ID   X6P928_RETFI            Unreviewed;       984 AA.
AC   X6P928;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, 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};
GN   ORFNames=RFI_02524 {ECO:0000313|EMBL:ETO34569.1};
OS   Reticulomyxa filosa.
OC   Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC   Reticulomyxidae; Reticulomyxa.
OX   NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO34569.1, ECO:0000313|Proteomes:UP000023152};
RN   [1] {ECO:0000313|EMBL:ETO34569.1, ECO:0000313|Proteomes:UP000023152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24332546;
RA   Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA   Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA   Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT   "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL   Curr. Biol. 0:0-0(2013).
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:ETO34569.1}.
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DR   EMBL; ASPP01002456; ETO34569.1; -; Genomic_DNA.
DR   AlphaFoldDB; X6P928; -.
DR   EnsemblProtists; ETO34569; ETO34569; RFI_02524.
DR   OrthoDB; 5688857at2759; -.
DR   Proteomes; UP000023152; 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:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd22332; HsdR_N; 1.
DR   CDD; cd18800; SF2_C_EcoR124I-like; 1.
DR   Gene3D; 1.20.58.2040; -; 1.
DR   Gene3D; 3.90.1570.50; -; 2.
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; IPR022625; TypeI_RM_Rsu_C.
DR   NCBIfam; TIGR00348; hsdR; 1.
DR   PANTHER; PTHR30195:SF16; TYPE I RESTRICTION ENZYME ENDONUCLEASE SUBUNIT; 1.
DR   PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR   Pfam; PF12008; EcoR124_C; 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   Reference proteome {ECO:0000313|Proteomes:UP000023152};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          328..452
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   984 AA;  113801 MW;  D227231A61AD0F79 CRC64;
     MTCYKNIAEN PNSTVVAEYI STEVGAQKYQ SENELEVEFI RILQSNGYEY LTIRSNDDLV
     MNLRNQMSRL NNVNFSDTEW NQIFNHYLAN KNDTIEEKTT RVQEDYIYNL KRDDGSTKNI
     RILDKDNIHN NSLQVINQYE TEGARKNRYD VTVLVNGLPL IHIELKRRGV AIREAFKQIN
     RYQRDSFWAE SWLFEYVQLF VISNGTHTKY YSNTTRNAHL KEQAGKSSGK KTSNSFEFTS
     WWTDGKNKRI SDLVDFGKTF LSKHSVLSVL TRYCVFTTDK LLLVMRPYQI AAAERILNKI
     ALATNHKQLG TIDAGGVQLA SRLDKIDKVI FVVDRKDLDD QTMKEYDKFK KGAANSNTST
     AILAKQLGDA NSKIIITTIQ KLSKFIVGNK GHRVFNGHIV LIFDECHRSQ FGEMHSQITK
     AFNKYHIFGF TGTPIFAANS SSGGNPYLKT TEQAFGQKLH TYTIVDAIND ENVLPFRIDY
     INTLKMKDDI KDKKVLAIDI EAAANSPERI KQVTEYILEH FDQKTKRNER YTIKGKRLYG
     FNSIFAVSSI EVAKKYYEEF KSRNTELKIG IIYSFGANET ESDEGILPDE DFDTTGLDKS
     SHDFLDNAIT DYNKNFGTSF DTSSQKFENY YKALSDRIKN REIDLVIVVN MFLTGFDATT
     LNTLWIDKNL RHHGLLQAFS RTNRILNSVK IFGNIVCFRD LEQATNDALS IFGNKEASGI
     VLLKSYNDYY NGWKKDGTHQ RGYIELISEL QERFPLPIFF EGEQAEKDFI KLWGAILRLR
     NILLSFDEFK GNEILNERDF QDYQSVYLDL YEKIRKRREA DKENINDDIV FEIELVKQVT
     INIDFILQMV AKYHKSLMKD KEILITIEKA MNSSIELRSK KELIEGFINT LNANTDVDKD
     WCIFTDESKA EELERIITEE NLKPKETRRF IANAFRDGEL KSNGTAFANI IPPVLMFDKD
     KSRAKKKSNA LEKLQKFFEK FFGL
//