ID I4WGZ9_9GAMM Unreviewed; 1071 AA.
AC I4WGZ9; M4NMR9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=R2APBS1_3887 {ECO:0000313|EMBL:AGG90938.1};
OS Rhodanobacter denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=666685 {ECO:0000313|EMBL:AGG90938.1, ECO:0000313|Proteomes:UP000011859};
RN [1] {ECO:0000313|EMBL:AGG90938.1, ECO:0000313|Proteomes:UP000011859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2APBS1 {ECO:0000313|EMBL:AGG90938.1,
RC ECO:0000313|Proteomes:UP000011859};
RG US DOE Joint Genome Institute;
RA Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Munk A.C.C., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Peters L., Pitluck S., Woyke T., Prakash O., Elkins J., Brown S.,
RA Palumbo A., Hemme C., Zhou J., Watson D., Jardine P., Kostka J., Green S.;
RT "Complete genome of Rhodanobacter sp. 2APBS1.";
RL Submitted (APR-2012) 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}.
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DR EMBL; CP003470; AGG90938.1; -; Genomic_DNA.
DR RefSeq; WP_007514462.1; NZ_CP088922.1.
DR AlphaFoldDB; I4WGZ9; -.
DR STRING; 666685.R2APBS1_3887; -.
DR REBASE; 51748; RdeR2ORF846P.
DR REBASE; 51961; Rsp24678ORF17055P.
DR KEGG; rhd:R2APBS1_3887; -.
DR PATRIC; fig|666685.9.peg.3613; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_005762_1_0_6; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000011859; 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; 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; 4.
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.
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 266..519
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|SMART:SM00487"
SQ SEQUENCE 1071 AA; 119161 MW; F4973D5433EFCF49 CRC64;
MTPILLEDHL EQAALQWLAG LGWEVAHGPD ISPPDAHTPG SERDSYRQVV LEHRLRDAIR
RLNPRIPATA QDEALRIVLN PNIPGPLQAN RQLHRWLTEG VPVQFQQGNE TRGDLVRLVD
FDDVRGNDWV AVNQFSIQGP KRTRRPDLLL FLNGLPIVLL ELKNPGDENA DIWSAFNQVQ
AYREDIPDLF IYNTLVVISD GIRARMGSLS AERERYMAWR TIDGAQTDPL GEMRELETLV
HGAFDRALLL AYLRNFILFE DDGALVKKVA GYHQFHAVRA VVESVLAASK PGGSRKGGVV
WHTQGAGKSI EMTCLAGTLM QHPAMGNPTI VVVTDRNDLD NQLFGVFAGV ADLLRETPVQ
ADTRPRLREL LGNRPSGGII FTTIQKFTPG EDEDVFPVLS ERQNIVVICD EAHRTQYGFE
AKLTGDLAKA KPAKMAADAA GSVAMAALMS HEASASYASS VRYGYAQHLR DALPNATFVA
FTGTPVSLTD RDTRAVFGDY VHVYDIEQAV KDGATVPIYY ESRLAKLELS DGDIDALDEE
VDELNEGAID DPSHAARIRR WAALEKVVGA APRIQKVASD IVEHFENRLA AMDGKAMIVA
MSREICVHLY DAIVALRPEW HAADPEKGVI KIVMTGSAAD KPMLKPHVYP KETRKRLERR
YKDSADPFKL VIVRDMWLTG FDAPCLHTMY IDKPMRGHNL MQAIARVNRV FKDKPGGLVV
DYIGIANELK QALADYTQAK GRGSPTIDAE EALEVLVERM ELLHGMLHGY DYAAFRAQAW
ALLPGAANHV LGLDDGKQRF ADQVLAATKA FALCCTLDAA LAYRDELAFL QAIKSAITKH
ATTDKKLSDE QKEHALRQII SRAVVSDQVI DIFAAAGLKR PDIGVLSEEF LQDMRHMKER
NLAVELLDRL LKGEIKSRFK TNVVQSAKFS ELLQASLTRY RNRAIETAQV IEELIAMAKK
FQQAAEHGDA LGLNRDEVAF YDALANNESA VRELGDETLR KIAVELTQKL RNSVTVDWAV
RDSVRAKLRV MVKTLLRRYK YPPDKQDEAV EIVLRQAETL TNTWAGAEQL G
//
