ID A0A3P1XU20_9MICO Unreviewed; 1056 AA.
AC A0A3P1XU20;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=EII30_01465 {ECO:0000313|EMBL:RRD61526.1};
OS Leucobacter sp. OH1287.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=2491049 {ECO:0000313|EMBL:RRD61526.1, ECO:0000313|Proteomes:UP000281351};
RN [1] {ECO:0000313|EMBL:RRD61526.1, ECO:0000313|Proteomes:UP000281351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH1287 {ECO:0000313|EMBL:RRD61526.1,
RC ECO:0000313|Proteomes:UP000281351};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
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:RRD61526.1}.
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DR EMBL; RQYM01000002; RRD61526.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1XU20; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000281351; 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; 1.20.58.2040; -; 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; 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:RRD61526.1};
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:UP000281351};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 321..483
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1056 AA; 120138 MW; FC91F91F1E9052B8 CRC64;
MINTPAPQYD LIAFSDESTV VAEYTPDTKT ADNHQSEAEL EREFIETLVS QAYERLHITK
EADLIENLRR QLEALNDYKF SDSEWERFFG NVIAGKNEGI EEKTAKIQEN HVQLLQRDNG
LTKNIKLLDK ANIHNNRLQV INQYQIDTSG KNGSGGSRST NRYDVTVLVN GLPLVHIELK
RRGVNIREAF NQINRYQRDS FWGGSGLFEY VQLFVISNGT LTKYYSNTTR EQHIKEAKNT
AKRRKTSNSF EFTSWWADAQ NKPILDLTAF AKTFFAKHTL LNILTKYCVL TAERMLLVMR
PYQIVATERI MQRIEIATNY KHLGSVKAGG YVWHTTGSGK TLTSFKTAQL ASALPSVDKV
LFVVDRKDLD YQTMREYDRF QKGAANSNTS TAVLKKQLED ENAKIIITTI QKLSTFIKAN
EKHDVYGKHV VIIFDECHRS QFGDMHNRIT KSFKRYNLFG FTGTPIFAAN SRSGSSAGLK
TTEQVFGDKL HTYTIVDAIT DKNVLPFRID YVKTSTVGGC LGSKISTVET EKLLLDERRI
REVVSYTLEH FAQKTKRSTS YGHSVVTNVA EAARTRGSKE AKRASRQVRG FNAIFATASI
EAARKYYNQF AIQQQDLPSD QQLKVGIIYS YGANEAADDG ILDEEAFDTD ALSTDAREFL
EEAINDYNEM FGTSYDTSAE KFQNYYKDLS MRLKNRELDL VIVVNMFLTG FDATTLNTLF
VDKNLRAHGL IQAYSRTNRI LNSVKTYGNI VAFRDLEEET NAALELFGNK DASGVVLMKP
FKHYYREYKD KVTELLEEFP LNKQIVGERA KRSFIKLFGA ILRLENILTS FDEFAGKELL
NRRQVQDYRS IYLNLHDEIR GEKEAENDPA HDDVVFEIEL IKQVEINVDY ILMLIEKHQQ
RLGNELQLDS GATLDEEGSL DEEINENIPA TIRRAIEASP SLRNKKDLFS EFIDSITGNS
TVEDEWQDYI RAKSESELAD IVKVERLNPE ETSRFMEKAF RDGALSTSGT AITKILPPVS
RFTPTGGHGE KKQTVIKKLT AFFDRFYGLG AGPGGR
//
