ID A0A0P6X8K5_9CHLR Unreviewed; 1022 AA.
AC A0A0P6X8K5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=ADN01_14755 {ECO:0000313|EMBL:KPL78460.1};
OS Levilinea saccharolytica.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Levilinea.
OX NCBI_TaxID=229921 {ECO:0000313|EMBL:KPL78460.1, ECO:0000313|Proteomes:UP000050501};
RN [1] {ECO:0000313|EMBL:KPL78460.1, ECO:0000313|Proteomes:UP000050501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIBI-1 {ECO:0000313|EMBL:KPL78460.1,
RC ECO:0000313|Proteomes:UP000050501};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Genome sequence of Levilinea saccharolytica DSM 16555.";
RL Submitted (JUL-2015) 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:KPL78460.1}.
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; LGCM01000055; KPL78460.1; -; Genomic_DNA.
DR RefSeq; WP_062418865.1; NZ_LGCM01000055.1.
DR AlphaFoldDB; A0A0P6X8K5; -.
DR STRING; 229921.ADN01_14755; -.
DR REBASE; 132902; LsaKIBI1ORF14745P.
DR PATRIC; fig|229921.5.peg.952; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000050501; 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:0004386; F:helicase activity; 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; -; 2.
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; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Helicase {ECO:0000313|EMBL:KPL78460.1};
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:UP000050501};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 312..464
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1022 AA; 117683 MW; 3B4EFBE797901A92 CRC64;
MSTYQIVAST TDATVVAEYA ADYSTRPESY QSEAELEAEF VRQLSAQGYE LFTGRDEAAL
RANLRRQLEA LNEMTFSEDE WGRFFRECVA NPGEGIVEKT RKIQVDHVQL LRRDDGSTKN
IYLLDKKNIH NNRLQVAHQI TQREGAYENR YDVTVLVNGL PLVHVELKRR GVAVREAFNQ
IQRYQRDSFW AASGLFEYVQ IFVISNGTHT KYYSNTTREA HLRRQGQGAA GGRGKHSSHS
FEFTSFWADA HNRIIPDLVD FSKTFFARHT LLNILTRYCV WTSENDLLVM RPYQIAATER
ILSRIAVSAQ YKRTGSIEAG GYIWHTTGSG KTLTSFKTAQ LAAALPTVDK VLFVVDRKDL
DYQTMKEYDR FEKGAADGNT STRVLQRQLE DRDEKGNPHE YRILVTTLQK LERFIRSNRQ
HPIYKKRVVL IFDECHRSQF GDMHQAVTRH FKQYHIFGFT GTPIFAANAG SGGSPLLRTT
EQAFGEKLHT YTIVDAISDQ NVLPFRIDYV NTLHMPEGVA DKKVYGIDRE KALADPRRVS
EVVRYVLEHF DQKTQRNTAY TLPSRTRQGE ERRVVGFNSI FAAASIPLAM RYYAEFRRQN
AEQQRGLKIA TIFSFSPNEE EAGGLLPDED FEMERLDAPA RDFLEAALRD YNAAFSTNYD
TSADKFQNYY KDLSLRMKNR EVDLLIVVNM FLTGFDATTL NTLWVDKNLR QHGLLQAFSR
TNRILNSVKT FGNIVCFRDL KEETDEAIAL FGNKDAGGVV LLRTYEEYYH GYEEEGQHQP
GYVERIAELT AAYPLGQPIT GEEAQKDFIR LYGAILRLRN ILSAFDDFTG QEILSERDFQ
DYHSRYIDLY QELRRGSEAD KESINDDLVF ELELIRQVEV NIDYILMLVA QYGQSNCQDA
SILTTIDKAV QSSLELRSKK ELIQRFIDQM NAATQVDEDW RQFLQERRAA DLEALIQDEK
LKPEETRRFM ENAFRDGVLK TTGTALDQIL PPISRFGGGR AEKKQGIIEK LLRYFEKYWG
LV
//
