ID F9U8Q8_9GAMM Unreviewed; 692 AA.
AC F9U8Q8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN ORFNames=ThimaDRAFT_1310 {ECO:0000313|EMBL:EGV19166.1};
OS Thiocapsa marina 5811.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocapsa.
OX NCBI_TaxID=768671 {ECO:0000313|EMBL:EGV19166.1, ECO:0000313|Proteomes:UP000005459};
RN [1] {ECO:0000313|EMBL:EGV19166.1, ECO:0000313|Proteomes:UP000005459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5811 {ECO:0000313|EMBL:EGV19166.1,
RC ECO:0000313|Proteomes:UP000005459};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L.,
RA Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V., Frigaard N.-U.,
RA Bryant D., Woyke T.J.;
RT "The draft genome of Thiocapsa marina 5811.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AFWV01000004; EGV19166.1; -; Genomic_DNA.
DR AlphaFoldDB; F9U8Q8; -.
DR STRING; 768671.ThimaDRAFT_1310; -.
DR PATRIC; fig|768671.3.peg.1402; -.
DR eggNOG; COG0610; Bacteria.
DR Proteomes; UP000005459; 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 Gene3D; 3.90.1570.50; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR InterPro; IPR040980; SWI2_SNF2.
DR PANTHER; PTHR42927; HELICASE SUPERFAMILY 1 AND 2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42927:SF1; HELICASE SUPERFAMILY 1 AND 2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF18766; SWI2_SNF2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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, ECO:0000313|EMBL:EGV19166.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000005459};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 136..226
FT /note="Restriction endonuclease type I HsdR N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04313"
FT DOMAIN 297..377
FT /note="SWI2/SNF2 ATPase"
FT /evidence="ECO:0000259|Pfam:PF18766"
FT REGION 435..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 692 AA; 76127 MW; FC8453FFD42F6392 CRC64;
MTTDTTERGL ERLICAAMTG SPCEPGALTH GPLDEPHADY GVGWMCGRAA DYDREYCVDL
TQLAAFLHET QLEVAAALDL HEDGPTRRKF LARIQGEITR RGTIDVLRHG IKHGPHHVDL
FYGTPSPGNA RAAERNKANR FSVTRQLRYS RDETQLALDL CLFINGLPVA SFELKNSLPK
QTVEDAVQQY KLDRDPRERL FELGRCVVHF TVDDHEVRFC TQLKGKASWF LPFNLGWNDG
AGNPPNPNGL KTDYLWRRIL TPAGLTDILE NYAQVVEIKN EKTGRKKTVQ IWPRYLQLDV
VRKLLADAAQ NGAGRRYLIQ HSAGSGKSNS IAWLAHQLIG LEQDGVPMFD SIIVVTDRRI
LDQQIKDTIK QFANDSDAIQ QAFSAYYRTT ILAEETDPDK LHDLKAALDG YQVYMSEQIE
DLVQRSLGGA ERDALDPILE PAWPSTETSS TRTARSTSKA RPKRSCGSTA SSPRSCPTPT
PTGRSSRSSS PFTLNPAVER PLECVPRGVR QGATRRRSGS TPTRCNAAGR RAGRAPGGVA
AVTRRVSSRT TTIFKAVKAL HEARSGQLPD LGSRAQAARP RGGGPRQGHP RSDRHGQLPG
REAGGSEDPA PRCGHGDRAG ADHRGRPQAR AEFGSALEHP QDLRRPVRPD LRARRSLSAR
VLGVHGQNAC ALRRLNAESS GKNGGDYSEG FL
//
