ID A0A2N4XI53_9BACT Unreviewed; 1075 AA.
AC A0A2N4XI53;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=C0V77_01850 {ECO:0000313|EMBL:PLK46115.1};
OS Emticicia sp. TH156.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Emticicia.
OX NCBI_TaxID=2067454 {ECO:0000313|EMBL:PLK46115.1, ECO:0000313|Proteomes:UP000234203};
RN [1] {ECO:0000313|EMBL:PLK46115.1, ECO:0000313|Proteomes:UP000234203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH156 {ECO:0000313|EMBL:PLK46115.1,
RC ECO:0000313|Proteomes:UP000234203};
RA Cai h.;
RT "genomes of bacteria within cyanobacterial aggregates.";
RL Submitted (DEC-2017) 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:PLK46115.1}.
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DR EMBL; PKRS01000001; PLK46115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N4XI53; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000234203; 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; 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 Helicase {ECO:0000313|EMBL:PLK46115.1};
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:UP000234203};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 323..510
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1075 AA; 119770 MW; 8BD68DCFDF5CE899 CRC64;
MTKLTETHIE NLAIELLCQL GYAYIYAPDV APDSPNPERE SYAQVLLMSR LQAAVQTINP
GIPVDAQAEA IREIQRIASP DMLTNNETFH RFLTEGVPVT VRIGGEDRGD RVWLIDFKNP
ANNQFVVASQ YTIVENNHNK RPDLLLFVNG IPLVLLELKN AADANTTLHS AFRQVETYKA
LIPGLFTYNG FVVISDGLEA KAGTVSSGFS RFMAWKTADG KAEASHLVSQ LETLIQGMLN
PATLIDLVRH FIVFEKSKKT DTATGITSIT TVKKIAAYHQ YYAVNRAVES TLRASGYSPA
PYQTGMAVVA EPPESYGVAG VSQQPAGDKK GGVVWHTQGS GKSLTMVFYT GKIVLALSNP
TILVITDRND LDDQLFDTFA ASKQLLRQEP VQADDRNQLK DLLRVASGGV IFTTIQKFQP
QEGNVYELLS DRTNIVVIAD EAHRTQYGFR AKTIDDKDAG GNVIGKKIVY GFAKYMRDAL
PNATYLGFTG TPIESTDVNT PAVFGNYVDI YDIAQAVEDG ATVRIYYESR LAKVSLSDEG
RQLVEDLDDE LEQEDLNNAQ KAKAKWTQLE ALIGSQNRIS NIARDMVTHF CQRQEVFEGK
GMIVTMSRRI AAELYEAIIA LKPAWHSDDL NKGVIKVVMT SASSDGPQIA RHHTTKEQRR
VLAERMKNPD DELQLVIVRD MWLTGFDAPS MHTLYIDKPM QGHNLMQAIA RVNRVYKDKP
GGLVVDYLGV ASDLKKALAF YTNAGGKGDP TELKEKAVQL MLEKLEVVAA MFHGFEYKHY
FEADTSKKLS LILAAENFIM QPPDQKIRFI NEVTALSRAL ALANPTNESM DVIDEISFFQ
AVKACVVKFV SRGSGRTDEE IETTIRQVID KALVSEKVVD VFDAAGIKKP DISILSEEFL
MELKGMQHKN VAFELLKKLL NDEIKARANT NMVQSKHLME MLENSIRRYH NKIITSAEVL
EEIITISKEI VKMDNEAKAM GLTKYEYGFY TAVANNDSAK ELMQKEKLRE LAIVLTETIR
KNATIDWTIK ESVRSGLRVA VKRLLRKYGY PPDMQLLATD TVLKQAEKMA NEIAG
//
