CDC62_AERPE
ID CDC62_AERPE Reviewed; 410 AA.
AC Q9YFU8;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=ORC1-type DNA replication protein 2 {ECO:0000255|HAMAP-Rule:MF_01407};
DE AltName: Full=ORC2;
GN Name=orc2; OrderedLocusNames=APE_0152.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-410 IN COMPLEX WITH DNA AND
RP ATP, FUNCTION, DNA-BINDING, AND DOMAIN.
RX PubMed=15465044; DOI=10.1016/j.jmb.2004.08.044;
RA Singleton M.R., Morales R., Grainge I., Cook N., Isupov M.N., Wigley D.B.;
RT "Conformational changes induced by nucleotide binding in Cdc6/ORC from
RT Aeropyrum pernix.";
RL J. Mol. Biol. 343:547-557(2004).
CC -!- FUNCTION: Involved in regulation of DNA replication (By similarity).
CC Binds DNA. {ECO:0000255|HAMAP-Rule:MF_01407,
CC ECO:0000269|PubMed:15465044}.
CC -!- DOMAIN: Contains an N-terminal AAA+ ATPase domain and a C-terminal
CC winged-helix (WH) domain. {ECO:0000269|PubMed:15465044}.
CC -!- SIMILARITY: Belongs to the CDC6/cdc18 family. {ECO:0000255|HAMAP-
CC Rule:MF_01407}.
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DR EMBL; BA000002; BAA79063.2; -; Genomic_DNA.
DR PIR; E72770; E72770.
DR PDB; 1W5S; X-ray; 2.40 A; A/B=2-410.
DR PDB; 1W5T; X-ray; 2.40 A; A/B/C=2-410.
DR PDBsum; 1W5S; -.
DR PDBsum; 1W5T; -.
DR AlphaFoldDB; Q9YFU8; -.
DR SMR; Q9YFU8; -.
DR STRING; 272557.APE_0152.1; -.
DR PRIDE; Q9YFU8; -.
DR EnsemblBacteria; BAA79063; BAA79063; APE_0152.1.
DR KEGG; ape:APE_0152.1; -.
DR PATRIC; fig|272557.25.peg.106; -.
DR eggNOG; arCOG00467; Archaea.
DR OMA; SEIHERY; -.
DR EvolutionaryTrace; Q9YFU8; -.
DR Proteomes; UP000002518; 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; 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; 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 3D-structure; ATP-binding; DNA replication; DNA-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..410
FT /note="ORC1-type DNA replication protein 2"
FT /id="PRO_0000421876"
FT BINDING 60..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01407,
FT ECO:0000269|PubMed:15465044"
FT BINDING 213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01407,
FT ECO:0000269|PubMed:15465044"
FT BINDING 225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01407,
FT ECO:0000269|PubMed:15465044"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:1W5S"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 27..41
FT /evidence="ECO:0007829|PDB:1W5S"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:1W5S"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 63..80
FT /evidence="ECO:0007829|PDB:1W5S"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 120..134
FT /evidence="ECO:0007829|PDB:1W5S"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:1W5S"
FT STRAND 177..186
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:1W5S"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 215..229
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 257..273
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 281..290
FT /evidence="ECO:0007829|PDB:1W5S"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 306..320
FT /evidence="ECO:0007829|PDB:1W5S"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 328..343
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 350..362
FT /evidence="ECO:0007829|PDB:1W5S"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:1W5S"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:1W5S"
FT HELIX 390..405
FT /evidence="ECO:0007829|PDB:1W5S"
SQ SEQUENCE 410 AA; 46005 MW; 28D950272EB88043 CRC64;
MLRHGLFKDR RVFDENYIPP ELRVRRGEAE ALARIYLNRL LSGAGLSDVN MIYGSIGRVG
IGKTTLAKFT VKRVSEAAAK EGLTVKQAYV NAFNAPNLYT ILSLIVRQTG YPIQVRGAPA
LDILKALVDN LYVENHYLLV ILDEFQSMLS SPRIAAEDLY TLLRVHEEIP SRDGVNRIGF
LLVASDVRAL SYMREKIPQV ESQIGFKLHL PAYKSRELYT ILEQRAELGL RDTVWEPRHL
ELISDVYGED KGGDGSARRA IVALKMACEM AEAMGRDSLS EDLVRKAVSE NEAASIQTHE
LEALSIHELI ILRLIAEATL GGMEWINAGL LRQRYEDASL TMYNVKPRGY TQYHIYLKHL
TSLGLVDAKP SGRGMRGRTT LFRLAPHLPA DRLIEVVDNI IQAKMASGYE
