ID A4YID4_METS5 Unreviewed; 417 AA.
AC A4YID4;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=ORC1-type DNA replication protein {ECO:0000256|HAMAP-Rule:MF_01407};
GN OrderedLocusNames=Msed_2046 {ECO:0000313|EMBL:ABP96186.1};
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549 {ECO:0000313|EMBL:ABP96186.1, ECO:0000313|Proteomes:UP000000242};
RN [1] {ECO:0000313|EMBL:ABP96186.1, ECO:0000313|Proteomes:UP000000242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
RC {ECO:0000313|Proteomes:UP000000242};
RX PubMed=18083856; DOI=10.1128/AEM.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
CC -!- FUNCTION: Involved in regulation of DNA replication.
CC {ECO:0000256|HAMAP-Rule:MF_01407}.
CC -!- SIMILARITY: Belongs to the CDC6/cdc18 family.
CC {ECO:0000256|ARBA:ARBA00006184, ECO:0000256|HAMAP-Rule:MF_01407}.
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DR EMBL; CP000682; ABP96186.1; -; Genomic_DNA.
DR AlphaFoldDB; A4YID4; -.
DR STRING; 399549.Msed_2046; -.
DR KEGG; mse:Msed_2046; -.
DR eggNOG; arCOG00467; Archaea.
DR HOGENOM; CLU_025112_3_2_2; -.
DR Proteomes; UP000000242; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd08768; Cdc6_C; 1.
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:SF26; CELL DIVISION CONTROL PROTEIN 6 HOMOLOG; 1.
DR PANTHER; PTHR10763; CELL DIVISION CONTROL PROTEIN 6-RELATED; 1.
DR Pfam; PF13401; AAA_22; 1.
DR Pfam; PF09079; Cdc6_C; 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|HAMAP-Rule:MF_01407};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_01407}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01407};
KW Reference proteome {ECO:0000313|Proteomes:UP000000242}.
FT DOMAIN 318..402
FT /note="Cdc6 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01074"
FT BINDING 72..76
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"
FT BINDING 230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01407"
SQ SEQUENCE 417 AA; 47716 MW; 46D1831F76374F72 CRC64;
MKVTTNLEDI IESGLSGSTI FKQQKVLSPD HIPSRLPHRE EKIKELSLAF RELTTNMGST
SVRVVVSGPT GTGKTVTTKS FGEALKKRLN ERGLRLEYIH ANCHSQRTLY LLTMEIASHL
KLPIPVRGLS SQEAFKIIHD YLVKRNIHLI LTLDEFDYLI NTSSYEDIYF LVRLYDELSS
ASRHISYIFI MRDEQNLYTL DRSIRDHILR NVIRLEPYKS NELKDILMDR VNEAFYPNVV
PDETVEYISN LYGHDKGGSG NARLAIEALE VAGKIAEARN SPLVLIEHVK EANSRINVEA
GEILDEIPLL DLHLLIMLKA LINLHNRLKV DSVPIGKLEK EYAELCAELG EEPRRHTQIY
EYVRRMKLMG ILETQQSGKG MRGRTTLISL SVPITQDFED LITKNLRMKL DNREEPV
//