ID D4GVY5_HALVD Unreviewed; 740 AA.
AC D4GVY5;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN Name=rmeR {ECO:0000313|EMBL:ADE04905.1};
GN OrderedLocusNames=HVO_2269 {ECO:0000313|EMBL:ADE04905.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800 {ECO:0000313|EMBL:ADE04905.1, ECO:0000313|Proteomes:UP000008243};
RN [1] {ECO:0000313|EMBL:ADE04905.1, ECO:0000313|Proteomes:UP000008243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC VKM B-1768 / DS2 {ECO:0000313|Proteomes:UP000008243};
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give random double-stranded
CC fragments with terminal 5'-phosphates, ATP is simultaneously
CC hydrolyzed.; EC=3.1.21.3; Evidence={ECO:0000256|ARBA:ARBA00000851};
CC -!- SIMILARITY: Belongs to the HsdR family.
CC {ECO:0000256|ARBA:ARBA00008598}.
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DR EMBL; CP001956; ADE04905.1; -; Genomic_DNA.
DR RefSeq; WP_013035629.1; NZ_AOHU01000042.1.
DR AlphaFoldDB; D4GVY5; -.
DR STRING; 309800.HVO_2269; -.
DR REBASE; 25107; HvoDSIIP.
DR PaxDb; 309800-C498_06610; -.
DR EnsemblBacteria; ADE04905; ADE04905; HVO_2269.
DR GeneID; 8925854; -.
DR KEGG; hvo:HVO_2269; -.
DR eggNOG; arCOG00880; Archaea.
DR HOGENOM; CLU_020974_0_0_2; -.
DR OrthoDB; 11644at2157; -.
DR Proteomes; UP000008243; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009035; F:type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR CDD; cd18032; DEXHc_RE_I_III_res; 1.
DR CDD; cd18799; SF2_C_EcoAI-like; 1.
DR Gene3D; 3.90.1570.30; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR013670; EcoEI_R_C_dom.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR Pfam; PF08463; EcoEI_R_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADE04905.1};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008243};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 172..336
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 524..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 740 AA; 85632 MW; 21A0D56000437E86 CRC64;
MADKGTDPED EAREVIDTQL KEAGWKDLEE EGGDTGFERE YSTSSGPVDY ALLVSGKPIA
VVEAKEAQKD AYAALTQSKR YAQDIGTGEN YAGRYGVPFV FTANSDEVWF QDLREEAPRE
RKLRSFHRPD GLEQFLNTDY KAAKEWLEDT PIRESDSNLW DNQFEAIQSI EESLQENKRR
MLVQMATGTG KTRMACAQTY RLLKSGYVNS VLFLVDRNSL GNQAESAFKN YDVGPAMKLS
DIYIIEQVED GVYPENADIV IATLQGMYSL LENHDELDIP QDAFDFIISD ESHRSIYGDW
RVVLNHFDAL QLGLTATPAT HTLSYFNENW VYQYGYWQAV DDGHVVPYET YRIQTGITMD
GLYYEDEEYE PGDLENKITV PSTNRLIAEE FRKQSGEDEK TLVFAKNDRH ATELEKIFRE
VYSDKDDRYV KKITYTTDDP DGWIKRFRNQ KYPKIAVTVD MVSTGVDVKP IENIIFIRPT
RSAVLYNQMI GRGTRTCDEI GKEKFTIYDC IGIVDYFSET PPFNTYRPDG TVDEEKSGQK
EREDDEDDEI IVADDVQDHL EFSGYMFETK DGQELRPDDY VTHFERYVRQ NQSEIEAIKI
IMESPEALKR KHLRELNRKL QDEPEKFSEE KLQKAYGQEM TDIIGFIKHA LGEDEFPTTE
DRVERAFSAW MQDKDFTEQE REWLNLLKRH FVQEKVIKKE DFNYVPFSRH GGWNSAAEAF
GGEEELKDVL QELNEDVILA
//
