ID A0A2I0PPP8_9EURY Unreviewed; 374 AA.
AC A0A2I0PPP8;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=ORC1-type DNA replication protein {ECO:0000256|HAMAP-Rule:MF_01407};
GN Name=cdc6 {ECO:0000313|EMBL:PKL68157.1};
GN ORFNames=CVV30_09470 {ECO:0000313|EMBL:PKL68157.1};
OS Methanomicrobiales archaeon HGW-Methanomicrobiales-1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales.
OX NCBI_TaxID=2013817 {ECO:0000313|EMBL:PKL68157.1, ECO:0000313|Proteomes:UP000233367};
RN [1] {ECO:0000313|EMBL:PKL68157.1, ECO:0000313|Proteomes:UP000233367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGW-Methanomicrobiales-1 {ECO:0000313|EMBL:PKL68157.1};
RX PubMed=28350393; DOI=10.1038/ismej.2017.39;
RA Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., Anantharaman K.,
RA Probst A., Burstein D., Thomas B.C., Banfield J.F.;
RT "Potential for microbial H2 and metal transformations associated with novel
RT bacteria and archaea in deep terrestrial subsurface sediments.";
RL ISME J. 11:1915-1929(2017).
CC -!- FUNCTION: Involved in regulation of DNA replication.
CC {ECO:0000256|HAMAP-Rule:MF_01407}.
CC -!- SIMILARITY: Belongs to the CDC6/cdc18 family. {ECO:0000256|HAMAP-
CC Rule:MF_01407}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKL68157.1}.
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DR EMBL; PGYM01000003; PKL68157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0PPP8; -.
DR Proteomes; UP000233367; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 NCBIfam; TIGR02928; orc1/cdc6 family replication initiation protein; 1.
DR PANTHER; PTHR10763; CELL DIVISION CONTROL PROTEIN 6-RELATED; 1.
DR PANTHER; PTHR10763:SF32; ORC1-TYPE DNA REPLICATION PROTEIN 2; 1.
DR Pfam; PF13401; AAA_22; 1.
DR SMART; SM01074; Cdc6_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01407}; Cell cycle {ECO:0000313|EMBL:PKL68157.1};
KW Cell division {ECO:0000313|EMBL:PKL68157.1};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_01407};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01407}.
FT DOMAIN 300..373
FT /note="Cdc6 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01074"
FT BINDING 62..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01407"
FT BINDING 206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01407"
FT BINDING 218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01407"
SQ SEQUENCE 374 AA; 42751 MW; 00507B9D846DD2A7 CRC64;
MKKNLLMWDE TLFRDPEVLE IDYVPEQFEF RDPQMQELAF QIRPALRGGR PLNTVCKGLP
GTGKTTSVRK LFAEIEETTK KLVPVYINCQ IDNTKFAIIS QIYKKLAGHL PPSSGTSFKQ
VFDAVARILV KDEIVLLVAL DDANYLLYEN EINKVLYTLL RSHEAYEGTR IGVIVIISDM
DVDLSRAVDA RVSSVFLPIE IYFEPYGDAE VREIMKARVM EGLFTGVLSE DLLSLVVEKT
LACGDLRVGI DLLKRATLSA ERAARRSIER EDICGAYEIS KYLHLSYTVK TLKDEERQIL
KSFAERSLKE SEMNAGEVYK SIKESLSIGY TRFYEIVKKM DALRLINLQY RDGKGRTRII
TLRYEPAKVL EYLS
//
