ID   A0A1Z5HDH9_9GAMM        Unreviewed;      1061 AA.
AC   A0A1Z5HDH9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=bplSymb_SCF10101P004 {ECO:0000313|EMBL:GAW87542.1};
OS   Bathymodiolus platifrons methanotrophic gill symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=113268 {ECO:0000313|EMBL:GAW87542.1, ECO:0000313|Proteomes:UP000196430};
RN   [1] {ECO:0000313|EMBL:GAW87542.1, ECO:0000313|Proteomes:UP000196430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPD1508-B01-01 {ECO:0000313|EMBL:GAW87542.1,
RC   ECO:0000313|Proteomes:UP000196430};
RX   PubMed=28453654; DOI=10.1093/gbe/evx082;
RA   Takishita K., Takaki Y., Chikaraishi Y., Ikuta T., Ozawa G., Yoshida T.,
RA   Ohkouchi N., Fujikura K.;
RT   "Genomic Evidence that Methanotrophic Endosymbionts Likely Provide Deep-Sea
RT   Bathymodiolus Mussels with a Sterol Intermediate in Cholesterol
RT   Biosynthesis.";
RL   Genome Biol. Evol. 9:1148-1160(2017).
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:GAW87542.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BDMN01000370; GAW87542.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5HDH9; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000196430; 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:GAW87542.1};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196430};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          280..515
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|SMART:SM00487"
SQ   SEQUENCE   1061 AA;  120046 MW;  920CDD58B4FF1E31 CRC64;
     MADHHEVNFE DNITQKLVNQ GWLEGKPANY DKQRALYTED VIKWIKATQP EVWIKLVKLN
     GLSAETILLD RLAKGLDSKG TIETLRNGFK IAGAGLISMG QKAPEDNRNE KVNKKYKENR
     LRVVRQLKYC PTREWEIDLV FFINGLPVAT VELKTDFTQL AELAVKQYKE DRLPIDPKTK
     RKEPLLTFKR GAIVHFAMSE SEIQMTTKLD GKNTYFLPFN KGNNGYAGNP AREYGEYPTA
     YFWEDILTTD AWLRIFHNFI YIETDKNKVD AKGKPYTKET LIFPRFHQLE AVNNMIDDAK
     KNGAGQNYLC EHSAGSGKTS TIAWTAHDLI SLRSPEGNAI FNSVIIVTDR NVLDAQLQDA
     VQQIDHQFGV ISAIEREKSN ESKSKQLAKA LTSGTPIIVV TIQTFPYAIE AILTEKSLSD
     RSFAVIIDEA HASQTGSNAQ GLRAALSMDS KKKMEDMSVD DLLLEVQNSR VRPANVSHFA
     FTATPKHSTM TLFGRPADPT QAVSDTNKPE SFHRYTMRQA IEEGFILDVL ENYMPYSAAY
     TLNESMKEDK RVDKKSARRS LAKWISLHPT NVSQKVDFIV NHFKDNVSHL LNGEAKAMIV
     TSSRASAVKY KLALDKYIKK NSIEGIQALV AFSDKIKATD LGDLTGFNVA DDAEFSESNM
     NSVGSQDLRH AFEQREYRIM LVANKFQTGF NQPKLVAMYV DKKVSGIESV QTFSRLNRIY
     PGKDKTFIID FVNEPDTILE AFKQYDNGAE LEKVQDLNVV YDMKDILDEQ HIYNDKDQET
     FKKTRDKSLL KGEVSPSMHK LLYAATQRPT DIFNEKIKNL NDSIQIWDNA FEKAYALGDK
     VAEKQTEHKR SEFTKEREEL MRFKTNLSRF VKTYNYIAQL ISFDDPDLEN FAAFSQLLAK
     RLKGVSPKDV DLTGLMISGY SIQALKQDEQ EDKAAEKLKP LKPNESPVSD REKQFLSEII
     AKLNELLGDT GTESGQKYFA VQIANDVTNN ELVSEQINKN TKEQSKNGDL PKVVTQSVIQ
     AMTSYNAIAS VLLKDKQVME DFVGIVYDLV KSGDSNGMLD I
//