ID Q8PUP0_METMA Unreviewed; 1042 AA.
AC Q8PUP0;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 131.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN OrderedLocusNames=MM_2292 {ECO:0000313|EMBL:AAM31988.1};
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952 {ECO:0000313|EMBL:AAM31988.1, ECO:0000313|Proteomes:UP000000595};
RN [1] {ECO:0000313|EMBL:AAM31988.1, ECO:0000313|Proteomes:UP000000595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88
RC {ECO:0000313|Proteomes:UP000000595};
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baumer S., Jacobi C.,
RA Bruggemann H., Lienard T., Christmann A., Bomeke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.P., Gunsalus R.P.,
RA Fritz H.J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM31988.1; -; Genomic_DNA.
DR RefSeq; WP_011034217.1; NC_003901.1.
DR AlphaFoldDB; Q8PUP0; -.
DR REBASE; 6261; MmaGORF2294P.
DR GeneID; 1480634; -.
DR KEGG; mma:MM_2292; -.
DR PATRIC; fig|192952.21.peg.2626; -.
DR eggNOG; arCOG00878; Archaea.
DR HOGENOM; CLU_005762_0_1_2; -.
DR Proteomes; UP000000595; Chromosome.
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:InterPro.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR CDD; cd18030; DEXHc_RE_I_HsdR; 1.
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; IPR004473; Restrct_endonuc_typeI_HsdR.
DR InterPro; IPR040980; SWI2_SNF2.
DR NCBIfam; TIGR00348; hsdR; 1.
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 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 Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 261..431
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1042 AA; 118819 MW; E04CC8EAE287262E CRC64;
MNIGKPERAT QDRIISLFHD ELGYSYLGNW IDREGNSNIE EELLAAYLTK NGYTRIQIGV
ALHLLKNAAN RHNQSLYSNN QAVYSLLRYG VPVKTEAGKV TDSVQLINWQ EPEKNDFAIA
EEVTLRGKRE RRPDIVLYVN GIAVGVLELK NSRVTIEDGI RQNLSNQQPE FNEWFFSTVQ
FIFAGNDSEG LRYGAIGTQE KYFLTWKEDE EDNSRFKLDK YLLKMCSKNR LIELMHDFVL
FDGGIKKLPR FHQYFAIKAA QKHVRQHRGG IIWHTQGSGK SIVMVLLAKW ILENNPNARV
VIVTDRDELD KQIEGIFNDA GETIKRTTSG RELMSQLSQA KPRLLCSLVH KFGRKSANDF
DAFIKDLESQ PSKTVGEVFV FVDECHRTQS GKLHRAMKAI MPNAVFIGFT GTPLLKKDKQ
TSLEVFGGYI HTYKFSEAVE DKVVLDLVYE ARDIDQRLGS EQKIDAWFEA KTKGLNDWQK
DELKKHWGTM QKLLSSRSRM DRVVNDIIFD FSVKPRLSSE RGNAILVASS IYEACKYFTL
FQKTPFKGKC AVVTSYNPQA QDVTKEDTGA NTETEKEFVY STYTELLKNI ETTPGMTKTE
TYEEKAKSLF IKEPANMKLL IVVDKLLTGF DAPPCTYLYI DKSMQDHGLF QAICRTNRLD
GEDKDFGYIV DYKDLFKNLV NDRGTGALQV YSSELDRSAG GVDPDVLMQD RLKKGRERLD
NALEALALLC EPVEPPKGEL EYIHYFCGNT EIPTDLQEHE TQRAALYKAT ASLVRAYANI
SDELESAGYS SSDTARIKQL LEHYLNIREI IRKASGESLD LKAYEADMRH LIDTYIEASE
PRKVSSFEDM PLLELIVKTG IDKAIVTQLG GLKGNRNAVA ETIENNVRSK IIKEHLNDPA
YYEKMSALLD EIIAARKAKA IEYEEYLKRI ADLVKQVEAG HEDDISEVLK KSPALRALYN
NLQNQGGYSE DLAKESDEYV TPHDKVLALA LRLDETVKRV RSDDWRGIEP RERVIKKAIH
DVLNDVDEVE RIFLIIKAQK EY
//
