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Database: UniProt
Entry: A0A0E3NX75_9EURY
LinkDB: A0A0E3NX75_9EURY
Original site: A0A0E3NX75_9EURY 
ID   A0A0E3NX75_9EURY        Unreviewed;       777 AA.
AC   A0A0E3NX75;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=MSMTP_1975 {ECO:0000313|EMBL:AKB25444.1};
OS   Methanosarcina sp. MTP4.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=1434100 {ECO:0000313|EMBL:AKB25444.1, ECO:0000313|Proteomes:UP000033049};
RN   [1] {ECO:0000313|EMBL:AKB25444.1, ECO:0000313|Proteomes:UP000033049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MTP4 {ECO:0000313|EMBL:AKB25444.1,
RC   ECO:0000313|Proteomes:UP000033049};
RA   Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA   Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT   "Methanogenic archaea and the global carbon cycle.";
RL   Submitted (JUL-2014) 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; CP009505; AKB25444.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E3NX75; -.
DR   STRING; 1434100.MSMTP_1975; -.
DR   REBASE; 109005; MspMTP4ORF1976P.
DR   KEGG; metm:MSMTP_1975; -.
DR   PATRIC; fig|1434100.4.peg.2639; -.
DR   HOGENOM; CLU_018958_0_0_2; -.
DR   OrthoDB; 11644at2157; -.
DR   Proteomes; UP000033049; 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:UniProtKB-EC.
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, ECO:0000313|EMBL:AKB25444.1};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033049};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          195..355
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   777 AA;  89627 MW;  ADCB492CF8488BA8 CRC64;
     MVQERGKKPE EEARENIDKK ELSERDICTK FITPALRNAK WDIRTQIREE VKLTDGRVIV
     KGNSSGRGKP KWADYILYHK PNLPLAVIEA KNNRHSVGDG MQQALMYAEM LDIPFAFSSN
     GDAFLVHDRT GTLGQVEEEI PLEKFPSPEF LWEKYCEWKG FDEGKQKVVT QDYYSGSGGK
     TPRYYQRIAI NRTVEAIAKG QDRILLVMAT GTGKTFTAFQ IIWRLWKGGV KQRILYLADR
     NILVDQTKIN DFKPFEKAMT KIKNRKVDTA YEIYLSLYQA VTGSEEEKNI YKQFSPDFFD
     LVIVDECHRG SAAEDSAWRE ILDYFSSATQ IGLTATPKET KEISNTDYFG KPIYTYSLKQ
     GIEDGFLAPY RVVRIDLDKD LEGWRPEKEK TDRYGRLIED RIYGQKDYDR GLVLEKRTEL
     VARKVTEFLK ENDRFDKTIV FCENIDHAER MRRALVNENS DLAAENRRYV MRITGDNPEA
     KIELDDFITP ESRYPVIATT SKLMSTGVDA QTCKLIVLDK RIQSMTEFKQ IIGRGTRIQE
     DYGKFYFTIM DFKKATELFA DPDFDGDPVQ VYDPEDGPFR GRGPLEGDGS EKYFVGDVEV
     NVIAERRQYF GPDGKLITES LKDYTRKTVL EDFESLDSFL QHWNEAEKKQ AILAELEEQG
     LLLDALSEEV GKDFDPFDLI CHVAFDRPPL SRKERAEKVR KSDYFSKYGE QAKEVLSALL
     NKYADEGLEN LESMKVLKVR PFDRIGSQLE IMRMFGGKKS YLDAVRGLEN QLYSVEV
//
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