ID A0A1S2L199_9BACI Unreviewed; 1009 AA.
AC A0A1S2L199;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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};
DE AltName: Full=Type-1 restriction enzyme R protein {ECO:0000256|RuleBase:RU364115};
GN ORFNames=AWH56_006835 {ECO:0000313|EMBL:QOY37338.1}, AWH56_21065
GN {ECO:0000313|EMBL:OIJ06249.1};
OS Anaerobacillus isosaccharinicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX NCBI_TaxID=1532552 {ECO:0000313|EMBL:OIJ06249.1, ECO:0000313|Proteomes:UP000180175};
RN [1] {ECO:0000313|EMBL:OIJ06249.1, ECO:0000313|Proteomes:UP000180175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB2006 {ECO:0000313|EMBL:OIJ06249.1,
RC ECO:0000313|Proteomes:UP000180175};
RA Bassil N.M., Lloyd J.R.;
RT "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT Anaerobacillus genus.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QOY37338.1, ECO:0000313|Proteomes:UP000180175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB2006 {ECO:0000313|EMBL:QOY37338.1,
RC ECO:0000313|Proteomes:UP000180175};
RX PubMed=28104661;
RA Bassil N.M., Lloyd J.R.;
RT "Draft Genome Sequences of Four Alkaliphilic Bacteria Belonging to the
RT Anaerobacillus Genus.";
RL Genome Announc. 5:e01493-16(2017).
RN [3] {ECO:0000313|EMBL:QOY37338.1, ECO:0000313|Proteomes:UP000180175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB2006 {ECO:0000313|EMBL:QOY37338.1,
RC ECO:0000313|Proteomes:UP000180175};
RX PubMed=29580368;
RA Bassil N.M., Lloyd J.R.;
RT "Anaerobacillus isosaccharinicus sp. nov., an alkaliphilic bacterium which
RT degrades isosaccharinic acid.";
RL Int. J. Syst. Evol. Microbiol. 69:3666-3671(2019).
RN [4] {ECO:0000313|EMBL:QOY37338.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NB2006 {ECO:0000313|EMBL:QOY37338.1};
RA Bassil N.M., Lloyd J.R.;
RL Submitted (OCT-2020) 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|ARBA:ARBA00011296,
CC 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; LQXD01000183; OIJ06249.1; -; Genomic_DNA.
DR EMBL; CP063356; QOY37338.1; -; Genomic_DNA.
DR RefSeq; WP_071318900.1; NZ_CP063356.1.
DR AlphaFoldDB; A0A1S2L199; -.
DR REBASE; 178017; Asp2006ORF21075P.
DR REBASE; 452742; Ais2006ORF6845P.
DR KEGG; aia:AWH56_006835; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000180175; Chromosome.
DR Proteomes; UP000180175; 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; 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, ECO:0000313|EMBL:OIJ06249.1};
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:UP000180175};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 259..432
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1009 AA; 117033 MW; E21D9FB21D905FBD CRC64;
MSVGQVERFT HDKVVQLLKT QLKYDYLGNW QDRSNNKNIE EDILKRYLSD KGYSIDLIQK
AIFQLTQAAS NQVKSLYDIN KEVYSLLRYG VKERVHAGEN METVHLIDWK EPLNNHFSIA
EEVTIKGENN KRPDIVIYIN GIAVGILELK RSTISVSEGI RQNLDNQDAA FIKPFFSTIQ
LIMAGNDTEG IRYGTIETKE KYYLTWKEES DNNNLLDRHI LQLCEKKRLI EMLHDFIVYD
RGVKKLCRPN QYFGVKAAQE SVRRREGGII WHTQGSGKSL TMVWLTKWIR ENVQDARVLI
ITDRDELDKQ IEKVFKGVNE EIYRTQSGKD LIDKINTPHP WLFCSLIHKF GNKEEADYDA
YIDELKKSLP VGFQAKGDFY VFVDECHRTQ SGKLHNAMKE LLPNAIFIGF TGTPLLKKDK
KKSIEVFGRY IHTYKFDEAV GDNVVLDLRY EARNVDQNIT SQRKIDQWFD AKTKGLTPHA
LAQLKQRWGT MQKVLSSRSR LEKIVSDILL DMETRDRLQN GRGNAMLVAG SIYEACKYYE
LFQNSGFSKC AIVTSYSPNI RDTKGERTGE ESITEKLKKY EIYMKMLNGM NSEEFEENVK
KKFVEEPAQM KLLIVVDKLL TGFDAPSATY LYIDKNMRDH GLFQAICRVN RLDGEDKEYG
YVIDYKDLFK SLEKSVDDYT TEAFDDYEQG DVEGLLSDRL EKAKERLDIA LETIKFLCEP
VAPPKDTIDY IRYFCAINIE NKDELKENEQ KRLALYKSTV TLIRSYANIA NEMEEAGYSK
DEIQSIKQDV GYYEKVRTEV KLASGDYIDL KQYEPAMRHL IDTYISAEES EVISEFDDLT
LVELIVARGK DAVDSLPKGI KENKDAVAET IENNVRRVII DESPTNPKYY EKMSILLDEL
IKERKEEAKS YENYLIKIIE LTKKVKNPST SSSYPRSMNS GAKRALYDNL DQNEELALNL
DNEIRTTKKD GWRGMKIKER EVYYAIQKYI DNDEVAERIF EIVKNQGEY
//
