ID F2J3N3_POLGS Unreviewed; 1071 AA.
AC F2J3N3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 OrderedLocusNames=SL003B_3748 {ECO:0000313|EMBL:ADZ72169.1};
OS Polymorphum gilvum (strain LMG 25793 / CGMCC 1.9160 / SL003B-26A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Polymorphum.
OX NCBI_TaxID=991905 {ECO:0000313|EMBL:ADZ72169.1, ECO:0000313|Proteomes:UP000008130};
RN [1] {ECO:0000313|EMBL:ADZ72169.1, ECO:0000313|Proteomes:UP000008130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25793 / CGMCC 1.9160 / SL003B-26A1
RC {ECO:0000313|Proteomes:UP000008130};
RX PubMed=21478361; DOI=10.1128/JB.00333-11;
RA Li S.G., Tang Y.Q., Nie Y., Cai M., Wu X.L.;
RT "Complete genome sequence of Polymorphum gilvum SL003B-26A1T, a crude oil-
RT degrading bacterium from oil-polluted saline soil.";
RL J. Bacteriol. 193:2894-2895(2011).
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; CP002568; ADZ72169.1; -; Genomic_DNA.
DR RefSeq; WP_013654478.1; NC_015259.1.
DR AlphaFoldDB; F2J3N3; -.
DR STRING; 991905.SL003B_3748; -.
DR REBASE; 33911; Pgi3ORF3751P.
DR KEGG; pgv:SL003B_3748; -.
DR PATRIC; fig|991905.3.peg.3866; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_005762_0_1_5; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000008130; 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:UP000008130};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 325..492
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1071 AA; 121688 MW; 3269EE4BD8511CD9 CRC64;
MTFNAAEKHQ SQVPALQLLV ALGFKPLSQE EALRLRGGRL RNVVLDDVLA EQLMRINRFT
HRGREYGFDL EDAHEAMRRL KPTPDRLKGL RGTNQDIYDT LVLGTTITKS IDGDSKSYSF
RYIDWEQPEN NVFHVTAEFS VERTASSQTK RCDIVAFVNG IPILVIENKR PTESLKKADS
QLIGYQNEDN IPQLFHFAQL LTAMNRNEAR YATVGTPRKF WQTWRDEEDT DEAIAPFANR
VLTAVEKDAI FSGDFAGARA YFDAMAAEGD RAVTVQDRTV YALCRPERLL DLIRRFTVFD
GGVRKVARHQ QFFGIRRAVE TVKQHDVSGA RKGGVIWHTQ GSGKSLTMVM LGRSLALERS
IENPRIIIVT DRDDLDKQIK DTFKSCDLEP VRATSGSHLL ELVQNKAPLV TTIINKFDTA
LRNSKLADDD PNIFVLVDES HRTQTGRYGG HSQFAAKMRR LLPKACYLGF TGTPLLKKEK
NTLSTFGRLI HRYAIDEAVA DGAVVPLLYE GRLVEQQVSG AVIDRWFDKI SEGLTDSQKA
DLKRKFSRMD ALAKTDQAIR AKAFDISEHY RQHWQGTGFK AQLVAPSKAA AVRFKEVLDE
IGHVSSAIVI SPPDENEGNE EVDQESKDLV RRFWSQMMAR YKTEEEYNRQ IIDAFKGSGD
PEILIVVSKL LTGFDAPRNT VLYVCKSLKE HNLLQAIARV NRLYEDGGTE KEFGFIVDYE
GLLGELDSAL TTYSAFEGYE AADLAGTVHD VREEIRKLPQ LHDQLWDLFK PVRNKKDMEQ
FEQHLADEAL RHDFYARLKA FSRCLHISLS SDKLFDVFDE TKVDALKRDW KQFSELKRSV
QLRYQETVDV REFEPKIQKL LDDHVVAMPA ETIIEVVNIN DPDALKAVVE ETGVSEASRA
DRIASATRRA ITEKMDEDPT FYKQFSELLE ETIRAYREKR LSEREYLNSV VDLASKVARK
DRGRDVPESI RGDEDAQAFF GILDGQLKTN GDEPVASDDS AAIAQQIIEI VKSHLIVDIW
SNEVAQNNLR NAIDDYFFDV LRDERGIDLP VEVLDDLELK IMDLARARFA A
//
