ID W8RWQ4_9RHOB Unreviewed; 1030 AA.
AC W8RWQ4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=roselon_03528 {ECO:0000313|EMBL:AHM05783.1};
OS Roseibacterium elongatum DSM 19469.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseibacterium.
OX NCBI_TaxID=1294273 {ECO:0000313|EMBL:AHM05783.1, ECO:0000313|Proteomes:UP000019593};
RN [1] {ECO:0000313|EMBL:AHM05783.1, ECO:0000313|Proteomes:UP000019593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19469 {ECO:0000313|Proteomes:UP000019593};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (MAR-2013) 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; CP004372; AHM05783.1; -; Genomic_DNA.
DR RefSeq; WP_025313399.1; NZ_CP004372.1.
DR AlphaFoldDB; W8RWQ4; -.
DR STRING; 1294273.roselon_03528; -.
DR REBASE; 81160; Rel19469ORF3525P.
DR KEGG; red:roselon_03528; -.
DR PATRIC; fig|1294273.3.peg.3485; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_005762_1_0_5; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000019593; 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; 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 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; 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:UP000019593};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 281..462
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1030 AA; 114293 MW; D97CB9C5664EC7B7 CRC64;
MAWNSESDLE DWMMGKLAGL GYAADSGAEI SPEKRDPERR SFHEAILRKV FEKAVRRLNP
GLPDGAVQEV MARVTDEVFA GDLMAENRRL HGLMTGGVPI TYFSQGEERH ERARLIDWGD
QDNAWHAFNQ VDMVGRNLRI PDIVIYLNGL PLVVVELKGT EGADIEAAFN QIETYKADIP
NLFRTSVFSV ISDGLNARYG TLSAGLDRFM KWRTVDGETI LSEREGLALN TLTEGLLNRP
VLLDMLRWFT VFEDEGKGPI KKAAGYHQFH AVRKAMESII GARGDNGKGG VIWHTQGSGK
SLLMTFLAGR AMHLPELENP TVLILTDRND LDNQLFATFG RCKDLLGEMP VQADSIQELK
TLLNRQVGGI VFSTIQKFRP ERGQDFPELT DRSNVIVMVD EAHRTQYGFE ARMDQKTGEL
RHGLAHHLRA ALPRAVYVAF TGTPVELVGA NTRSVFGDYI DVYDIAQAVE DGATVPIYYE
GRVARVEIAD DLRDSLDEEF DEATEALPED EAGAAARKWS QIEKLVGAGP RLYAVVADIL
EHFDARLEAI DGKAMIVCMS RRICVEVYER IVAARPDWHS ETDESGAVKV VMTGNATDPP
NFQPHIRSKA KLEALRKRYK DTGDPLKLVI VRDMWLTGFD APCMHTLYVD KPMKGHGLMQ
AIARVNRVFA GKPAGLVVDY IGLAADLKKA LAHYSQGDQA QTGVDEREAV SAFLSALDVA
RGLFHGFDYS RVLGGTAADR IEILPAAADH VLHQARADGK EGHKDFGKRF LDAVAALAKA
FKLAAGSPEA KQHAEEVAFF LAVRSALQKL DVKGGGGRNS SPDFAIEQLL NRAVASTEVV
DILEACGFDR PDISVLSEEF LLEIQHMQHK NLAVEALKKL LNGEIQARTR GNVVQNQKFS
ERLTNAIARY HNRSVDALQV IQELIGMAKD LSAEPEDDMS EAERSFYDAL AQNESAVEVM
DNDQLKVIAA ELVRSVRENS GVDWWQRDDV RAKMRVAVKR ILRRYGYPPD LQAEAVKLVI
KQAEAMARSM
//
