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Database: UniProt
Entry: A0A139CR60_9EURY
LinkDB: A0A139CR60_9EURY
Original site: A0A139CR60_9EURY 
ID   A0A139CR60_9EURY        Unreviewed;       804 AA.
AC   A0A139CR60;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
DE   Flags: Fragment;
GN   ORFNames=AWU59_972 {ECO:0000313|EMBL:KXS43717.1};
OS   Methanolobus sp. T82-4.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanolobus.
OX   NCBI_TaxID=1794908 {ECO:0000313|EMBL:KXS43717.1, ECO:0000313|Proteomes:UP000074030};
RN   [1] {ECO:0000313|EMBL:KXS43717.1, ECO:0000313|Proteomes:UP000074030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T82-4 {ECO:0000313|EMBL:KXS43717.1};
RA   Wolfe R., Daly R., Wrighton K.;
RT   "Methanolobus T82 Annotated.";
RL   Submitted (FEB-2016) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXS43717.1}.
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DR   EMBL; LSRV01000022; KXS43717.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139CR60; -.
DR   STRING; 1794908.AWU59_972; -.
DR   PATRIC; fig|1794908.3.peg.2414; -.
DR   Proteomes; UP000074030; Unassembled WGS sequence.
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   InterPro; IPR021810; T1RH-like_C.
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   Pfam; PF11867; T1RH-like_C; 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};
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          292..474
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   NON_TER         804
FT                   /evidence="ECO:0000313|EMBL:KXS43717.1"
SQ   SEQUENCE   804 AA;  91736 MW;  EBA9F070F3960446 CRC64;
     MSCIVSESEV EEAALEILTE LGYGYFYGPD IAPETPDSQR VTYSDVFLIE RLRAAIATLN
     PHIPSPAREE ALKKVVRTES QDLIHSNQVF HNMLVNGVDV EYRNNEGEVV YDKVWLFDFK
     EYSNNEYIAV NQFTVVENRN NRRPDIVLFI NGLPLVVMEL KRPEDDSEYE DDDLIWTAYN
     QFQTYKDEIP SLFRYNAFLI ISDGQEARAG TITSSRQWFT SWKTIDGENT ADFLIPEMEV
     LLKGMCNKDV ILDLVQNFMV FEGDHGPIIK KLARYHQYHA VNKAVQNTIE ASRPDGDRRC
     GVIWHTQGSG KSLSMIFYAG KLVVDMDNPT IVVITDRNDL DGQLFESFAR CSSLLRQHPV
     QANTGAELRD LLSVASGGIV FTTIQKFLPE NSEDSFPALT ERSNVIVIAD EAHRSQYGLE
     MKMSQKDDEA RFSYGFAKHM RDALPNASFI GFTGTPIEFD DRNTPAIFGD YIDIYDIEQA
     VKDGVTVKIF YENRLSRIDI VAEARNTLDT QFALLTEDRE EYESEKLKSR WSRLDAVVGS
     KSNLKKLAAD IIPHFESRVA TPEGKGMIVC MNRRTCVDLY NEIIALRPNW HDDDDLKGAV
     KVIITGSAAD EKSMQPHIRS KSKRMKIRDR MQDPDDPLKI VIVCDMWLTG FDAPCLHTMY
     FIKWLKGHTL MQAIARVNRV FKDKPGGLIV DYVGLLYDLK YAMANYTRSG GRGKPADLKD
     EAVDLMLEKY EIVRDMFHGF NYRRILTASP KEKLTIVREG ADFILSLGRT EQQSKHERKR
     FIQHVTELSK AFALSKPHAQ ADLI
//
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