ID B7C9M4_9FIRM Unreviewed; 936 AA.
AC B7C9M4;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
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};
DE AltName: Full=Type-1 restriction enzyme R protein {ECO:0000256|RuleBase:RU364115};
GN Name=hsdR {ECO:0000313|EMBL:EEC90526.1};
GN ORFNames=EUBIFOR_00882 {ECO:0000313|EMBL:EEC90526.1};
OS Holdemanella biformis DSM 3989.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Holdemanella.
OX NCBI_TaxID=518637 {ECO:0000313|EMBL:EEC90526.1, ECO:0000313|Proteomes:UP000004315};
RN [1] {ECO:0000313|EMBL:EEC90526.1, ECO:0000313|Proteomes:UP000004315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3989 {ECO:0000313|EMBL:EEC90526.1,
RC ECO:0000313|Proteomes:UP000004315};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEC90526.1, ECO:0000313|Proteomes:UP000004315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3989 {ECO:0000313|EMBL:EEC90526.1,
RC ECO:0000313|Proteomes:UP000004315};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Eubacterium biforme (DSM 3989).";
RL Submitted (NOV-2008) 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|ARBA:ARBA00011296,
CC 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:EEC90526.1}.
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DR EMBL; ABYT01000052; EEC90526.1; -; Genomic_DNA.
DR RefSeq; WP_003864687.1; NZ_DS996841.1.
DR AlphaFoldDB; B7C9M4; -.
DR STRING; 518637.EUBIFOR_00882; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_004848_1_0_9; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000004315; 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; -; 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; 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; 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 Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 260..408
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 936 AA; 109974 MW; 22A862697B50787F CRC64;
MSSNLGYESE KTLEDNLIKQ LCADGYEFVE INDIDDLHLN FRKQVNKHNA SRLNGHELSD
KEFERLLVKI QGKGVYGSSK TLRSLQDITM DDGSTQYIEL FNTKNNEWCK NEFQVTHQVT
MVGKYENRYD VTLLINGLPL VQIELKRRGI DFKEAFNQVI RYKKHSLNDL FRYVQIFIIS
NGIDTKYFAN SDKEMDFQYT FYWTDKNNNR IDNLYDFALD FLPKCHISKM ISRYMVVDDT
QKSLMVMRPY QYYAVEELMK RAYETNNNAY VWHTTGSGKT LTSFKLSQLL STNREVAQVF
FLVDRKDLDS QTIEEFNRFQ KDTVDMTDST DTLIAQMKDS SKKIILTTIQ KMSNACKNDK
YQDVIDRFDG KKVVFIIDEC HRSQFGEMHK MIKKKFPRAQ YFGFTGTPRF AENASQDGRT
TADIFEKLVH HYLIKNAIAD GNVLGFNVDY VRTISSTVDI EDDEEVEAID TEEVLMDDQR
ISNIVDYVLK IHNSKTNNRR YNAIFTVRSI PMLIKYYDEF KKRNTDLKIA GIFTFGANED
GELETEHSRD SLERMIKDYN QMFDKNYSTN TFSAYFTDVS KKVKNTELDI LLVVNMFLTG
FDAKRLNTLY VDKRLKHHDL IQAFSRTNRI ETANKPYGNI VCFQTNKKAV DDAVKLFSLT
DNADEVLMKP YEYYRDEFRK AVEELLKHTP SPEEAEHGGD EQEEYKFVLL FRELVRLMVK
LKTFDEFEFT EDELGMSNQL YEDFVSKYKK IYRDIRPDQQ KTSILSDVSF DIELLRNDKI
NVHYILELIK NAVSEPSREK RRKTLDEIEK MIESATDPEL YMKSDLIHGF IDSIASEMDP
DADFEYEYNQ YMEEQRTNEI REVAAKYQIP EPKINRLIGD YEFGGFVDKN DIKTDLTKDV
IKREKEENNF SSSMRAKNSI TNTITQFIKD VVIKYM
//
