ID A0A143XRP8_9BACT Unreviewed; 1035 AA.
AC A0A143XRP8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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_3 {ECO:0000313|EMBL:CVI70530.1};
GN ORFNames=BN3659_01899 {ECO:0000313|EMBL:CVI70530.1};
OS Alistipes sp. CHKCI003.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=1780376 {ECO:0000313|EMBL:CVI70530.1, ECO:0000313|Proteomes:UP000198813};
RN [1] {ECO:0000313|EMBL:CVI70530.1, ECO:0000313|Proteomes:UP000198813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHKC3 {ECO:0000313|EMBL:CVI70530.1};
RA Oliw E.H.;
RL Submitted (JAN-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; FCNT01000072; CVI70530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143XRP8; -.
DR STRING; 1780376.BN3659_01899; -.
DR REBASE; 151021; AspCHKC3ORF1895P.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000198813; 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};
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:UP000198813};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 297..442
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1035 AA; 119871 MW; 0E43659EE5129F21 CRC64;
MAYYNTIAES NNFIVLDDYE KYSVLNEPSV VYQTEASLEH EFIQDLRNQG YEYLPDLNTP
EALLANVRTQ LQALNDVEFT DSEWDRYVEE YLDKPSDSLV EKTRKIQDDY IYDFVFDDGH
IKNIYLVDKQ NLSRNKVQVI RQFVQEGSHL NRYDVTILVN GLPLVQVELK KRGVAIREAF
NQVHRYSKES FNTNNSLYKY IQIFVISNGT DSRYFANTVE RNKNSFDFTM NWAKANNSLI
KDLKDFTATF FQKNTLLNVI LTYSVFDSNN TLLIMRPYQI AATERILWKI KSSYQAKKWS
TTEGGGYIWH TTGSGKTLTS FKAARLATQL DFIDKVFFVV DRKDLDYQTM KEYQRFSPDS
VNGSESTAGL KRNIDKDDNK IIVTTIQKLN NLMKSESDLP IYQKQVVFIF DEAHRSQFGE
AQKLLKKKFK KYYQFGFTGT PIFPENALGS DTTASVFGRE LHSYVITDAI RDEKVLKFKV
DYNNVRPRFK GIETERDEKK LSAAENKSAL LHPARIKEIS QYILDNFKIK THRGIGANKG
FNAMFAVSSV DAAKCYYEEL NNLQQGTEKP LKIATIFSFA ANEEQSAIGE IIDENFEPTA
MDISAKEFLT NAINDYNAMF KTSFGVDSRE FQNYYRDLAK RVKNKEIDLV IVVGMFLTGF
DAPTLNTLFV DKNLRYHGLI QAFSRTNRIF DATKTFGNIV TFRDLEQHTI DAITLFGDSN
TRNVVLERSY KEYLEGFKDI VTGEARRGYI EVVKELNERF PNVDEIETEL DKKDFSKLFG
EYLRIENILQ NYDEYTHLKA LQAIDLDNPN AVEEFKNTYF VTDEDIKDMQ QVEMLSERAV
QDYKSTYNDI RDWLRREKDG SVAEKSKIDW DDVVFEIDLL KSQEINLDYI LELIFEKNNK
TKDKTALIEE IRGVIRASVG NRAKESLIVD FINETDLDTI TDKASIIESF FEYAQSKQKQ
EASELISSEN LNEEEAKRYI TVSLKREFVS ENGTDFNSIL PKMSPLNPMY LTKKHKVFQL
IAAFVEKFKG VGGRI
//
