ID A0A374W7I6_9BACE Unreviewed; 1034 AA.
AC A0A374W7I6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-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=DXB63_16435 {ECO:0000313|EMBL:RGN42845.1};
OS Bacteroides sp. OM05-12.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=2292283 {ECO:0000313|EMBL:RGN42845.1, ECO:0000313|Proteomes:UP000264777};
RN [1] {ECO:0000313|EMBL:RGN42845.1, ECO:0000313|Proteomes:UP000264777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OM05-12 {ECO:0000313|EMBL:RGN42845.1,
RC ECO:0000313|Proteomes:UP000264777};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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:RGN42845.1}.
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DR EMBL; QSUN01000033; RGN42845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A374W7I6; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000264777; 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; 1.10.10.2110; -; 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; 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, ECO:0000313|EMBL:RGN42845.1};
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:UP000264777};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 296..441
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1034 AA; 119681 MW; 1430B795199A6F42 CRC64;
MRQYNTIAES KNFIVLDDYA KYSMVSEPLV GYQTEFALER EFIQDLINQG YENPTIKSAE
AMLANARTQL QELNNMVFSD GEWARYVEEY LDKPSDNLVE KTRKIHDNYI HDFVFDDGHI
QNIYLVDKKD IARNKLQVIS QFEQTGTHAN RYDVSILVNG LPLVQIELKK RGVAIREAFN
QVHRYTKESF NKENSLFKYL QIFVISNGTD SRYFANTVER NKNSFDFTMN WAKADNTLIK
DLKDFTATFF QKNTLLNVLL TYSVFDTSDT LLVMRPYQIA ATERILWKIK SSYQVKQWSK
PEGGGYIWHT TGSGKTLTSF KAARLATELE FIDKVFFVVD RKDLDFQTMK EYQRFSPDSV
NGSESTAGLK RNLDKDDNKI IVTTIQKLNN LMKSEGELSI YQKQVVFIFD ECHRSQFGEA
QKLLRKKFKR YYQFGFTGTP IFPENALGDE TTASVFGREL HSYVITDAIR DEKVLKFKVD
YNDVRPKFKE IESEQDEEKL SSAEHKKAML HPARIKEISQ YILQNFRIKT HRNQGGGKGF
NAMFAVSSVD AAKCYYEELN RLQKDNENSL KIATIFSFAA NEEQNAVGEI PDETFELSAM
DLSAKEFLTK AIADYNAMFK TSYSVDSKEF QNYYRDLAKR VKSKEVDLII VVGMFLTGFD
APTLNTLFVD KSLRYHGLMQ AFSRTNRIYN ATKTFGNIVT FRDLEAATIE AIRTFGDSST
RNVVLEKSYK EYLEGFTDIV TGEARRGYIE VVKELNEKFP NPEAIVTEKD KKEFSKLFGE
YLRVENILQN YDEFTHLKAL QSIDINDPQA IEAFKEAYFI ADKDIAAMQE LEVLPNRTIQ
DYRSTYNDIR DWFRRERSSK EGEESKVDWD DVVFEVDLLK SQEINLDYIL ELIFEHNKKT
SDKIALIEEI RRVIRASIGN RAKESLVVDY INETDIDAIC DKPSILDSFY SYAQEKLRVE
AAQLIADENL NEQEAKRYIS TSLKREYASE NGTELNSILP KMSPLNPQYL TKKQSVFQKL
ASFVEKFKGI GGKL
//
