ID A0A102DCN3_9SPHN Unreviewed; 976 AA.
AC A0A102DCN3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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};
GN ORFNames=AQZ49_06585 {ECO:0000313|EMBL:KUR79073.1};
OS Novosphingobium sp. FSW06-99.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1739113 {ECO:0000313|EMBL:KUR79073.1, ECO:0000313|Proteomes:UP000061032};
RN [1] {ECO:0000313|EMBL:KUR79073.1, ECO:0000313|Proteomes:UP000061032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSW06-99 {ECO:0000313|EMBL:KUR79073.1,
RC ECO:0000313|Proteomes:UP000061032};
RA Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA Glaeser S.;
RT "Draft genome sequence of Novosphingobium sp. FSW06-99 (=LMG 27919), a
RT Novosphingobium acidiphilum related species isolated from a surface water
RT sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUR79073.1}.
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DR EMBL; LLZQ01000006; KUR79073.1; -; Genomic_DNA.
DR RefSeq; WP_067614143.1; NZ_KQ954253.1.
DR AlphaFoldDB; A0A102DCN3; -.
DR STRING; 1739113.AQZ49_06585; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000061032; Unassembled WGS sequence.
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; 2.
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 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 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, 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 Reference proteome {ECO:0000313|Proteomes:UP000061032};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 267..434
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 976 AA; 109943 MW; 91E181F04AF53FF9 CRC64;
MTDLAISEAG SVQFPMVRHA AEIGWTPLMP DDARAKRGSE AAMFLRDELE GAIARFNPWL
APDAVRSIFE TLDAIPATIE GNRAMLGWMR GEQSWYDENE KRHRRVTLID YEHISANAFH
VTWEWTLKPP ARKGNRADVL FLINGLPVAI VEHKNPKDGN AMERAIVQLR RYEAETPELL
GAPQLFNVTH LIDYWYGVTW NANRRFIARW KEAREETYRF AVQAFFERTD FLRTLQHWVL
FYVEDNETRK SVLRQHQRRA IDAVVARCAD PAKRRGLVWH TQGSGKTFTL LTAAKLILED
KERFDNATVI LVVDRTELEG QLKGWVERLL GEMQKQDIAT RRANSKDDLQ ALLDADFRGL
VIAMIHKFEG ITKGSADRAN IHVFIDEAHR SVAKDLGSYL MGAVPNATII GFTGTPIADT
ERGKGTFKIF GADDERGYLD KYSIRESIDD ETTLPIKHVM APSTMTVPLD RIDREFFALA
EAEGISDIEE LNRVLDRAVG LRAFLKADDR VANVAKFIAD HFRENVLPLG YKAFVVAVDR
EACAKYKREL DKHLPPEWSE AIYTSNVNDA VERPDVAALQ LTDDRESDVR LLFKKPAEEP
KILIVTDKLL TGYDAPVLYA MYLDKPMRDH VLLQAIARVN RPYVDSEGVR KPIGLVVDFV
SVLRDLKKAL KFDSEDVSGV IEDLDLLLTD FLGKIAVAKT EFLDAGESGS ADERLEALVY
GRFLDPEPRK AFFEAYKDIE NLWEILSPSA ELVDHIATFK RLAQLYATVR NAYADQVGFV
ADLAYKTRRL VEANAEQSGL GNLTKTVTFD VKTLDALRDS KGSDEGKVFN LVRGLQKEVD
DDQANAPILQ PLKDRAERIL KDMESRNVNG LAAIDLLGAL AAEKEALLAE AKASGLSAEA
FGVMIALRGD PALVDGKIDV RQVAGLIDEL RNRYPNAKLN DDERRRLRGA LYLPLLSLSD
DDRSRIVDLI MRSLLS
//
