ID G2IZU4_PSEUL Unreviewed; 1105 AA.
AC G2IZU4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=NH8B_1060 {ECO:0000313|EMBL:BAK75892.1};
OS Pseudogulbenkiania sp. (strain NH8B).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Pseudogulbenkiania.
OX NCBI_TaxID=748280 {ECO:0000313|EMBL:BAK75892.1, ECO:0000313|Proteomes:UP000001274};
RN [1] {ECO:0000313|Proteomes:UP000001274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274};
RX PubMed=22038961; DOI=10.1128/JB.06127-11;
RA Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.;
RT "Complete genome sequence of the denitrifying and N(2)O-reducing bacterium
RT Pseudogulbenkiania sp. strain NH8B.";
RL J. Bacteriol. 193:6395-6396(2011).
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; AP012224; BAK75892.1; -; Genomic_DNA.
DR RefSeq; WP_014086327.1; NC_016002.1.
DR AlphaFoldDB; G2IZU4; -.
DR STRING; 748280.NH8B_1060; -.
DR REBASE; 40105; Psp8BORF1062P.
DR KEGG; pse:NH8B_1060; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_005762_0_0_4; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000001274; 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 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.
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:UP000001274};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 294..527
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|SMART:SM00487"
SQ SEQUENCE 1105 AA; 122686 MW; 02D1060D2199AD4D CRC64;
MGWELDDVEK PFVAQLQALG WAYNAGSLDD PAVTGRTSFA EVIQEGLLRE QLRALNPGAD
GVPWLDEARL SEAVAAITRL GTHKLLEANE KATTLLIRGL TVDGLPGWDG GRGQTIRYID
WDTPSNNRFT VINQYRVDCP PGFNSAKQFI VPDLVLLVNG IPLVVVECKS PSIPEPLAEA
VDQLRRYSNQ RKAAFEVDDN EGNEPLFATN QLLVATSFDE ARVGCVGAAF EHYAQWKTVV
GPDGNGSEIE VAQALGKPAL SEQERLIAGL LSPVHLLDVV QNFMLFMQAG GQTIKTVCRY
QQYRAVNRAI VRLKTGQTRL QHGEHDQRGG IIWHTQGSGK SLTMVFLVRK MRADAQLRRF
KVIVVTDRKD LQGQLSVTAT LTGEVVEVAE SASGVRALAQ RQGPGLIFAT IQKYRDQDGT
GDAPLTADDL PKVEEPKANY KPDEKFEVLN EDDSILVLVD EAHRTQAGDL HAKLMAGLPN
CARIGFTGTP IIMGEKKRTH EIFGEFIDRY TIKEAETDGA TVPVLYEGRT ANGAVKDGAS
LDELFEDLFR QHTPEELETI KQKYTTKGHI FDAPALIADK ARDILRHYVT NILPNGYKAQ
VVAYSRLAAI RYFDALKQAR DELLAEAQAL SPEDKALDDE ALCQRPAKVQ AAVQAWRYRD
TLARIEFAPI ISGSNNDDPA WKQWTDDAAH EQLIKRFKKP LFDAKPEKTD PLAFLVVKSM
LLTGFDAPIE DVMYLDRPIR EAELLQAIAR VNRTGFGKRC GIVVDYYGVA QHLKEALAAY
ADEDVEGALA SLKDEVPVLR DRHLRVVDLF RQRGVESLDD TEACVEALGS ERLRAEFAVK
LKAFLASLDT VLPRPEGLPY SGDAKRLAYI YARARNRYKD TPVLGKDVGA KVRKLIDDHV
ISLGVDPKIP PIQLTDAEFD THVARAASDR AKASEMEHAI RSHIRKHTDE DPVLYRKLSE
RLSDILKTLG EQWNEVISQL QKIIDELRTG NAGSADAPSD LPEHCAPFLR TVLDVVCAGQ
TPTAAELLRL KDVTVELVDL LVQELQGNRD IWSPHKRAAQ EDLNTQLFEH LMRLRPPLVD
TDKAGVLADK LMEQARANHD KLVQV
//
