ID U2MM34_9BACT Unreviewed; 1100 AA.
AC U2MM34;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-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=HMPREF1218_1421 {ECO:0000313|EMBL:ERK02720.1};
OS Hoylesella pleuritidis F0068.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=1081904 {ECO:0000313|EMBL:ERK02720.1, ECO:0000313|Proteomes:UP000016600};
RN [1] {ECO:0000313|EMBL:ERK02720.1, ECO:0000313|Proteomes:UP000016600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0068 {ECO:0000313|EMBL:ERK02720.1,
RC ECO:0000313|Proteomes:UP000016600};
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:ERK02720.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWET01000021; ERK02720.1; -; Genomic_DNA.
DR AlphaFoldDB; U2MM34; -.
DR PATRIC; fig|1081904.3.peg.1040; -.
DR Proteomes; UP000016600; 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; 1.
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:UP000016600};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 292..483
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 978..1005
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1100 AA; 125987 MW; 1E72EE55E6227C64 CRC64;
MNSPYKTMAT YQEQRERDYQ NKLVKRFVDE LHYKYLGNWQ YAKGETVNSL GKQNSPILDD
EVRLYLKAQK KKDKTPKYTE RQIEDVLFQL KSKARLGNAK MSGLMQCNTD LYDVLMSGIK
SQPDPEFNHE DVMFFDFDDY SNNNFAIAEE VSYIDPLLGK NKRPDIVVYV NGIALAVIEL
KRSLVNYEEG IKQHLSNERD FIPSFFTTIQ FTIASNDGVE FRYGTIGTPL KFWCKWKRDT
TKLGDILTEQ ESYSMFFNKE NFMFFFRYGV LNDGGIKKVL RPHQIYAIKA AAARMPKKES
GVIWHSQGSG KSLTMVALAS YIRRNYENPR VVVITDRKEL DLQLAGTFIK GGNTLHRATS
SSDLLDTLNK GEEWLICSLI HKFGANGSED EAEKDESGTK VSLDEYLDEL QAIIAQKYGN
NFSVKGDNIF VFVDECHRTQ SGRLHEAMRT IMGKEIMLIG FTGTPLLKKD KGDMFNRIKS
MSERTFGPYI HKYLHKQAVE DKVVLDLQYE YRNVEQQLIN RQKVDQKLAA LTTGRELTDE
QRRMVEDRWA TLEKVYSTKE RIERIGYSIL DDIGFGLLQH DWSNAMLVAG SIYQAYRYYK
FFTQDSSNTQ LRRRVAVVTS YDPMDSDIAN DSADTSKETE AKFKYDWAKQ SFKDAGDGIN
NADDYEKWAK NLFIKRPAQM KLLIVVNKLL TGFDAPCATV LYIDNDIKDH TLFQAVCRVN
RLGEDIKDEE GNVIVRTHKE FGRIISFKNL FDSIEDAVVK FNDGEGFSGL DDVDVEGLLD
SAVNKCKEKL KAATEAYEGL KAIWESKGLT ELELLADYYV TEQKGETPAQ CRRNLMYSIT
GGMVATYNNI SDYFRQTDFT PKQIERFASL SREAGTIQRK VRQKSGDDFD PRTLDPDMRQ
LLDQHIRAED AETLVEASAD FSFLDLINDD TDTDKAADEA IRQAGGNANG AAEVIEGKAR
RVNTDWNSGD QEEQRAFSER LQALLDQLRE SNATAKERIK ALIEHIKAIK HGSEVPEGLN
NKRRKALWNN RAAWNAPADD SEVIEIIKKI DDFIYRNAGA NWQDPDSNAS WDLRDDLQAM
FPSFSEQDIY EIYRLASQNS
//
