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Database: UniProt
Entry: H8GQ95_METAL
LinkDB: H8GQ95_METAL
Original site: H8GQ95_METAL 
ID   H8GQ95_METAL            Unreviewed;      1009 AA.
AC   H8GQ95;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=Metal_0720 {ECO:0000313|EMBL:EIC28554.1};
OS   Methylomicrobium album BG8.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomicrobium.
OX   NCBI_TaxID=686340 {ECO:0000313|EMBL:EIC28554.1, ECO:0000313|Proteomes:UP000005090};
RN   [1] {ECO:0000313|EMBL:EIC28554.1, ECO:0000313|Proteomes:UP000005090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BG8 {ECO:0000313|EMBL:EIC28554.1,
RC   ECO:0000313|Proteomes:UP000005090};
RX   PubMed=23580712;
RA   Kits K.D., Kalyuzhnaya M.G., Klotz M.G., Jetten M.S., Op den Camp H.J.,
RA   Vuilleumier S., Bringel F., Dispirito A.A., Murrell J.C., Bruce D.,
RA   Cheng J.F., Copeland A., Goodwin L., Hauser L., Lajus A., Land M.L.,
RA   Lapidus A., Lucas S., Medigue C., Pitluck S., Woyke T., Zeytun A.,
RA   Stein L.Y.;
RT   "Genome Sequence of the Obligate Gammaproteobacterial Methanotroph
RT   Methylomicrobium album Strain BG8.";
RL   Genome Announc. 1:E0017013-E0017013(2013).
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; CM001475; EIC28554.1; -; Genomic_DNA.
DR   RefSeq; WP_005369681.1; NZ_CM001475.1.
DR   AlphaFoldDB; H8GQ95; -.
DR   STRING; 686340.Metal_0720; -.
DR   REBASE; 62990; MalBG8ORF715P.
DR   eggNOG; COG0610; Bacteria.
DR   HOGENOM; CLU_010804_0_0_6; -.
DR   Proteomes; UP000005090; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; 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.
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   Helicase {ECO:0000313|EMBL:EIC28554.1};
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:UP000005090};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          306..509
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          440..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          888..911
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1009 AA;  114164 MW;  D63B6A2E44EC3C12 CRC64;
     MVSKTTEKEL EIAIEKQLTG TCLEAQKSVA EVGDLPFSPN HGYQLGLAQD FNARYAIDSK
     RFWAFLEHTQ HDGLEKLQKH GGDWRLKVLE RFDKLIKKYG LLHLLKKGLS VDDATLHLMY
     PAPLASSSDK VKQNFADNLF SSTRQVRYSL SNTLEEIDLV LFVNGLPFAT LELKNPWSGQ
     TARYHGQKQY CEDRDINQPL LQFGRCLVHM AVDTDEIYMT TKLAGQQTFF LPFNQGHNFG
     AGNPPNPNGH KSAYLWQAVF SKNSVANIIQ HFVRLDGSSK EPLDKRTLFF PRYHQLDVVR
     KLVAHAGQNG VGQTYLIQHS AGSGKSNSIT WAAYQLIEAY PASLDTPGAI ALEKPLFDSV
     IVVTDRRLLD KQLRDNIKDF SEVKNIVAPA FKSSELKSAL EQGKKIIITT IQKFPFIIDG
     IADLSDKRFA VIIDEAHSSQ SGSAHDNMNR AMGKSEQAEE DAVDVQDKIL QAMQSRKMRG
     NASYFAFTAT PKNTTLEKFG VKQADGSFEP FHLYSMKQAI EEGFILDVLA NYTTYKSYYE
     IQKSVADNPL FDSAKAQKKL RAFVERHQQT IAVKAEIMLD HFIPQVVNSK KLKGKAKGMV
     ITQNIEAAIR YYRAISQLLT DRGNPFKVAI AFSGTKEVDG IEYSEAQINS FAENETRDTF
     DKDEYRLLIV ANKYLTGFDQ PKLCAMYVDK KLQGVLAVQA LSRLNRAAPK WGKKTEDLFI
     LDFFNSVDDI KTAFDPFYTA TRLSEATDVN VLHELKDALD EVAVYEWFEI EQFVELYFGN
     ADAQQLSPII DTAADRFNQE LALDELAKAD FKIKAKQFVK IYGQMAAIMP FEIAAWEKLF
     WFLKFLIPKL IVKDPSADRI DELLESVDLS SYGLERIKLN HGIGLDASES ELEPSNSNPR
     GTHGGGGERD PLDEIIRSFN ERWFQGWGAT PEAQRIKFIN IADGIKAHPD FQEKYQNNPD
     VHTRLLAFEK IFEDVILKNR RNELELYKLL ANDPAFKAAM QQSLRQMVA
//
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