ID   A0A3D8JAU2_9HELI        Unreviewed;       933 AA.
AC   A0A3D8JAU2;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=CQA57_03430 {ECO:0000313|EMBL:RDU74011.1};
OS   Helicobacter anseris.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=375926 {ECO:0000313|EMBL:RDU74011.1, ECO:0000313|Proteomes:UP000256695};
RN   [1] {ECO:0000313|EMBL:RDU74011.1, ECO:0000313|Proteomes:UP000256695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 04-9362 {ECO:0000313|EMBL:RDU74011.1,
RC   ECO:0000313|Proteomes:UP000256695};
RA   Mannion A.J., Shen Z., Fox J.G.;
RT   "Novel Campyloabacter and Helicobacter Species and Strains.";
RL   Submitted (APR-2018) 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:RDU74011.1}.
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DR   EMBL; NXLX01000006; RDU74011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8JAU2; -.
DR   OrthoDB; 9804086at2; -.
DR   Proteomes; UP000256695; 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   Gene3D; 3.90.1570.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; 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; 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, ECO:0000313|EMBL:RDU74011.1};
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:UP000256695};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          170..356
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   933 AA;  107406 MW;  880AD25CB9592D3F CRC64;
     MKKPEEIARE QIDQKLKLAG WEIQTKENFN RLASQGVAYC EFCTSDKKFA DYVLYVEGKI
     IGIIEAKKSG YLLSGVFAQS SHYANFIPKG APIFQNAPAF IYESNGEEIY FCDLREQDYR
     SRILSYFHTP SSLLNLIKSD PLRNFLKNIP LLEKNNLREC QYHAIKNLES SLAENHNRSL
     LQMATGSGKT YTACNISYRL LKYARAKRIL FLVDRKDLGS QTLSEYENFK ISNRSFSELY
     IINHITQNTI PEDSQIVIMT IQRLYSILTN TPLTEEDEEL ESSQTLQNVI SKIPYNQSIP
     FDFFDFIIVD ECHRSIYGNW RAILDYFDSF IIGLTATPSK LTFGFFQSNL IYSYTYEQSV
     LDGVNVDFWA WRIETNITQN GSVIPPKSLI IKRDKRDRKI IYEELDEELA YSNKDLDTKV
     LNRSQIRTIL TEYKKLIYSQ LFSERKSEDE SKNLAYIPKT LIFAKDDHHA EEITLIAREV
     FGKGNTFAQK ITHTNKNSKE AIRDFRTNPN FRIAITVDMI ATGTDIKPLE VLIFMRNVKS
     SGYFEQMKGR GCRSIDDQAL REVTPNAKSK NKFYIIDCIG VLDSAKILST PIIKGDRAQT
     PTLKKAIEDI AKGIITPQNT SLLASKISRI AQKIDKKDEA YLQKLLEETF IPPIQTPLQG
     NFGENKEEYD FIPSNSLLSL SKQLYTLSNI LEEDITLHPS TPTPLTQEEQ KEQLANFITA
     PFNHASFRNS LINIAKILYI YIDELNTDEV TLSQPIESTN QIEDFERFII EHKDSILALS
     ILYDKKKIHI TQNALEELKQ KLQESQIDIA KLWKSYAKKQ NKQSAYKNLT DLISLVRLGY
     QQIKELHSFA ENANKLYELY LGRLINKGIH LTKEQRNLFD TIKECIITEG YFSQKDFGEY
     FADEGGIAYA NRVLGDSFKL EVCLEELYEA LVG
//