ID A0A108T8K4_BACSE Unreviewed; 976 AA.
AC A0A108T8K4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 Name=hsdR {ECO:0000313|EMBL:KWR55222.1};
GN ORFNames=AA415_01671 {ECO:0000313|EMBL:KWR55222.1};
OS Bacteroides stercoris.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=46506 {ECO:0000313|EMBL:KWR55222.1, ECO:0000313|Proteomes:UP000056419};
RN [1] {ECO:0000313|EMBL:KWR55222.1, ECO:0000313|Proteomes:UP000056419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL09T03C01 {ECO:0000313|EMBL:KWR55222.1,
RC ECO:0000313|Proteomes:UP000056419};
RX PubMed=26768901; DOI=10.1186/s12864-016-2377-z;
RA Coyne M.J., Roelofs K.G., Comstock L.E.;
RT "Type VI secretion systems of human gut Bacteroidales segregate into three
RT genetic architectures, two of which are contained on mobile genetic
RT elements.";
RL BMC Genomics 17:58-58(2016).
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:KWR55222.1}.
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DR EMBL; LRGC01000006; KWR55222.1; -; Genomic_DNA.
DR RefSeq; WP_060385800.1; NZ_LRGC01000006.1.
DR AlphaFoldDB; A0A108T8K4; -.
DR STRING; 46506.AA415_01671; -.
DR PATRIC; fig|46506.5.peg.1778; -.
DR Proteomes; UP000056419; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000056419};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 278..438
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 976 AA; 111764 MW; B83F9D624CC65E3C CRC64;
MFNEDNTVEQ MLIEAATQSS WQYVKSQDIP RSSDSVLVES WLLEALVRLN PITRQQAEQV
IYKLRAAITC GGNYDELVTA NDRFRTLLFN ENTEPFGKDG EYIPIRFFSE DAVEDYCVVT
NQWEFPRSSV EGGKRLDLVY LINGIPVCVG EVKSPVRPQI TWANGAIDML HYEKSIPEMF
VPNILTFATE GKELQYAGIC APVDKWGPWF KDESRQHGTI ESVKSNVMGL VQPNRLLDIY
RYYSVFTGTS SGKKIKIVCR YQQYLGGEAI VQRVLNTYRE KQGPKKGLIW HFQGSGKSWL
MVFAAQKLRL QNELHAPTVV IVDDRIDLED QITGDFTRAD IPNIEPAKTK EELVAFFKQD
QRKILITTIF KFGDVDSVLN ERDNIILLVD EAHRTQEKDL GQKMRSALPN AFFFGLTGTP
INKRDKNTFQ SFGADEDLEK GGYISKYTFQ NSVEDGATLE LNFQTVPVEM HLNEAQLQEE
FDELTDQISE EEKNELVKRT SVEAFFTAEK RINDVARYIV NHFKEYVEPT GMKAQVVVYN
RDCCVKYKKA IDALLGSEDA TTIVMHTAGD KADEYKAYCR DREQERKLLD QFRDPLSPIK
MVIVTSKLLT GFDAPILQCM YLDKPMKDHT LLQAICRTNR KYNVDKKCGL IVDFVGVFDN
VAKSLAFDEE TVKTVVKNID EIKVLIPQFL QECIDFFPGV DRTIGGWEGL QAAQQCLLDE
STKTNFAKHF SRLAKAWETV SPDAMLAAYQ ADYTWLAQVY QSVRPVSTGG SLIWTLLGAK
TIEIIHRNID TIDIGTPLED LVVDGDVIDM VLEQAKDNPK KILEVEKMLR LRLGEHHGDP
NYKVFAEKLD ELRRHMEENL ITSIDFLRGL LTLAKEVLEE EKNSNQPLDK REQAKAALTE
LFESIKTEDT PIIVERVVAD IDENVVAIVR KFKDAFKSIT AQREIKKKLR SILWVNYQIK
DQEVFDKAYQ YIEMYY
//
