ID A0A0Q9L8H2_9MICC Unreviewed; 1074 AA.
AC A0A0Q9L8H2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, 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=ASG92_11195 {ECO:0000313|EMBL:KRE45999.1};
OS Arthrobacter sp. Soil736.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736395 {ECO:0000313|EMBL:KRE45999.1, ECO:0000313|Proteomes:UP000051775};
RN [1] {ECO:0000313|Proteomes:UP000051775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil736 {ECO:0000313|Proteomes:UP000051775};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE45999.1, ECO:0000313|Proteomes:UP000051775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil736 {ECO:0000313|EMBL:KRE45999.1,
RC ECO:0000313|Proteomes:UP000051775};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRE45999.1}.
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DR EMBL; LMSB01000066; KRE45999.1; -; Genomic_DNA.
DR RefSeq; WP_056634947.1; NZ_LMSB01000066.1.
DR AlphaFoldDB; A0A0Q9L8H2; -.
DR STRING; 1736395.ASG92_11195; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000051775; 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:0004386; F:helicase activity; 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 InterPro; IPR021810; T1RH-like_C.
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 Pfam; PF11867; T1RH-like_C; 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 Helicase {ECO:0000313|EMBL:KRE45999.1};
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 Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 304..479
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1074 AA; 118509 MW; 1B3A400D429370B5 CRC64;
MTSGQSGGTT VTTAPAVAFS EADWEGVALE LLAEPLGWRP ATGQDIAPGR GERDSWDELL
IRPRLLTALQ RFNPTVPAQY LQQALAEIAS PKSQDAITEN HRIHNCLTGG YRLSYIDLDG
REANPTIHLL SSDPDQNDWL AVNQVTLVQG DYKRRFDVVL YCNGMPVSVI ELKKAGSATA
DVASAHAQLQ TYLREFPMAF RFCVFTLASD GIQAKFGTPF TPLNHFSPWN VDDDGVPVAP
GYMEDGQAVT ALETALQGLY NQERFLQLTR NFTAFDEGSD GLSKRIAKPH QYFAVTKAVG
STVQAVESNG KAGVVWHTQG SGKSMEMELY ANLVARHPKL KNPTVVVITD RNELDGQLFE
GFDRSLLLAE SPKQIRKRSE LREELSNRTT GGIYFTTLQK FGRSKSEKDA GSDHPLLSDR
RNIIVVVDEA HRSHYDDLDG YARHLRDALP HATLIAFTGT PISFDDRNTQ EVFGEYIDIY
DLSRAVEDGA TVPVYFEPRL IKVGLASNVT EEILDQAADE ATLGLDETER ERIEASVAVV
NAVYGAPQRI AALAADLVAH WENRSARMGM FIEAPGKAMI VGGTREICAK LYTAIVELRP
DWHSDDLTKG KIKVVYSGTA SDVPPVSNHV RRDSANAVVK ERLKDVDDEL ELVIVKDMML
TGYDSPPLHT LYLDRPLKGA LLMQTLARVN RTFRGKEDGL LVAYAPLAEN LAKALGEYTK
DDRTNKPVGK NIDEAVGLTV SLVDSLRGLL AGYDWKAVLM KGGPKAFLNA VTGAVSYLRN
PGSPGNQPAD GEESLAAKYR RFSSQLSRAW ALCSGSETLA ELRPEIQVYE EIRVWMAKYD
AADRQASGEP VPEEIQRLLG NLIASATSSG EVLDIYDAAG MPRPSLDDLT PEFIAKTQQA
RNPQLAIEAL RKLIADESAK TTRNNVIRQR AFSERITELM KKYTNQQLTS AEVIAELVEL
AREVAAEGKR GLQFTPPLNS DELAFYDAVA QNESAVEVQG EGVLADIARE LVSVMRRDVR
TDWTVRDDVR AKLRSSIKRL LVRFGYPPDK QPEAIKLVME QMESMAPRFA EARG
//
