ID A0RPM0_CAMFF Unreviewed; 1023 AA.
AC A0RPM0;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 102.
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 OrderedLocusNames=CFF8240_0985 {ECO:0000313|EMBL:ABK82486.1};
OS Campylobacter fetus subsp. fetus (strain 82-40).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360106 {ECO:0000313|EMBL:ABK82486.1, ECO:0000313|Proteomes:UP000000760};
RN [1] {ECO:0000313|Proteomes:UP000000760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=82-40 {ECO:0000313|Proteomes:UP000000760};
RA Fouts D.E., Nelson K.E.;
RT "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL Submitted (NOV-2006) 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; CP000487; ABK82486.1; -; Genomic_DNA.
DR RefSeq; WP_002849536.1; NC_008599.1.
DR AlphaFoldDB; A0RPM0; -.
DR REBASE; 14045; Cfe8240ORF990P.
DR GeneID; 61064815; -.
DR KEGG; cff:CFF8240_0985; -.
DR PATRIC; fig|360106.6.peg.955; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_005762_0_1_7; -.
DR Proteomes; UP000000760; Chromosome.
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 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; 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:UP000000760};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 295..453
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1023 AA; 117694 MW; 588D27BCD38AF047 CRC64;
MTPNVSENQI QQNCINLLRN MGYEFIAREQ NISFRDGKTS GVLLKEMLAK KLYEINSYEY
KGQKYKFSQN NIAKAIEDID VSLNEGLMVA NEKITNRLLL GTSYEESLTD GSKKSFSFKY
IDFDDIENNH FLITEEFALE RINQNETIKT RRPDLVIFIN GIPLVVIELK KSSVSYENGV
RQLAMEQKND EIPQLFKFIQ LTVAGNSNEA RYGTTGTPAK FYGIWKEDEL RESNLAMIVH
DRQITSLDRT LFALVSRDRL LRLIKHYILF DKKAKKVCRY QQFFGIEKTL QRVERTDNGM
RAGGLIWHTQ GSGKSLTMVM LTKLLKLTYT KAKIIVVTDR IDLDEQIHRT FENTEIKASR
ASSGSDLIDK LQSGVSVITT LVHKFEKVSN SKVCINDNSI FVLVDESHRT QSGDLHNAMK
KALPFACYLG FTGTPLLKRE KSSFNKFGGE IHRYTIGDAV KDGAVLPLLY EGRLVDQEVL
SPEGLVRKFD MISRDLSDEA KRDLQRKWAR FQRVASSEPR LEFIAMDINE HFKKTLKMQN
GGFKAMLATS SKYEAIKYHE IFEEYGDIKT AYIISSNEHE ELEGGHKEYV AKSWQETIKD
FGSEEEYVKY VKDEFIHGDE IDLLIVVDKL LTGFDAPRAS TLYVDKQLKE HNLLQAIARV
NRLYDGKDYG YIVDYRGLLG ELDQALSDYA SLSEFDIDDI NGAVIDVRNE IAKAKTYYAN
LDSLFCEVKF KDDLESYVEV LSDIQKRDDF KEWLSYLARA FKLALCSEKV SDILSQDEIK
TYKSKIKFYN ELRQVAQLRY HETCDFGKYE AQMQKLLDTF VNANGINELT KLVNIFETEF
DEEVQRVEGK NAKADTILSA ISAVIQERME SNPAFYKSIS DQIEDVISKY KEKRLSEEEK
LAKAKQLKGL ITGAIKPNID KYPKEFENKK SIFAIYDNLV DILGDIEVPD SKLIIKNLTI
KFDEIYEKAS KKPEWIKNKD VENDITSAME DMLWDIEDEY GISIENKEMI YQTIRGIGIG
FYA
//
