ID   A0A1G8GGH6_9VIBR        Unreviewed;      1149 AA.
AC   A0A1G8GGH6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=SAMN04488136_13712 {ECO:0000313|EMBL:SDH93387.1};
OS   Vibrio xiamenensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=861298 {ECO:0000313|EMBL:SDH93387.1, ECO:0000313|Proteomes:UP000198854};
RN   [1] {ECO:0000313|EMBL:SDH93387.1, ECO:0000313|Proteomes:UP000198854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10228 {ECO:0000313|EMBL:SDH93387.1,
RC   ECO:0000313|Proteomes:UP000198854};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FNDD01000037; SDH93387.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8GGH6; -.
DR   STRING; 861298.SAMN04488136_13712; -.
DR   OrthoDB; 9804086at2; -.
DR   Proteomes; UP000198854; 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; 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; 1.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198854};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          383..535
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          607..795
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   COILED          148..203
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1149 AA;  131687 MW;  8066BB701683453E CRC64;
     MKTSVNFEHL RNQWPELADL GAFAENYAVS DPQSSMVKLR CYIEKIVGYL YSELHLPVEP
     NASVHDKLTN HSFIQIVDRL ILDKFHLIRR QGNKAAHEGY VDQHDAIWLV KEAYYIGVWL
     YIAYGNGHQD DLPDYQSPEN APRSGEEKAE YKRKNKQLQI KLAQNSAQLE QAIKELEEVR
     EAQLEAQREA ARLKLEIDQA KANQLIEKTI QLKSTFEFNE AETRKRLIDA ELRSEGWDVS
     DDDSSTEQVK KEFEVEGISS PSGKGFCDYV LFDDNDLPLA VIEAKRTRRD HKEGRDQAKE
     YADALEKRYG QRPVIFYTNG YDITLWDDAQ DYTPRQVFGY YSKDSLQYLI QQRTLRKSLL
     ETPIDINVAG RDYQIESITR VCERFVDKHR KALIVQATGT GKTRVAIALA KRLLAAGWAK
     RVLFLCDRKE LRKQAANAFN EHTKEPLFVK GRSKQDKMSS ARIVIATYPG MMQTYQEFDV
     GHFDLIVADE SHRSIYNKYG ELFKYFDALQ VGLTATPVEM ISRSTSQLFG CSYKMPTANY
     PLELAIEQGH LVPFKVVAHT TKFLRDGIHS ADLTDEQVAE LEEQGIDANE LEFDAKLIDK
     AIFNKDTNRQ ILKNLMENGL RDVDGQLPGK SIIFARNIDH ANLLAELFYE LYPQYGGQFC
     RVIHSKNERA EELIDQFKSA EGDNDEITIA VSVDMLDTGI DVPQCVNLVF AKPIKSKVKF
     WQMVGRGTRL CENLYGAGQH KKHFLIFDHW DNFNYFKMNP EEEEQRPGKS LAQQLFEAKV
     RLATEALKKA NMDLFAQTVP LIKADIEDLN DGVIAVREQW KLKAELSDER CLNAMAPVTR
     EKLLNQMAPL MQWRNTQGLS EALRFDLQMI NAQIVKLLQP DLIDKEVLPL MQKVTSLSMH
     LNEVRQHATT IAQVQERDFW QNAEFTEMEK VRQTLRSVIH LRDKGVSPEP PKPTVLDIKE
     DAAEYRTDEV KTDIRTVDYE IFRQEVEKTL TPLFDTDSVL KKIRAGEAVT EDELAQLSAL
     VHTQNPHVNL AILSEFYPDT SAPLDHILRT IIGMNRQEIE KQFTQFLQQL HTQLSSRQQR
     FIIMLKDHLC RYGTISVEQL YDAPFNQLDD AGLDGVFPIA AQADVIAQFV SHYSVPLGKK
     QASVTANNA
//