ID M7XHK9_9BACT Unreviewed; 1087 AA.
AC M7XHK9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=C943_03854 {ECO:0000313|EMBL:EMS34038.1};
OS Mariniradius saccharolyticus AK6.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Mariniradius.
OX NCBI_TaxID=1239962 {ECO:0000313|EMBL:EMS34038.1, ECO:0000313|Proteomes:UP000010953};
RN [1] {ECO:0000313|EMBL:EMS34038.1, ECO:0000313|Proteomes:UP000010953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK6 {ECO:0000313|EMBL:EMS34038.1,
RC ECO:0000313|Proteomes:UP000010953};
RA Vaidya B., Khatri I., Tanuku N.R.S., Subramanian S., Pinnaka A.;
RT "Genome assembly of Mariniradius saccharolyticus AK6.";
RL Submitted (JAN-2013) 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:EMS34038.1}.
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DR EMBL; AMZY02000007; EMS34038.1; -; Genomic_DNA.
DR RefSeq; WP_008625236.1; NZ_AMZY02000007.1.
DR AlphaFoldDB; M7XHK9; -.
DR STRING; 1239962.C943_03854; -.
DR eggNOG; COG0610; Bacteria.
DR InParanoid; M7XHK9; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000010953; 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; 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:UP000010953};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 317..498
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1087 AA; 125283 MW; 5D1F9CD2BE6176F6 CRC64;
MKFTESQLEK AFTELLGQQG FPHSLGIALV RKPEEVIIEE DLRGFLAEHY SHQGITTYEI
QSIILRLKAL PASDLYETNK RFLRMLSDGF ILKREDRSQK DIYIQLLDYA GLNSQRRPLE
EHAVAIAADE EERDFTSPLS ESYGKDTNRY RFVTQMEILG GEKRIPDGIL YINGLPLVVF
EFKSAIREEA TIHDAYRQLT VRYRRDIPEL FKYNAFCVIS DGVNNKAGSF FAPYEFFYAW
RRVAGPSRSA GKADSEVDGI DSMYTLVQGM FHKDRLRDIL RNFIYLPDNS KKEEKIVCRY
PQYYAARALY ESIKKAQKPD GDGKGGTYFG ATGCGKSFTM LYLTRLLMKS EYFESPTIVL
ITDRTDLDDQ LSAQFVNAKQ FIGDNTVESV ESRAYLRLKL QGRQSGGVFL TTIHKFTEDT
ELLSGRSNII CISDEAHRSQ VNLDQKLKVN EDGVKKTFGF AKYLHDSFPN ATYVGFTGTP
IDATLDVFGK VVDAYTMTES VRDEITVRIV YEGRAAKVAL KNGELEKIER YYKEAAEMGS
NEYQIDKSKE QTAKMYVILG DPERLKAVAE DFILHYERRV SEGATVKGKA MFVSSSREIA
YALYKNIIAL RPEWNEIREA AEGADLTEKD RRELKPIERI KLVMTRSQDD PEELWKLLGT
KDDRKELDRQ FKNPKSNFKI AIVVDMWLTG FDVPFLDSIY IDKPIQQHNL IQTISRVNRK
FEGKHKGLVI DYIGIKKQMN LALAQYNKGD RDNFEDIDKS LVVVKDHLDL LGRLMHKFDT
TKYFKGNTLE QLHCLNLAAE FVQQTKELET RFMGLVKRLK AAYDICAGSE KLTQTERDYT
HFYLAVRSIV FKLTKGNAPD TAQMNEKVRE MIKDALESDG VEEIFKLGEE GTSEQDIFDE
DYLAKIDKIK LPNTKIKLLQ QLLAKAIQEI KKVNRIKGID FSKKMQSIVE RYNDRSVNDI
MRSEVYEEMA EALTNMIWEV HREFKAGDAL GIDFEEKAFY DILKELCKKY DFSYPEEKLI
ELAKAVKDLV DGQSKFPDWN KRDDIKAALK VGLILLLDEF GYPPVERDEV YVEIFEQAEN
FKKYQSK
//
