916.1.
DR AlphaFoldDB; O27636; -.
DR SMR; O27636; -.
DR STRING; 187420.MTH_1599; -.
DR EnsemblBacteria; AAB86072; AAB86072; MTH_1599.
DR GeneID; 1471868; -.
DR KEGG; mth:MTH_1599; -.
DR PATRIC; fig|187420.15.peg.1563; -.
DR HOGENOM; CLU_025112_3_0_2; -.
DR OMA; YLFYENE; -.
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 Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01407; ORC1_type_DNA_replic_protein; 1.
DR InterPro; IPR015163; Cdc6_C.
DR InterPro; IPR014277; Orc1/Cdc6_arc.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036390; WH_DNA-bd_sf.
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..379
FT /note="ORC1-type DNA replication protein 2"
FT /id="PRO_0000151009"
FT BINDING 69..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01407"
FT BINDING 211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01407"
FT BINDING 223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01407"
FT MUTAGEN 71
FT /note="K->E: No labeling with ATP."
FT /evidence="ECO:0000269|PubMed:11514535"
FT MUTAGEN 148
FT /note="D->N: Retains some ability to be labeled."
FT /evidence="ECO:0000269|PubMed:11514535"
FT MUTAGEN 337
FT /note="R->A: Decrease in dsDNA binding and strong decrease
FT in ssDNA binding."
SQ SEQUENCE 379 AA; 43302 MW; 48692C544BF94D01 CRC64;
MKGDKRRDIR DILLHDETLF RNMNAFDPDY VPENYRYRES QMEALAVCIR PALRNGRPVN
AVILGSCATG KTTAIKKIFE MVESTSEGVV CCYINCQLHT TRFGIFSQIY SKIFGHQPPE
TGVPFSRIYQ TIMQHLASEK RALVVALDDI NHLFYSKNAN KVLYDILRAH EVFEGVRTGV
FAVLSDIEFR YALDKNVDSI FIPQEIVFPP YTREEVFNIL RDRVRVGFYP GVISDELLER
ITDHTMDTGD LRYGIDLLRV CGNLAEADAS PVIGEEHLER ALKSTGPVNL IHTVRTLNEN
EREFLRILAD AGEDMTAGAL YELFRESTGS SYSSFNRIIE KLEFLRLIDT RLTGKGVRGN
SRILIPRFSR EDLRRCPGF
