ID A0A0M7BDQ0_9RHOB Unreviewed; 1023 AA.
AC A0A0M7BDQ0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 Name=hsdR_2 {ECO:0000313|EMBL:CUH39475.1};
GN ORFNames=JSE7799_02202 {ECO:0000313|EMBL:CUH39475.1};
OS Jannaschia seosinensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=313367 {ECO:0000313|EMBL:CUH39475.1, ECO:0000313|Proteomes:UP000049455};
RN [1] {ECO:0000313|EMBL:CUH39475.1, ECO:0000313|Proteomes:UP000049455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7799 {ECO:0000313|EMBL:CUH39475.1,
RC ECO:0000313|Proteomes:UP000049455};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-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; CYPR01000149; CUH39475.1; -; Genomic_DNA.
DR RefSeq; WP_055663653.1; NZ_CYPR01000149.1.
DR AlphaFoldDB; A0A0M7BDQ0; -.
DR STRING; 313367.JSE7799_02202; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000049455; 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 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 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:UP000049455};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 271..443
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1023 AA; 115380 MW; C325F3AE534E37FA CRC64;
MSKIGEAERK AQNRVIDLLS AHQTDAPGGL GWRYLGDWQK REGNANIEED LLRLWLLSRG
YAPEIVTQAI TLLKREARME DTKLYEANQS FYEMLRYGLA VAPGPGEAPV TVRFIDWADV
AANDMGVAEE VAIKGKDAKA WNKRPDLVLY VNGIALGTVE LKKSTVGVGE GIRQTLDNQR
PEFIRHFFTT VQITFAGNDS EGLRYAPIQT PQPYWLAWKE ESEITARLDR DVTQMMSPAR
FLELINDFTL FDAGIKKIAR PNQYFGVKTA QERVQAKEGG IIWQTQGSGK SLIMVMLARW
IREAKPDARI LVVTDRKELD RQISEDVFGG TGDKVRRARS GTDLMAALAD PTDRIICSLV
HKFGKREETE MAGLISDIQS AKIGAPVGEF YVFIDEAHRT QSGTLARAMR QVLPDAMFIG
FTGTPLLKSD KETSLETFGP YIGKPYRFDE AVDDGVVLDL RYEARDIDQR ISAPAKIDAW
FEAHTKMLTP IAKATLKQRW GTLQRVLSSR DRLEQIAKDI IMDMEMKPRL NAGRGNAMLV
AGSIPEACKF FEIFRKSGSV LADRCAIVTS YKRAAPEITG EETGMGETEK QYVHRVYTDL
LGETSEENYE EEALRLFKKE PGRMKLLIVV SRLLTGFDAP TATYIFIDKQ MKDHGLFQAI
CRVNRLDGDD KDFGYIVDYK DLFRNIESAV DDYTSEAFDA FDKEDVEGLI TDRAEQADQD
LRLARDAWLG LMDGVEQPKS DDEIFVYFSS PQGIDIDPDA EEKARRRQAL YKIAGRYARA
FANIAAEPEG SGFNDLELGE IRREVECAIG IRDAVRLHSG DAVDMKLYEP AMRHLIDNYI
RANDSDIISH LDDISLIDLV ESKGADAEND LPPASKRKRE NVAEAIENNV RKLIIEETPV
NPRFYEKMSE LLTDLVRQRR EGAIEYAEYL ERIAALVRDA KAGHGNTYPP SIKSAGLKAL
FDNLDTDEAM ALQVDRAVRE TAPFGWRGNA MKERKVRRCL AQVLDDPDTV ERIFEILKNQ
SEY
//
