ID A0A1R4ITG5_9MICO Unreviewed; 1047 AA.
AC A0A1R4ITG5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN ORFNames=FM104_03815 {ECO:0000313|EMBL:SJN22969.1};
OS Microbacterium esteraromaticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=57043 {ECO:0000313|EMBL:SJN22969.1, ECO:0000313|Proteomes:UP000196320};
RN [1] {ECO:0000313|EMBL:SJN22969.1, ECO:0000313|Proteomes:UP000196320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B Mb 05.01 {ECO:0000313|EMBL:SJN22969.1,
RC ECO:0000313|Proteomes:UP000196320};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUKO01000012; SJN22969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4ITG5; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000196320; 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; 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.
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:SJN22969.1};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000196320};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 295..528
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|SMART:SM00487"
SQ SEQUENCE 1047 AA; 114949 MW; FDD5EC1F38BD9A45 CRC64;
MSDAQLLEHE FETNLCEELA ERGWLYEDAG RTAAAGWDVG LALVPRDVLS WLQTQYPDEY
EKAVPSDLVN GQRDAAERGL LEHLTKELAK QTKMDPTTGH PVGGLLGVLR KGFSYAQIGR
PAAKFGPMVI FPPANPNLIE VVEQSDAVVL RILRQVRFDT ATTESIDVVL TANGLPIVTM
ELKTDNTQTV QHAIRQYKED RKPGRTRALL APGRALVHFA VSTDLVFMTT KLQGGDTVFL
PFNQGNNGHE GNPVSDTGSP ANYLWRDILA RSTFLRILKD FALFEPSKTG KKDGRLVFPR
FHQLRAVERV VGDIEQRGPG GKYLIWHSAG SGKTKTIAWL SHRLIRHMSA DSKSTFDSVI
VVTDRTVLDE NVRDDMNLVQ SSKGLVVSVG EKSGAKSPQL KKALLEGDHI ITCTLQTFPE
VMKLIENMDD LRGRRWAVVA DEAHSSQSGA SARQLKELLA DVVGLDFDED DIDAELSAED
LLRAKNSAVA NAENITFIAL TATPKAKTLR LFGTQNLETD RWEAFDTYTM AQAIEEGFIL
DVLRNYSTYD MFLRVKNAIE GEEDTEIQVN TGEAVTNIVR YARLHPTAVA QKVRVVVEHF
RRNVAHLLGG EARAMVVTGT RMEAYTWSKK MNAYIAEQGY TDMDTLVAFS GSLADGSGDR
VTEVSMNGVS DVAAAFREEG IYKVLIVANK FQTGFDEPRL MAMYVDKKLS GITTVQTLSR
LNRMYPGKTS PMVVDFMNSP EHIEKDFQLY YEDAHVEGEV DPNALYTLAE RLDTAGYYTE
SGLEAVARAY LEGLGGEQIS KAVSPIAARW QGAWKQAKLA GDKAARAEIE AFRADVISYR
NAWQFLSQIV DYDDPALAER AVLTTLLARR LHTDGIEIDM SYLDGVQLTG VKLVPSAIGE
DHSLREGSGE AIPLPAFDGE RGGGVGSAPK RGPLDEAIDA VNELFSAKGV DVSSDSVAGF
ITAFWGFLDA DDDAVAMARN NSAAQMKASE SFNNAVGLAM LKAVRESQEI QSYMTDPSFM
DDIAEIAANA LHAQHQEDAD GRVEAGA
//