ID J4U9Y4_9FIRM Unreviewed; 1064 AA.
AC J4U9Y4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 ORFNames=HMPREF1142_1808 {ECO:0000313|EMBL:EJP18907.1};
OS Peptostreptococcaceae bacterium AS15.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX NCBI_TaxID=936556 {ECO:0000313|EMBL:EJP18907.1, ECO:0000313|Proteomes:UP000006605};
RN [1] {ECO:0000313|EMBL:EJP18907.1, ECO:0000313|Proteomes:UP000006605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS15 {ECO:0000313|EMBL:EJP18907.1,
RC ECO:0000313|Proteomes:UP000006605};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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:EJP18907.1}.
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DR EMBL; ALJM01000048; EJP18907.1; -; Genomic_DNA.
DR AlphaFoldDB; J4U9Y4; -.
DR PATRIC; fig|936556.4.peg.2134; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000006605; 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 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:UP000006605};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 331..507
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 923..953
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1064 AA; 124458 MW; EA8416023AFED83E CRC64;
MSEVKNYSRN KDFNEATRVQ MPALVHLSRL GYKYFGKITE DMKGIKYDGD TNILLEVFKN
QFKKLNPTHA GEVEEVLRSI RQELDNDDLG KSFYKRLVAI SPTKLIDFEN INNNTFHYTA
EFTCKNGQDE FRPDITLFVN GLPLLFIEVK KPNNKGGMVA ESTRMNNQRF PNKKFRRFIN
ITQLMIFSNN MEYETLGGIT PIQGAFYCTG ARDTTKFNCF REVNPANSDI APFIKNFPYL
EINQDMEKQI LSDFNCQVIH TSPEYQTNLN ENTPTNRIIT SMCSKQRLLF LLKYGFAYVR
MDREIDGKIE SLDQKHIMRY QQFFATFAVI EKLDEGIKSG VIWHTQGSGK TALSYHLTYA
LTDYYAKQNK VAKFYFIVDR LDLLEQASSE FEARGLEVKT ASSRKELMAQ FRTNQSQDGN
SGRMEITVVN IQRFAEDKEK VVINDYDTNL QRIFIIDEAH RGYNPKGCFL ANLFDADQEA
IKIALTGTPL LKEERASWKV FGNYLHTYYY DKSIQDGYTL KIIREDIETS YREKLSEIYD
SIEHLVEKKD IKKSYIVEHD SYVKELLQYI ISDLKKFREI QGDDTLGGMV ICETSEQARK
LFAYFDETQE ELNCNESVKS KLKAGLILHD SDDKETRKEI VKDFKKNNTI DILIVFNMLL
TGFDAPRLKR LYFGRKLKDH NLLQALTRVN RPYKDNFYGY VIDFADIKKN FDETNEAYLK
ELNRFNDPAE TGDGNTMDTL SQVLESPEEL VGKMKEVRQV LFNYTIDNAE DFSSEISTIE
DKEELLKLKK VLISARDLCN IVRTFGDEEL KQKFEKLEIT RLPSMISEVS HCIDIINQKE
VFSMHDETKQ IVNKAMEDIE FSFKSISKEE MKIISGGIEL KEKWKKTINE FADNFDQDDP
EYITLREAFM QRFKEHGFVI ESIKEFNEQS EALEDVLKKL AEIKRKNTAI LRRYKGDTKF
ARVHKRIKEE NERRKITSAT PIASEYDEDI VDVLNTIKRN IDSKVYDRND ILKKDAYFEQ
TVMKEITDSM NSMNFSNSRE DRSFIQFRVS REYLDQYNSY YMYA
//
