ID B0NL99_BACSE Unreviewed; 1076 AA.
AC B0NL99;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
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:EDS16829.1};
GN ORFNames=BACSTE_00223 {ECO:0000313|EMBL:EDS16829.1};
OS Bacteroides stercoris ATCC 43183.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=449673 {ECO:0000313|EMBL:EDS16829.1, ECO:0000313|Proteomes:UP000004713};
RN [1] {ECO:0000313|EMBL:EDS16829.1, ECO:0000313|Proteomes:UP000004713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43183 {ECO:0000313|EMBL:EDS16829.1,
RC ECO:0000313|Proteomes:UP000004713};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides stercoris(ATCC 43183).";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS16829.1, ECO:0000313|Proteomes:UP000004713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43183 {ECO:0000313|EMBL:EDS16829.1,
RC ECO:0000313|Proteomes:UP000004713};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2007) 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}.
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:EDS16829.1}.
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DR EMBL; ABFZ02000012; EDS16829.1; -; Genomic_DNA.
DR RefSeq; WP_005652536.1; NZ_DS499667.1.
DR AlphaFoldDB; B0NL99; -.
DR REBASE; 21228; Bst43183ORF224P.
DR GeneID; 31796060; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_015458_1_0_10; -.
DR Proteomes; UP000004713; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 322..498
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 937..964
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1076 AA; 125258 MW; 5A5770304B363A2A CRC64;
MKQFSEATRV QMPAMVHLTR IGYTYFGKLS EDKNGTVYDS DTNILLQVFE RQFKNLNPGH
EGEYLQVLKD IRKELNDDDL GRGFYNRLKA VSPVKLIDFD NIGNNTFHFT AEFTCKNGQD
EFRPDITLFV NGLPLCFVEV KKPNNHGGML AESARMNKER FPNKKFRRFI NITQLMIFSN
NMEYDALGGI VPIQGAFYCT GARSYAPFNC FREENLSGQK IAPFHRDYLY KEIDKTVEKQ
ILSDYNCQVI HTSPEYQTNL GFNTPTNRIL TSMCSPERLL YIIRYGIAYV RMEREVDGKI
ESTDQKHIMR YQQLFASLAI RQKLAEGVKS GVVWHTQGSG KTALSYYLTY ILNDFYSKQN
KVAKFYFIVD RLDLLEQATQ EFEARGLVVS TANTRAELME QFRSNQAQQG VSGQAEITVV
NIQRFAEDKE KVRISDYATN LQRIFILDEA HRGYKPGGCF LANLFDADTD AIKIALTGTP
LLKEERASCK VFGNYLHTYY YDKSIADGYT LKIIREDIET SYKERLSDVY DKLETLVQKK
DIRKSEIIEH PSYVSELARY IMTDLKEFRK IQGDDTLGGM VICETSEQAR RLYDVFQEEW
QKYQPKPIKI KLSDGSYVVG EPEVDYKSKY RPLKAGIILH DTDDKETRKQ IVKDFKKNMT
VDILIVFNML LTGFDAPRLK RLYFGRKLKD HNLLQAITRV NRPYPGMRYG FVIDFADIKR
NFKETNEAYL QELNRFNDVD ETGESAATDT FTQVIEDKEE ILNQMKKVRQ TLFNYTYDNA
EEFSSEISTE EDKAVLLDLK QALESAKNMA NIVRTFGDDE MKEQFAKLEI TKLPQLLSEV
QRRISIINQK EAFNTNEETK TLINEAMMDI EFTFSKIGQE EMRLISGGVE LKEKWQRTIS
SFTQNFDQDD PEFISLREAF MERFKEHGFV IDTIAKFNEE TQALDEIIGR LQDLQKRNNV
LLKKYKGDEK FARVHKRIRE VNKQREDKGQ KPMFSFLDEE IAAILNIIKE DVDAKVYDRN
DILKKDAYFG RTVMALINGC LYHFPQIKPE MEDYKFIQTR ISQQYINQYN ATYGIS
//
