ID   A0A1Y6D0T9_9GAMM        Unreviewed;       821 AA.
AC   A0A1Y6D0T9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, 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=SAMN02949497_3950 {ECO:0000313|EMBL:SMF96549.1};
OS   Methylomagnum ishizawai.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomagnum.
OX   NCBI_TaxID=1760988 {ECO:0000313|EMBL:SMF96549.1, ECO:0000313|Proteomes:UP000192923};
RN   [1] {ECO:0000313|EMBL:SMF96549.1, ECO:0000313|Proteomes:UP000192923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=175 {ECO:0000313|EMBL:SMF96549.1,
RC   ECO:0000313|Proteomes:UP000192923};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-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   ---------------------------------------------------------------------------
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; FXAM01000001; SMF96549.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y6D0T9; -.
DR   STRING; 1760988.SAMN02949497_3950; -.
DR   REBASE; 218951; Msp175ORF3952P.
DR   OrthoDB; 9804086at2; -.
DR   Proteomes; UP000192923; 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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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; 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};
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:UP000192923};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          179..362
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          571..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..615
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   821 AA;  93000 MW;  15EC157DA33F0036 CRC64;
     MNKKNLSERD ICTKFITPAL DRAGWDIQSQ VREEVSFTKG RIIVRGKLVT RGKAKRADYI
     LYHQPNLPIA LIEAKDNSHA VGHGMQQALA YAEVLDIPFV FSSNGDGFVF HDRTGLATEV
     ETELGLEQFP SPAQLWERYR AWKGLEPAQE QVFLQDYHED SGGKEPRYYQ RVAINKTVEA
     IARGQDRILL VMATGTGKTY TAFQIIWRLW KAGARKRILF LADRNVLVDQ TMVNDFRPFG
     SAMAKLSTAA KTIEREDGVE VRLPSAVDKK HRRIDTSYEI YLALYQAITG PEERQKLFRE
     LSPGFFDLIV IDECHRGSAA EDSAWREILE HFSGATQIGL TATPKETEYV SNSHYFGPPV
     YSYSLKQGIH DGFLAPYKVV KVHLDVDVEG YRPAPGETDL NGYEIEDRHY NQKDFDRVLV
     IDERTRRVAH WVSEYLKQSG DRFQKTIVFC VDTEHAARMR QALVNENADL AGQNSRYVMR
     ITGDDAEGQM QLGNFIDPEA KYPVIVTTSR LLSTGVDAQT CRLIVLDRPV GSMTEFKQIV
     GRGTRVHEDS RKFYFTLVDF RGAANHFADP AFDGEPVQIY EPGEDDPVTP PEDVPPPADD
     DDEPLPPEPG EDETVIDGEP PIIHLPPEVG EAPGKYYIKG QPVTVLTERV EYLDENGKLV
     TESLRDYSRR TIRQQYTSLD QFLARWKSAE RKEAIIEELA EEGLLLDPLL EEVGKDLDPF
     DLICHIAFDQ PPLTRSERAA NVKKRDVFTQ YGPQARAVLD ALLAKYQDEG MLDGLDNVEI
     LRNRPFDTMG MPFQLIKQFG TKASFEDAVH ELQAALYQDV A
//