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}.
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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
//