ID A0A0D5YS66_9FLAO Unreviewed; 1085 AA.
AC A0A0D5YS66;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=VC82_1506 {ECO:0000313|EMBL:AKA35127.1};
OS Allomuricauda lutaonensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=516051 {ECO:0000313|EMBL:AKA35127.1, ECO:0000313|Proteomes:UP000032726};
RN [1] {ECO:0000313|EMBL:AKA35127.1, ECO:0000313|Proteomes:UP000032726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-HSB-11 {ECO:0000313|EMBL:AKA35127.1,
RC ECO:0000313|Proteomes:UP000032726};
RA Kim K.M.;
RT "Complete genome sequence of Muricauda lutaonensis CC-HSB-11T, isolated
RT from a coastal hot spring.";
RL Submitted (MAR-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}.
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DR EMBL; CP011071; AKA35127.1; -; Genomic_DNA.
DR RefSeq; WP_045801814.1; NZ_CP011071.1.
DR AlphaFoldDB; A0A0D5YS66; -.
DR STRING; 516051.VC82_1506; -.
DR REBASE; 109834; Mlu11ORF1511P.
DR KEGG; mlt:VC82_1506; -.
DR PATRIC; fig|516051.4.peg.1553; -.
DR HOGENOM; CLU_005762_1_0_10; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000032726; Chromosome.
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:AKA35127.1};
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:UP000032726};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 332..519
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1085 AA; 121857 MW; 5A6CC96A0BC5CD44 CRC64;
MTRITENSIE DFAIKLLEHL GYEYIYGPSI APDAEDSALS GVERRTSFEE VLLTQRLTEA
VRRINPTVPP AAQEEAIKEI QRIHSPELLT NNETFHRFLT EGIKVSYQKD GQQRGDLVWL
IDFNTPENND FIVANQFTVV EDGVNKRPDV ILFVNGIPLV VIELKNAADE NATIKSAFRQ
IETYKAVIPS LFTYNAFTII SDGLEARAGT ISAGYSRFMK WKTSDGKTEA SGLVPELDTL
IKGMLNKATL LDLVRHFIVF EKSSRQENHG NQEIGQIKVQ TIKKLAAYHQ YYAVNRAVES
AMRATGYTVE KETPTSMVME SPESYGVAGV KSQPKGDRKG GVVWHTQGSG KSLSMVFFTG
KIVLALDNPT VVVITDRNDL DDQLFDTFAA STQLLRQEPK QVESRQDLKE KLKVASGGVI
FTTIQKFSPE EGNVYETLSE RENIVVIADE AHRTQYGFKA KTVDDKDEHG NVIGKKTVYG
FAKYMRDALP NATYIGFTGT PIESTDVNTP AVFGNYIDVY DIAQAVEDGA TVRIYYESRL
AKVNLSEEGK KLVEELDDEL DGEELTETQK AKAKWTQLEA LIGSENRIKN VANDIIQHFG
QRQEVFEGKG MIVAMSRRIA ADLYEEIIKL KPEWHSDDLD KGVIKVVMTS SSSDGPKIAK
HHTTKQQRRI LADRMKDPDD ELKLVIVRDM WLTGFDAPSM HTLYIDKPMK GHNLMQAIAR
VNRVYKDKPG GLVVDYLGIA SDLKKALSFY SDAGGKGDPT IAQEQAVELM LEKLEVVAQM
FNGFPYEDYF EADTSKKLSM ILAAEEHILG LEDGKKRYIN EVTALSKAFA IAVPHEQAMD
VKDEVSFFQA VKARLAKFDS TGSGRTDEEI ETTIRQVIDQ ALVSEQVIDV FDAAGIKKPD
ISILSEEFLL ELKGMKHKNV ALEVLKKLLN DEIKAVSKRN LVEGKSLKDM LENSIRKYHN
KILTAAEVME ELINLSKEVV NVKEGPKKMG LSDFEYAFYR AVANNESAKE LMQQDKLREL
AVILTERVRK NASIDWTIKE SVRAKLKVII KRTLRQYGYP PDMQKLATET VLKQAEMIAK
ELTNN
//
