ID U2Q654_9ACTN Unreviewed; 1061 AA.
AC U2Q654;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=HMPREF0682_1973 {ECO:0000313|EMBL:ERK51856.1};
OS Propionibacterium acidifaciens F0233.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=553198 {ECO:0000313|EMBL:ERK51856.1, ECO:0000313|Proteomes:UP000017052};
RN [1] {ECO:0000313|EMBL:ERK51856.1, ECO:0000313|Proteomes:UP000017052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0233 {ECO:0000313|EMBL:ERK51856.1,
RC ECO:0000313|Proteomes:UP000017052};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (AUG-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:ERK51856.1}.
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DR EMBL; ACVN02000269; ERK51856.1; -; Genomic_DNA.
DR AlphaFoldDB; U2Q654; -.
DR Proteomes; UP000017052; 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; 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 Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 280..455
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1061 AA; 118888 MW; 99043AB07688453A CRC64;
MMITEAQLEA SLLDWLGDLG WEPGTGTELE PQRASLGDLV LTEDLVEALR LLNPSVPDQY
LREAAADMVR VRSQDALAEN RDFHVLLVHG YRGLSYVDAD GREQTLTIRL LGAPEQNRYR
AAQQVRLLRG DQSRRLDVVL YVNGLPLVVV ELKQAGTRNA TIAKAHAQLG TYLAEFPAAF
RPVVAAIISD GINARYGTPF TRLNHYSPWN VDEDGAPSPA DSDQLLELEN LAHGLLEPAR
LLDVVRNFTA FDETDEGLTK RIAKPHQYFA VRKALDSTLA ALGTNGKAGV VWHTQGSGKS
MEMELYTNLV LTHPRMQNPT IVVITDRNEL DGQLYGTFAR STLLPDEPRQ IKRRSQLRSE
LAGRASGGIY FTTLQKFSRT AAEHDAGHAH PLLTDRRNVV VIVDEAHRSH YDDLDGYARH
LRDALPNATL IAFTGTPISE VEHNTREVFG DYIDIYDLSR AVTDGATVPV YFEPRLIEVR
LDDDMSAEKL DELADEQTEG LDDEARERVE RTVAKLNAIY GAPERIDALA RDIVEQWERR
RESMTEFLAP TEPGENTEPH GKALIVCATR EICARLYTRI VELRPGWYSD QDDRGLVKVV
YSGSPSDPEP IRSHVRRDSQ NKAIKNRLRD VDDDLELVIV KDMMLTGFDA PPLHTLFLDR
PLKGALLMQT LARVNRTFRG KQDGLLVAYA PLTENLNQAL REYTATDETT RPVGRDTAEA
VRVTWEIVAA LRELLVGHDW RTTATSGARD AGLRAVSDTV EYLRSPATPG NQAEQDGQTL
GERFRALSTQ LARMWTLAGG TENLAEIATE VRFYEEVRVW MAKLDARQRE ANGQPVPEEI
VRVLRGAVAQ ATAAGDITDL YEAAGLQRPT LQELDVQTIE QMRQGPSPHL AVEALRDLLV
KEAEAVTRNN VVRRKTFSER ISELMIRYTN QQITAADVIY ELGRLAEDVR AENGRGTRFD
PPLSHDELAF YDAVCQNDSA VLARGTDVLA RIARELVAVM RRDTRTDWTR RPEAQARLRA
SVKRLLRRHH YPPDKQKSAV ELVIEQMETL APGYVRGKDS L
//
