ID E6J4K6_9ACTN Unreviewed; 860 AA.
AC E6J4K6;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=ES5_00667 {ECO:0000313|EMBL:EFV93469.1};
OS Dietzia cinnamea P4.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC Dietzia.
OX NCBI_TaxID=910954 {ECO:0000313|EMBL:EFV93469.1, ECO:0000313|Proteomes:UP000004165};
RN [1] {ECO:0000313|EMBL:EFV93469.1, ECO:0000313|Proteomes:UP000004165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P4 {ECO:0000313|EMBL:EFV93469.1,
RC ECO:0000313|Proteomes:UP000004165};
RX PubMed=21901521; DOI=10.1007/s10482-011-9633-7;
RA Procopio L., Alvarez V.M., Jurelevicius D.A., Hansen L., Sorensen S.J.,
RA Cardoso J.S., Padula M., Leitao A.C., Seldin L., van Elsas J.D.;
RT "Insight from the draft genome of Dietzia cinnamea P4 reveals mechanisms of
RT survival in complex tropical soil habitats and biotechnology potential.";
RL Antonie Van Leeuwenhoek 101:289-302(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:EFV93469.1}.
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DR EMBL; AEKG01000029; EFV93469.1; -; Genomic_DNA.
DR RefSeq; WP_007626256.1; NZ_AEKG01000029.1.
DR AlphaFoldDB; E6J4K6; -.
DR Proteomes; UP000004165; 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; 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 284..465
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 596..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 95819 MW; 345FA6EDC386643C CRC64;
MIKVDETLVE LAAMSYFKDL GYETGSGPDL AHDGPSPERL SYGDVFLRER LRRALVRLNP
DHLDLIDEAL ADIERAESQS PVAENYRIHR LLTEGAHVEY RDIGGGIRTA TVRFFDFDDP
DNNDWLAVRQ FTIDENRVRR PDLVVFVNGL PVAVGEWKNP TSEAASLKVA WQKIQSYRSD
IPSLFLTNAL TVLSDGTTAS VSTFTANFEH YAPWKAIAGP EPVKGMPALK VLIYGAFDKS
RLLDLIKNFV VFSDEGGGKI IKRIAKYHQF WAVNKAVEST VIASGPDGDQ RGGVVWHTQG
SGKSFEMLFY AVKTMRDPRM NNPTLVFLTD RNDLDDQLYE EVFGQAMILP ERPIRADTRA
ELRELLRRSS GGIIFTTLQK FAPTGGAESN PSLTDRRNVI VVADEAHRSQ YGFSSRLTKD
GRIRTGLAKH LRDALPGATF LGFTGTPIES TDKSTQAVFG DYIDVYDLTR AVEDGATVKI
YYESRLAKVA LSEDDLDALD ALADEITEGS DEELARKTVS KWSRVEAVVG SEQRLDMVAA
DIVKHWEKRQ AEMPGKAMIV TMSRRIAVRL YEKIVALRPD WHSDDHEQGR IKVVMTGTSD
DPPEYQPHVY DKQQRRDIKD RAKDPTSDLE LVIVRDMWLT GFDSPSMHTM YLDRSLKGAG
LMQAIARVNR TFRDKPGGLV VDYFGLFANL QEALREYSPS DRSQAGVPIE ELVNVILEKH
DVIRGILHGC DYNSCPSLPS GKRLEEVSKV TDFVLEDEDR RTRFLDEVLA LVKAFALAGS
REEVQSVADD IRLFTSARAA VLKIISPDSG AGGSGSPELD TAISQLVNQA VTGESVLDVY
AMAGETRHQD VSSNSSWQCQ
//
