ID Q6F779_ACIAD Unreviewed; 1020 AA.
AC Q6F779;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN OrderedLocusNames=ACIAD3430 {ECO:0000313|EMBL:CAG70086.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG70086.1, ECO:0000313|Proteomes:UP000000430};
RN [1] {ECO:0000313|EMBL:CAG70086.1, ECO:0000313|Proteomes:UP000000430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG70086.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6F779; -.
DR STRING; 202950.GCA_001485005_02263; -.
DR REBASE; 9583; AspADPORF3432P.
DR KEGG; aci:ACIAD3430; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_010804_0_0_6; -.
DR Proteomes; UP000000430; Chromosome.
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; 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; 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 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};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAG70086.1};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000430};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 297..518
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1020 AA; 116635 MW; 3E7ADE3A772C2587 CRC64;
MGGNAMHSEY YFEQAIEQSL TTAGGYVKGN PKDYDPRLAL FPKDVVAFIQ ETQPKVWEKI
HNSCKDETET RIVNDLAHAL DTEGALSVLR QGFKCFGKKI KMAYFAPNTS INKTTKEQYD
ANVLKCTRQL RTEFNEVPDM VLSLNGIPMI TLELKNEFSA SGWNVEDAKI QFKKDRNAKG
RLFEFKKRTL VHFAVDTCDV YMTTKLDGEN TFFLPFNKGY LNGKGNPPVE GDVRTHYLWT
ETLARHSFME IFARYMHLSV ETKKIRTDTG FRYIEKETMI FPRYHQLDAV RKLTKHSKAN
GSGHNYLIQH SAGSGKSNTI AWLAHQLASM HNADDKKIFN SIIVITDRIV LDRQLQETIA
QFEHKDGVVQ KIDENTLQLT NALASNVPII ITTIQKFPYI MQSIRTQAKK GIKVDLSTEG
KNFAVIVDEA HSSQSGETAM ELRKILNKDG IESAIAQEFL DDGDEDESEL TDDVKKHLFA
EASKRSRQPN LSFFAFTATP KWKTLACFDE AGDNGEAPFH HYSMKQAIQE GFILDVLANY
TTYGQYYKLI KIADNDPELA KNKTKALMAR FVSMHPSVIA QKVEIIVEHF RTVTMHRIGG
RAKAMVVTNS REQAVRYKLA FDEYIKEKKY TGIKSLVAFS GKLEVDGTEY TEPKMNGFKE
TELPDQFDTD DYQVLLVAEK YQTGFDQPLL HTMFVDKKLS GIQAVQTLSR LNRCAYGKED
TFVLDFVNTL EDIYKAFKPF YEQTKLGDIP NEQKLNELGH TLDQWKFYFE VDLNDFANIW
FKDRSKLTGH EHKQLNSIID RAVDKYKKIH PDDLVHQQEQ QKLFKSQLQS YLNLYLFLSQ
IMDFTDSEHE QRYAYLKALL QKLPKGSKEN EVDLSKIVEL QFYRLQKLSE NSIDLGHGEA
KALKGSTDVG TGQAESTDNV SHLIDELNEA FGTDFTVADQ LFFDQVEQAA IENEEIVQAV
NANSLDSFTE YLSGKLIDLF LVRLAGNEEV CNKVMSTDEL RKKVAKRLAK HIYTRTKKKV
//
