ID A0A0G0PTC8_9BACT Unreviewed; 947 AA.
AC A0A0G0PTC8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=UT63_C0081G0001 {ECO:0000313|EMBL:KKR31143.1};
OS Candidatus Gottesmanbacteria bacterium GW2011_GWC2_39_8.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1618450 {ECO:0000313|EMBL:KKR31143.1, ECO:0000313|Proteomes:UP000034539};
RN [1] {ECO:0000313|EMBL:KKR31143.1, ECO:0000313|Proteomes:UP000034539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKR31143.1}.
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DR EMBL; LBXN01000081; KKR31143.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0PTC8; -.
DR PATRIC; fig|1618450.3.peg.1391; -.
DR Proteomes; UP000034539; 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; 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 Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 284..449
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 947 AA; 109089 MW; 56401D77638424EB CRC64;
MIFLNEDTLV QQTTADYLRD GLGWDSIYAY NQETFGSEGF LGRKSDREVV LTRYLKDALK
KFNPNLPETA YDEAIRQVVD YSQSQSMLSS NYDKYQLFKD GVLVSYQGDH GEIKKERLRL
FDFNTATNNH FLAVRELWIQ GNLYRRRIDI VGFINGIPLL FVECKNIHKD LKNAFERNFA
DYKDTIPHFF HHNAIVMLAN GDKAKIGTIT AGYEHFHEWK RLSETDHGVV DMETLLKGVC
DKKNFMDIFE NFIVYDDSTG KQIKVLAKNH QYLGVNKVIK SLNDPTRAKG KLGVFWHTQG
AGKSYSMVFF STKVHRKIGG NYTFLICTDR EDLDTQIYKT FAGCGVADND KTPCRPSSGR
NLGELMSQQK AYVFTTIQKF NQEVDPDEGY TKRDDIIVMT DEAHRTQYGT LSLNMRNALP
NANFIGFTGT PLFTNDQITE KVFGKYISTY DFQRAVEDKA TVPLYYDSRG DTLGVATNDI
NERIAEKLEE IENDDIDVSQ RLEKELKRDY HIITAEKRLN QIAKDFVDHY STSWEAGKAM
FVCIDKLTCV RMHKLIGQYW DQKTEEIKES WKMASGEEKD QLANQLAWMG ETKMAVIVSE
EQGEVEKFRK WGFDITPHRR LIKNGFELSD GMRIDVDSAF KKEEHQFRIA IVCAMWLTGF
DVPSLANLYL DKPLKAHTLM QAIARANRVN GDKNNGLISD YCGILKNLRK ALATFTGTGD
TGRTGGLGPD ELDPTRTKEE LLKDLKETIE LVSNYLHDRK ASHDAIMNAS GFERNKAIII
AKEAVNENDE TRKKFEVMCR EVFIKFKACL TIPGVNTYRD HYSAINIIYK SLQKDRDQAD
ISDIIKQLHE VIDEAITVTP DRVKESSLPY DISKINFDRL RKEFEHTKTK NTTVQSLKSV
IEKKLQPLIQ RNPLRTDFQE HYETIIDEYN KEKDRKSRLK CQNMCLN
//
