ID   A0A136HEJ3_9GAMM        Unreviewed;      1155 AA.
AC   A0A136HEJ3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   03-MAY-2023, entry version 19.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=AXW15_08995 {ECO:0000313|EMBL:KXJ53925.1};
OS   Neptuniibacter sp. Phe_28.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Neptuniibacter.
OX   NCBI_TaxID=1795871 {ECO:0000313|EMBL:KXJ53925.1, ECO:0000313|Proteomes:UP000070472};
RN   [1] {ECO:0000313|Proteomes:UP000070472}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Donaho J.A., Gutierrez T., Seitz K.W., Teske A.P.,
RA   Baker B.J.;
RL   Submitted (FEB-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}.
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:KXJ53925.1}.
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DR   EMBL; LSMR01000127; KXJ53925.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136HEJ3; -.
DR   Proteomes; UP000070472; 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; 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; 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; 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.
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   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          386..543
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   COILED          159..211
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1155 AA;  132531 MW;  85993910333FB35A CRC64;
     MSNFAFLNEW PELQEHAKQA EAVVNSDPRS SCFYSRYTLE RTVYWMFEFD AWLARCKPKY
     DSTLNTLINQ SEFKRSLGSN VFPKIKAVQK AGNNAVHSER KVSARESTQS LKELHHILYW
     FYRTYTAVKP AADQVFDLNK IPQTVQVDAK LVMTSAKKLK ELQKTLSERD DQHQEILEKE
     RKQNKALQAQ LTKLQQQLAE QKAQNSKAAE QVKDPHDYCE AETRKYLIDQ YLKEMDWNLD
     APNVKEFPVT GMPISKQNPK GNGYVDYVLW GKDGKPLAVV EAKRTTRSAK EGKRQAELYA
     DCLGNDPQLG GQRPLIYYTN GYEIYFWDDL SYTERKVQGF LNQDEMQRII DRRALALDLK
     AVELDTHIAG KGRPYQRLAI ESVCEQFGIE RQRKSLLVMA TGTGKTRTTI ALVDLLMRAG
     WVKNTLFLAD RNALVNQAKK EFSKLLPKSS PEILSSGTRT LKGRVYLSTY PTMMNLLSAA
     PDTRLFGVGH FDLVIVDEAH RSIYKKYRYI FDYFDALLLG LTATPKSEID KNTYDIFEQP
     DDDPTFAYEL HEAIADKFLV PPKDVKVDLG FVRKGIKYSE LSDDEKDEWE SKEQLEDRDE
     VLPSEVNQFL FNIDTVDKAL EILMERGIKV AGGDRLGKTI IFAANNAHAE FIVERFDANY
     PKYKGKFARV ITYKETYADS LIDEFKGEKK PSDNNVPLTI AASVDMLDTG IDVPEVVNLM
     FFKVIKSKVK FLQMLGRGTR LCENLFGPED NKQFFKVFDI CKNFEYFEMN PDGAKDNGTK
     SLSQAIFEKR LTLSQQLIDN EKFGLYGAEL QRYLIEILHH RVEGMNLDNF IVRPVRRVVE
     KYKKLDAWWK LDNESLAELE KQVAILPTEA EPLAPDEQDE ELALRFDHMV LMMQLALTDN
     TGISDYYQDK LTQIASKLES KASVPAVSDQ LEWIQYVQSA HFWTDLSLEE LEQTRRKLRL
     LLRHIETESK GVVYTNFQDE VLGIEENEGV YEFSSEGGLA LYRKRVESYI REHQDDLTIQ
     RIKRNQSITK LDLAQLDNKL FEASGIPDKE SYLSTIHPDK SLGVFIRELV GLDRGAAKEA
     FSVYLDEATY NSQQIRFVNT IIDYLTQNGV MSPAMLAKPP FSDIHFEGVF GLFDDGAVMD
     LRNRIKGIEA SAVGE
//