ID A0A0X8D6B8_9BACL Unreviewed; 1113 AA.
AC A0A0X8D6B8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN ORFNames=ACH33_16035 {ECO:0000313|EMBL:AMA74178.1};
OS Aneurinibacillus sp. XH2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=1450761 {ECO:0000313|EMBL:AMA74178.1, ECO:0000313|Proteomes:UP000065566};
RN [1] {ECO:0000313|Proteomes:UP000065566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xh2 {ECO:0000313|Proteomes:UP000065566};
RA Xi L.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMA74178.1, ECO:0000313|Proteomes:UP000065566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xh2 {ECO:0000313|EMBL:AMA74178.1,
RC ECO:0000313|Proteomes:UP000065566};
RA Zhang Z., Qiao N., Zhang Y., Xiao Z., Jing L., Zhao J.-Y.;
RT "Draft genome of the novel themophilic polyhydroxyalkanoates producer
RT Aneurinibacillus sp. XH2 (CCTCC M 2013550) isolated from Gudao oilfield in
RT China.";
RL Submitted (JAN-2016) 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; CP014140; AMA74178.1; -; Genomic_DNA.
DR RefSeq; WP_057899903.1; NZ_CP014140.1.
DR AlphaFoldDB; A0A0X8D6B8; -.
DR STRING; 1450761.ACH33_16035; -.
DR REBASE; 137617; AspXH2ORF16045P.
DR KEGG; anx:ACH33_16035; -.
DR Proteomes; UP000065566; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; 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; cd18032; DEXHc_RE_I_III_res; 1.
DR CDD; cd18799; SF2_C_EcoAI-like; 1.
DR Gene3D; 3.90.1570.30; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR025285; DUF4145.
DR InterPro; IPR013670; EcoEI_R_C_dom.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR Pfam; PF13643; DUF4145; 1.
DR Pfam; PF08463; EcoEI_R_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Helicase {ECO:0000313|EMBL:AMA74178.1};
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:UP000065566};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 357..518
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 590..759
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 153..190
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1113 AA; 129932 MW; E551C4BE623D63C6 CRC64;
MLSNFHFLVE KPHYESFTNA CLEAEKALIV SPATCAILTR RALELAVKWV YSFDSALKAP
YQDNLSSLIH HHGFLSIIDE DLLPLLRYIV KLGNVAVHTN SMITREEAIL SLHNLHQFVS
WIDYCYSDEY TAADFDESLL QIGEEKRERP EELKDLYERL SSKDKRLEEM MKENEQLRAL
LTAKREANTK EYDFQVDESS EFETRKKYID LDLKLAGWEF KKDVVIEYPV VGMPNQEGIG
YVDYVLFGDN GKPLAVIEAK RTTADPNKGK QQAKLYADCI EKMYGQRPII FYTNGFETNI
WDDLNYPARK ISGFYNKEEL RLLIDRRTMN LPLKNVKIND NITNRYYQKE AVLAVCDALE
KKRRKALLVM ATGSGKTRTA ISIVDVLTRH NWVKNILFLA DRKTLVTQAK NNFSHLLPNL
TLCNLLDNKD NPEESRMVFS TYPTMMNAID EAKRKDGKRL FTVGHFDLII VDESHRSIYK
KYRAIFHYFD AMLLGLTATP KDEIDRNTYE VFDLENGVPT YAYELDQAVQ DGYLVDYRTI
ETKLKFLEEG IHYDDLSEEE KERYEETFDD EVGEDIDSAA LNEWLFNDDT IDTVLKNLME
KGIRVEGGDK LGKTIIFAKN HRHAERIVQR FDQLFPEYKG GFARVIDYSV NYYQTLIDDF
SDRNKLLQIA VSVDMLDTGV DIPEVVNLVF FKKVRSKSKF WQMIGRGTRL CKDLLGIDQD
KTHFLIFDYC GNFEFFRENP KGIEGKAVES LTERLFNSKV EIIKELQHLQ YQEEEYIAHR
NEFIDEVLAE INKLNEENFR VRQHIQYVHK FKNRAKWDSL AAMDVNEIKK YISPLIVPLN
DDEFAKRFDL LMYTIELAKL QTKNATKPIK SVIRTAEALS RLGSIPQVVE QKYIIEKVQT
EEFWSEADIF ELETVREALR DLVKFLEKET QKIYYTNFKD EILEVKENGP MFDVNDLQSY
RKKVHHYLHE HRDQIAIYKL RNNKKLTAQD LKALEEILWN ELGTKEDYQK EFGETPVTKL
VRQIVGLDPQ AANEAFSEFL SSERLNINQS RFVKLIIDYF VRNGVMDKKV LQEEPFKTAG
GIVELFKDNM DDARKIIRII DEINKNSEDI VGA
//
