ID C4KBH1_THASP Unreviewed; 1000 AA.
AC C4KBH1;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=Tmz1t_3150 {ECO:0000313|EMBL:ACR01747.1};
OS Thauera aminoaromatica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=164330 {ECO:0000313|EMBL:ACR01747.1, ECO:0000313|Proteomes:UP000002186};
RN [1] {ECO:0000313|Proteomes:UP000002186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MZ1T {ECO:0000313|Proteomes:UP000002186};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sayler G.S.;
RT "Complete sequence of chromosome of Thauera sp. MZ1T.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACR01747.1, ECO:0000313|Proteomes:UP000002186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MZ1T {ECO:0000313|EMBL:ACR01747.1,
RC ECO:0000313|Proteomes:UP000002186};
RX PubMed=23407619; DOI=10.4056/sigs.2696029;
RA Jiang K., Sanseverino J., Chauhan A., Lucas S., Copeland A., Lapidus A.,
RA Del Rio T.G., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D.,
RA Brettin T., Detter J.C., Han C., Chang Y.J., Larimer F., Land M.,
RA Hauser L., Kyrpides N.C., Mikhailova N., Moser S., Jegier P., Close D.,
RA Debruyn J.M., Wang Y., Layton A.C., Allen M.S., Sayler G.S.;
RT "Complete genome sequence of Thauera aminoaromatica strain MZ1T.";
RL Stand. Genomic Sci. 6:325-335(2012).
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; CP001281; ACR01747.1; -; Genomic_DNA.
DR RefSeq; WP_012585828.1; NC_011662.2.
DR AlphaFoldDB; C4KBH1; -.
DR STRING; 85643.Tmz1t_3150; -.
DR REBASE; 20874; TspMZORF3154P.
DR KEGG; tmz:Tmz1t_3150; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_005762_0_0_4; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000002186; 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.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000002186};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 302..466
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 869..911
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1000 AA; 113674 MW; 1426B2A2D75AB84C CRC64;
MFTESNTVEA YLSDLLADLG NPLANKAEEP SPNYLRKPRR TGWHFAAPAD IPRQPHELLV
EPWLRDALIR LNPEIAARPD LADEVLYKLR AIVLSVRSDG LIRANEEMAA WMRGERSMPF
GPNNEHVPVR LIDFDDLGRN EFVLTRQFTF RAGPAERRAD LVLLVNGLPL VLIEAKTPVK
KCISWVDGAL QVHEDYEKFV PELFVCNVFS VATEGKEFRY GSIGLPVKDW GPWNLDGEAD
DARGQTHPLK SLRQSVESML RPQVVLDILA SFTLFATDKK KRRIKIICRY QQYEAANKIV
ERVLAGQPKK GLIWHFQGSG KSLLMVFAAQ KLRMHPRLKN PTVLIVVDRI DLDTQITGTF
TGADIPNLEK ADSREKLQQL LAQDVRKIII TTIFKFGETP NGKAGALNER SNIIALVDEA
HRTQEGDLGR KMREALPNAF LFGLTGTPIN RADRNTFYAF GADEDEKGYL SRYGFEESIR
DGATLRLHFE PRLVDLHIDK AAIDEAYKDL TGGLSDLDRD NLAKTAAKMA VLVKTPERIR
RICEDIVQHY QSKVEPNGFK GQVVTFDRES CLLFKAELDK LLPTEATDIV MSVQPGDRKE
RPEYARYDRS RDEEERLLDR FRDPADPLKL IIVTAKLLTG FDAPILQAIY LDKPLRDHTL
LQAICRVNRT YSEQKTHGLV VDYLGIFDDV AAALEFDDQS VKQVISNIQE LKDKLPEAMQ
KCLAFFPGVD RSQQGYEGLI AAQQCLPNND TRDAFAAEYS VLARIWEALS PDPLLGQYET
DYKWLSQIYQ SVQPSSGHGK LIWHSLGAKT IELIHQNVHV DAIRDDLDTL VLDADLLEAV
LSNPDPKKAK ELEIKLNRRL RKHQGNPKFK DLSERLDALK ERFESGQINS VDFLKQLLQI
AKETLQAERE TPPEEDEDRG KAALTALFNE VKTPETPIIV ERVVTDIDEI VRLVRFPGWQ
GTQAGEREVK KALRKALFKY KLHADEELFE KAFSYIRQYY
//
