ID R7J386_9BACT Unreviewed; 1040 AA.
AC R7J386;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=BN799_00374 {ECO:0000313|EMBL:CDE58295.1};
OS Prevotella sp. CAG:873.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262936 {ECO:0000313|EMBL:CDE58295.1, ECO:0000313|Proteomes:UP000018078};
RN [1] {ECO:0000313|EMBL:CDE58295.1, ECO:0000313|Proteomes:UP000018078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:873 {ECO:0000313|Proteomes:UP000018078};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDE58295.1}.
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DR EMBL; CBJF010000229; CDE58295.1; -; Genomic_DNA.
DR AlphaFoldDB; R7J386; -.
DR Proteomes; UP000018078; 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 ENDONUCLEASE SUBUNIT; 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:UP000018078};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 307..469
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1040 AA; 119800 MW; 95051FB363F326BB CRC64;
MSNYDLISEN PESTVVAEFE GGYYSAAQYQ NEAAMEADFI KRLQAQAYEY LPITCEKDLI
ANLRVQLERL NGIRFTDREW EGFFREYLGN PNDGIVEKTR TIQEDHKKVL QREDGSFDNI
YLIDKESIHN NHLQVINQYV PEGGSHENRY DVTILVNGLP LVHIELKRRG VEVREAFNQI
RRYNRESFWA GCGLFEFVQI FVISNGTLTK YYSNTTRDSH VRQQGKGSKK QTSNSFEFTS
YWARLDNEPI RDLVDFTQTF LSKHTLLNVL TRYCVFTSEN MLMVMRPYQI AATEAIIQRI
RTSTNQKTWG RREGGGYIWH TTGSGKTLTS FKTARLASRM DEIDKVLFIV DRKDLDYQTM
KEYDRFEKGA ANSNSSTAVL TRQLNDENCR IIITTIQKLS NFIARNAKHK IYTQHVVMIF
DECHRSQFGD MHRAIVRKFT QYHMFGFTGT PIFPDNAGAI RNVEYTTTEG TFGDRLHSYT
IVDAIRDGNV LPFRVDYVRT LRPEDEIEHE AVPAIDQDKI LKAPERISLI TKYILDHFDQ
KTKRNAQYYD FSKLTNIGAM AKAKATVEEV KVKTKLQGFN SMFAVESIPF VKLYYTELMR
QMAELPPNRR LKIATIYSYA ANEAEEDFGG DENSENTDGL DQSSRDFLEK CIADYNEMFG
TSYDTSAEKF QNYYKDVSLR MKNREIDLLI VVNMFLTGFD ATTLNTLWVD KNLRMHGLIQ
AYSRTNRILN SIKSFGNIVC FRNLEPATNA ALELFGDKEA GGLVLIKTFD EYYNGYVKKD
GTAVKGYRPM VEDELLTDFP LGSIILGEKA EKEFIRLWGA ILRLRNILQS FDQFKGKEIL
TNDQYKDYQG LYLDLYEKYR PKPSDAVDVN DDIVFEMELV KSVEINIDYI LFLVAQKNGD
PKHDAELEID IKKSIAATPD LRDKEDLIMQ FVSNASAGTD VNDEWSRYVR EKLDKEVAEL
IATEKLKPEK TIEFLQQSFR DGEIRESGTG IADILPPIPL FGVAGVNREA KKEKVTEKLK
ALFHRFYDLC GGVFPGTDAK
//
