ID   J0SB81_9EURY            Unreviewed;      1030 AA.
AC   J0SB81;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=Metli_2033 {ECO:0000313|EMBL:EJG07974.1};
OS   Methanofollis liminatans DSM 4140.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanofollis.
OX   NCBI_TaxID=28892 {ECO:0000313|EMBL:EJG07974.1};
RN   [1] {ECO:0000313|EMBL:EJG07974.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4140 {ECO:0000313|EMBL:EJG07974.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Lu M., Detter J.C.,
RA   Tapia R., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Spring S., Schuler E., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanofollis liminatans DSM 4140.";
RL   Submitted (AUG-2011) 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; CM001555; EJG07974.1; -; Genomic_DNA.
DR   RefSeq; WP_004040073.1; NZ_CM001555.1.
DR   AlphaFoldDB; J0SB81; -.
DR   STRING; 28892.Metli_2033; -.
DR   PATRIC; fig|28892.9.peg.2201; -.
DR   HOGENOM; CLU_010804_0_0_2; -.
DR   OrthoDB; 11429at2157; -.
DR   Proteomes; UP000005095; Chromosome.
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; cd22332; HsdR_N; 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   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; 2.
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, ECO:0000313|EMBL:EJG07974.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          300..520
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1030 AA;  117072 MW;  DFADC4B255B4D845 CRC64;
     MTGQTDEKAF ETYLEEILRK GGWQAGKKEE WDVERALFPQ RIVSFLQETQ PDLWAEMQGL
     HGERLEDLIL ATLVKELDTK GTLHVLRHGF KFYGKTFRLA SFKPAHGLNA ETLALYAKNQ
     LTLTRQVPCH PGRCDTVDLL FAVNGIPVAT CELKNPGTGQ TWRNAVRQYR EDRDPRAPLF
     QFKKRSLVHF AADSEQVYMT TCLENDRTNF LPFNRGSHPG QIQCGAGNPA HPSGYRTGYF
     WEDVLQRDSF LDIIGRFMFI ENKEQTVDDG HGGKKRIKKE KMVFPRYHQL DALRAIVAAA
     KKEGPGHNYL IQHSAGSGKT NSISWLSHRL ASLHNADDKK IFDCVIVITD RRILDQQLQD
     AIYQIEHAQG VVQAIDQDSK QLAAALIDGT KIVVTTLQKF PFVLHGLLTA AGAKNLEEAT
     EEEKEQAKAW QRAIAVRNYA VIVDEAHSSQ SGETSRELKA ILGAAATPGE NGDPDWEDGL
     NQVMQSRGRQ PNLSFFAFTA TPKGKTIELF GRPGADGVPE AFHLYSMRQA IEEGFILDVL
     TNYTTYATYY RLLKAIEEDP AMPRKKAARV LAKFMSLHPY NIEQKTAVIV EHFRTHVQHR
     LGGRAKAMLI TATRLNAVRY MEAFQRYIDE HGYTDIHPLV AFSGTVTDPN TGLEYTEPGM
     NIDVITGQHI SESQLPERFD SNDYQILIAA NKYQTGFDQP LLHTMYVDKR LDGVHAVQAL
     SRLNRKIPGK DEPFVLDFVN EAEDIYGAFK PYYDKTSLQE CTDPSQLEAL KFQLDQAQVY
     FWSEVAAFAR IFYKPPDQQK PSDHARMQFH LQPAVDRFKG IEDEEKKQEF RDRLCSYVRL
     YAFMSQIMPY NDPDLEMLYS YGRFLIPHLT LDQDEEIVKV SNEVELQYYR LERVFSGAID
     LREGDVPGVR APSAVGTGKA KEEKAPLSEI IEVLNERFGT QFAEGDRLFF QQIKESACSD
     DRVIQTALAN PLDKFELGIR RLIEEIMIDR MADNDKIVTR YMSDQEFQGS AFPILAKEIF
     DAVRKEAADE
//