ID   A0A1R1MI00_9GAMM        Unreviewed;      1113 AA.
AC   A0A1R1MI00;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=BGP75_03665 {ECO:0000313|EMBL:OMH39417.1};
OS   Motiliproteus sp. MSK22-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Motiliproteus.
OX   NCBI_TaxID=1897630 {ECO:0000313|EMBL:OMH39417.1, ECO:0000313|Proteomes:UP000187359};
RN   [1] {ECO:0000313|EMBL:OMH39417.1, ECO:0000313|Proteomes:UP000187359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSK22-1 {ECO:0000313|EMBL:OMH39417.1,
RC   ECO:0000313|Proteomes:UP000187359};
RA   Nakajima Y., Yoshizawa S., Ogura Y., Hayashi T., Kogure K.;
RT   "Draft genome of Motiliproteus sp. strain MSK22-1.";
RL   Submitted (AUG-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:OMH39417.1}.
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DR   EMBL; MIEQ01000020; OMH39417.1; -; Genomic_DNA.
DR   RefSeq; WP_076714746.1; NZ_MIEQ01000020.1.
DR   AlphaFoldDB; A0A1R1MI00; -.
DR   STRING; 1897630.BGP75_03665; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000187359; 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; cd22332; HsdR_N; 1.
DR   CDD; cd18800; SF2_C_EcoR124I-like; 1.
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   InterPro; IPR021810; T1RH-like_C.
DR   PANTHER; PTHR30195:SF15; TYPE I RESTRICTION ENYME HINDI ENDONUCLEASE SUBUNIT; 1.
DR   PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR   Pfam; PF04313; HSDR_N; 1.
DR   Pfam; PF18766; SWI2_SNF2; 1.
DR   Pfam; PF11867; T1RH-like_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187359};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          287..526
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|SMART:SM00487"
SQ   SEQUENCE   1113 AA;  126709 MW;  7B72DDCB82DB20B5 CRC64;
     MSEYQFVEKP LLNQLESMDW QVIEQGSGVP QNPTLSLRSS FREVMLKNEF IQAVKAINLL
     DSGQPWLTDS QLETLFEDFS YFDTTDLLKA NETFLTRLYK WQVDANEVTG EQDPVVKIID
     FDDWQANRFI AINQFRIDTP GGVKDSIIPD IVLFVNGIPL VVIECKDVNS FTSDAMSEGI
     KQLRRYADLR EDTIEAGLKE GEQQLFWTNQ LMISTYGDDS KFGSITSTED YFFHWKTIHP
     ATTPYMDLEI KVHRKQEQLV QGMLSPERLL DITRSYTLFM DAGKQRIKVI CRYQQYRAVQ
     KILARMRSGK SGADRSGVVW HTQGSGKSLT MVFLVRRLRR DPLLKDYKVL MVNDRKDLDK
     QLGETAALTG EKVYSISSAT AVWEKLTDNS STLNMVMVHK FREEDDSNTP AYFAKAIDAA
     NEPANHYSTK GADYSSKVAE PSTNYAVFDT FGEVNTSDKV LILIDEAHRT QRSGKDRASL
     SDNLFDAFPK ATRLAFTGTP LIADHHTDPT WKRFGNDPDN PYIDTYKLQD AVDDGATLQI
     LYEGKTADTA IYDKHGFDTK FEDLFKDRSD EELAVIRRKY GATGDVLEAE DRIQEIADDL
     VKHYIRNILP SGFKAQVVCA SKQAAIHYQT YIRKALGTWR TEEESKPKDE QDKALLEQVR
     QLKAAVIISS DGTNEKAVFV AARKEARELN AVENFKKKFD AEKPETGVAF LIVCDMLLTG
     FDAPIEQVMY IDKKLKEHNL LQTIARVNRT YPDKTVGYVV DYIGLTENLK TALSLYSGKD
     QTDILESFKS IESEIPVLES RYRRLIQLFE DNDISLIEAL VKQKLDNNAQ RYEVTEAAVR
     ALEDIKTRDS FNVYLKKFMQ SMDIILPNRL ADPFKIPMYQ FSHLQAKARE RYKDDSINIG
     GAGEKVRKLV NEHLVSLGIN PKVAPVELFS PSFVQNVRKN QDARAAASEM EHAIRKHCKI
     NEGEDPVMYK RFSEKLEEVL KKYNESWDQV VMALEELREE IDRGRGDQSD SNGPFYDLIV
     DIAFDGDASP GKQQPIKNLV DAIIGVLGDE IRTLNFWQRP AEVAALEGKL EEAFILSDIT
     ELMDCQEQLV TEVVALAKRR EQSLLEDTAE VEA
//