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Database: UniProt
Entry: A0A1G7Q8E3_9BACT
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ID   A0A1G7Q8E3_9BACT        Unreviewed;      1049 AA.
AC   A0A1G7Q8E3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=SAMN05216518_11619 {ECO:0000313|EMBL:SDF94792.1};
OS   Bacteroidales bacterium KHT7.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX   NCBI_TaxID=1855373 {ECO:0000313|EMBL:SDF94792.1, ECO:0000313|Proteomes:UP000198526};
RN   [1] {ECO:0000313|EMBL:SDF94792.1, ECO:0000313|Proteomes:UP000198526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KHT7 {ECO:0000313|EMBL:SDF94792.1,
RC   ECO:0000313|Proteomes:UP000198526};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNBQ01000016; SDF94792.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7Q8E3; -.
DR   STRING; 1855373.SAMN05216518_11619; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000198526; 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; 1.20.58.2040; -; 1.
DR   Gene3D; 3.90.1570.50; -; 2.
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; IPR022625; TypeI_RM_Rsu_C.
DR   NCBIfam; TIGR00348; hsdR; 1.
DR   PANTHER; PTHR30195:SF16; TYPE I RESTRICTION ENZYME R PROTEIN; 1.
DR   PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR   Pfam; PF12008; EcoR124_C; 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   Reference proteome {ECO:0000313|Proteomes:UP000198526};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW   ECO:0000256|RuleBase:RU364115}.
FT   DOMAIN          317..465
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1049 AA;  120394 MW;  B9EE4D5C778C3BCA CRC64;
     MNQSIIIEEQ HRTVVAQYSP IPRNDDDYQS EAKLEKELIS TLSAQGYGTP AIHTEADMLA
     NLRRQLEALN SITFTDAEWA RFFKQNIQCE PNNGQSVSND VIEQCTIKIQ KTRTFSLTRD
     DGTVKNIDII DAANPYRNTL QVINQYVPEG GAHANRYDVT ILVNGLPLVH IELKRRGVNI
     KEAFNQINRY GRDSFWAGSG LFNYVQIFVV SNGTNTKYYA NTTRYAHVKE QNGQKQGKVK
     KDCNSWEFTS FWADEQNNII ADLADFARTF FAKSTILNIL TRFCVFTVDK NLMVMRPYQI
     AATENILLRI RRALNLHHEG TRDAGGYIWH TTGSGKTLTS FKTAQLASCM PEIDKVLFVV
     DRKDLDYQTM KEYDNFQKDS ANSNTNIGVL HRQLNDSQCH IIITTIQKLS ILLGKKDPRY
     SLNCLDSRIV IIFDECHRSQ FGDMHKVIVR KFKRYMIFGF TGTPIFAENA GSARKTTADL
     FGDKLHTYTI IDAIRDKNVL KFHVDYISTM HMKDGVKDEQ VWGINTKEAL HDSRRIHNNV
     AYVLDHYAAK TKRDETYIVS RIENVEEVIK RGKKVDEVKQ KHRVRGFNSI FAADSVEMAI
     AYYNEFKLQQ ANTPENERLK IATIFTYGSN EEETDADDDI IDDTNESPEN VEQLKQKSPV
     AYEALSSAID DYNRMFSTQY SLDGDNFQSY YKDVSQRVKN RELDMVIVVG MFLTGFDAKT
     LNTLWVDKNL KMHGLLQSYS RTNRILNSIK NCGNIVNFRN LEEETDRALS LFGDKDAAGV
     VLLRPFGDYY YGYDTPDGKH HPGYTEIVSE LLEKFEPTEA FFLSLSVEQK KDFVRLFGAF
     LKMNNLLSIF DQFTEDKRVI KVGQVQDFTS LYQEVREELQ GNKTKGDSTN INDDLVFEME
     LVKQIQVSIE YILMLVKEYH DSNCTDKEIR VKISKAVKAS PDLRDKIELI ERFIERMTAS
     SGDVFDEWDK YVAEQKEEEL KAIIAQFNLN EEKTRAYLAQ SESDGFISAS GTALAEVLPP
     LNPFLPQRAE VKAKVFEALE NLFNKYRSV
//
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