ID A0A438AM46_9RHOB Unreviewed; 1022 AA.
AC A0A438AM46;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=EKE94_04420 {ECO:0000313|EMBL:RVV99911.1};
OS Mesobaculum littorinae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Mesobaculum.
OX NCBI_TaxID=2486419 {ECO:0000313|EMBL:RVV99911.1, ECO:0000313|Proteomes:UP000285908};
RN [1] {ECO:0000313|EMBL:RVV99911.1, ECO:0000313|Proteomes:UP000285908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M0103 {ECO:0000313|EMBL:RVV99911.1,
RC ECO:0000313|Proteomes:UP000285908};
RA Li F.;
RT "Mesobaculum littorinae gen. nov., sp. nov., isolated from Littorina scabra
RT that represents a novel genus of the order Rhodobacteraceae.";
RL Submitted (NOV-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:RVV99911.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RQXX01000001; RVV99911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A438AM46; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000285908; 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; 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 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:UP000285908};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 271..442
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1022 AA; 114697 MW; B8CDE027035754A0 CRC64;
MSKIGEAERK AQDRVIDLLC GDKSGTSGGL GWRYLGDWQK REGNANIEPS LLRPWLEARG
YAPEVITQAI TRLEREARME GTKLYEANQS FYDMLRYGVA IAPGPGEAPV TVRFVDWGDA
GANDLGVAEE VSIKGKDAKA WNKRPDLVLY VNGIALGVVE LKRSTVGVGT GIRQTLDNQR
PEFIQHFFTT VQITFAGNDS EGLRYAPIKK PQPYWLAWKE ESEISARLDR DVTQMMAPTR
FLELIHDFTL FDAGIKKIAR PNQYFAVKAA QERVGSREGG IIWQTQGSGK SLIMVMLARW
IREAFPDGRI LVVTDRKELD SQIEDVFGNT GDKVRRARSG NDLMAALADP TDRIICSLVH
KFGKKEEGEL ESLISDIQNA NIGAPKGEFF VFIDEAHRTQ SGKLAKAMRK VLPKAMFIGF
TGTPLLRSDK GTSLETFGPY IGKPYRFDEA VEDGVVLDLR YEARDIDQRI SAPEKIDAWF
EAKTKGLTPI AKATLKQRWG TLQRVLSSRD RLEQIANDII LDMEMKPRLN AGMGNAMLVA
GSIPEACELF EIFRKSGSIL ADKCAIVTSY KRAAPEITGE ETGMGETERQ RVHRVYTELL
GDTSEEEYEE EALRLFKKEP GRMKLLIVVS RLLTGFDAPT ATYIYIDKQM RDHGLFQAIC
RVNRLDGDDK DFGYIVDYKD LFRNIESAVD DYTSEAFDAF DKEDVEGLIT DRAEQADTDL
RTARDAWLGL LDAVEQPKGD DELFAYFSSP EGIESDPDAE EKARRRQALY KLAGRYARAY
TNVAAEPDGS GFNELELAEM RKEVEHAIGV RDAVRLHSGD AVDMKLYEPA MRHLIDNYIR
ADDSQAISHL DDISLIDLVE SKGAQAEDDL PAPSKRKREN VAEAIENNVR KLIIDETPVN
PKFYEKMSEL LTDLVAQRRS GAIEYAEYLE KIAELVRVAK SGHGNTYPES MKSPGQKALF
DNLGQDEALA RRVDEAVRAT APHGWRGHTM KEKKVRRCLE AEISDPDTVD TLLQILKNHG
EY
//
