ID I4W4J7_9GAMM Unreviewed; 1057 AA.
AC I4W4J7;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN ORFNames=UU5_12083 {ECO:0000313|EMBL:EIL94388.1};
OS Rhodanobacter sp. 115.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1162282 {ECO:0000313|EMBL:EIL94388.1, ECO:0000313|Proteomes:UP000004557};
RN [1] {ECO:0000313|EMBL:EIL94388.1, ECO:0000313|Proteomes:UP000004557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=115 {ECO:0000313|EMBL:EIL94388.1,
RC ECO:0000313|Proteomes:UP000004557};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
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 -!- SIMILARITY: Belongs to the HsdR family.
CC {ECO:0000256|ARBA:ARBA00008598}.
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:EIL94388.1}.
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DR EMBL; AJXS01000287; EIL94388.1; -; Genomic_DNA.
DR AlphaFoldDB; I4W4J7; -.
DR REBASE; 52025; Rsp115ORF12068P.
DR PATRIC; fig|1162282.3.peg.2301; -.
DR Proteomes; UP000004557; 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; IPR040980; SWI2_SNF2.
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; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 301..477
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 778..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1057 AA; 119719 MW; 776F4F845D48CB71 CRC64;
MTTFNEDSRV KIPALLHLER LGYRYLSLKQ ARRDPGNNIF PEILEAALLR INPDLRPQDL
PSLLDELHLD LQHEDLGKAF HKRLTARSGV RLVDFDNLDN NSWHAVTELP FENGEDNFRP
DITLLVNGLP LAIIEVKKRM NPGGVLEERR RMDRRHANRK FRHFFNLIQL QVFSNNMEYD
EAAIDPVQGA FYAASTYGDA HFNYFREERQ AELASAVAPL SEATEDAILT DTNLVSIKGS
PEFERNKAAD TPTHRLLTSL FSRQRLAFIL QYAFAWLDEE DGVQKHVMRY PQLFATLAIA
ERLAAGTRKG IIWHTQGSGK TALAYYNVRF LTDWFQQRGQ VPRFYFIVDR LDLLKQARDE
FRLRGLTVHV IDSRDAFARD IKQSGATRND RGTAEITVVN IQKFKDDPDV VAAQDYNLAV
QRVYFLDEVH RSYNPKGSFL ANLEQSDRGA IKIGLTGTPL IGEQLQSKAL FGDYIHKYYY
NASIADGYTL RLIREEIATR YKMELQQALA AIEVQQGGIE RKALYAHKHF VGAMLDYILR
DFVQSRITFG DDSIGGMVIC DSAEQARELH RQFQQLMQQE ARPIVAEPAN DAAYRQDRVA
EDAAHYARQP LSAALILHDE GDKQSREDQV KAYKKGRIDL LFVYNMLLTG FDAPRLKKLY
FGRVIKNHNL LQALTRVNRR YGKFRYGYVV DFADIQAEFD RANRDYYDEL TAELGDEIEH
YSQLFMSEAE IRASVEAIRE ALFAFSLDDA ELFSQQVGQI QDRQQLLAIV KALTQARETV
QPDPSRWSRA SRRPARFPQA ARSAHRGAER AGRAQPQAPA GTRRRHLRPA QPGAGGRDLQ
VRENRRGRAE AGRRTEGHPA PHPRNPGVHP GPARPGLDQP QGRTGAPVQG QETQRSEPAG
NAGEHHRAAR HRTARPHTQP GQRQPRRPLR RRRQADARAQ APAGFAPPGR QPDPPARRAG
RHQARHGRRR ARQPRTAGQP GVLRAQRHAH RDAPLPGQAA RAGCRHPPPD PAAAGGRIPG
RIPGPVAVRP GMNPRCWRPG AHRASVVSQM LCKRMPP
//
