ID K2DZR8_9BACT Unreviewed; 755 AA.
AC K2DZR8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Type I restriction enzyme endonuclease subunit {ECO:0000256|RuleBase:RU364115};
DE Short=R protein {ECO:0000256|RuleBase:RU364115};
DE EC=3.1.21.3 {ECO:0000256|RuleBase:RU364115};
DE Flags: Fragment;
GN ORFNames=ACD_23C00074G0002 {ECO:0000313|EMBL:EKD99218.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD99218.1};
RN [1] {ECO:0000313|EMBL:EKD99218.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
CC -!- FUNCTION: Subunit R is required for both nuclease and ATPase
CC activities, but not for modification. {ECO:0000256|RuleBase:RU364115}.
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 ECO:0000256|RuleBase:RU364115};
CC -!- SUBUNIT: The type I restriction/modification system is composed of
CC three polypeptides R, M and S. {ECO:0000256|RuleBase:RU364115}.
CC -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000256|ARBA:ARBA00008598,
CC ECO:0000256|RuleBase:RU364115}.
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:EKD99218.1}.
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DR EMBL; AMFJ01008612; EKD99218.1; -; Genomic_DNA.
DR AlphaFoldDB; K2DZR8; -.
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; cd18030; DEXHc_RE_I_HsdR; 1.
DR CDD; cd22332; HsdR_N; 1.
DR CDD; cd18800; SF2_C_EcoR124I-like; 1.
DR Gene3D; 3.90.1570.50; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR InterPro; IPR004473; Restrct_endonuc_typeI_HsdR.
DR InterPro; IPR040980; SWI2_SNF2.
DR InterPro; IPR021810; T1RH-like_C.
DR NCBIfam; TIGR00348; hsdR; 1.
DR PANTHER; PTHR30195:SF15; TYPE I RESTRICTION ENYME HINDI ENDONUCLEASE SUBUNIT; 1.
DR PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF18766; SWI2_SNF2; 1.
DR Pfam; PF11867; T1RH-like_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364115};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364115};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364115};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 282..467
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT NON_TER 755
FT /evidence="ECO:0000313|EMBL:EKD99218.1"
SQ SEQUENCE 755 AA; 84333 MW; 0E465AB9A7549DB1 CRC64;
MTEDQLERDT LAWLQDVGYT HRRGPDIAFD GSSPERADYR QVILPFRLRE AINRLNPSIP
VAAREDALKQ VTDLGIPSLL PSNRAFHKLL VGGVPVQYQK DGETCGDFVR LIDWAHSEKN
EWWAVNQFTI KGAHKTRRPD IILFVNGLPL VLLELKNPAD ENANIWKAFD QIETYKEQIP
DVFQYNEVLV ISDGTDALMG SLSANAERFM AWRTIDGVNL DPLGPFQELQ TLVRGALAPQ
YLLDYIRYFV LFEDDGQLVK KIAGYHQFHA VRAAIEQVVM ASRPGASHKG GVVWHTQGSG
KSITMTCFAA RVMQEPAMEN PTIVVITDRN DLDGQLFGVF SLAQDLLREQ PTQALTRPDL
RTKLGNRPSG GIIFATIQKF MPGEDEDTFP VLSERSNIVV IADEAHRTQY GFKATLKGKP
GEEKYQAGYA QHLRDALPNA TFVGFTGTPV SSTDHDTRAV FGEYIHVYDM QQAKEDGATV
AIYYESRLAK LRLKDEDLPA IDDEVDELAE DEEESQQAKL KSRWAALEKI VGAEPRVASV
AADLVAHFEE RSTAQSGKAM VVAMSREICV HLYNEIIKLR PDWHDPDPEK GAIKIVMTGS
ASDKALLRPH IYDGKVKKRL EKRFKVPADP LRLVIVRDMW LTGFDAPCVH TLYVDKPMKG
HNLMQAIARV NRVFKGKQGG LVVDYIGIGN ELKAAMKEYT ASKGRGTPTV DAREAYSVLM
EKLDVLQAML HGCDYSDFLT GGHQTLARAA NHVLG
//
