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Database: UniProt
Entry: A0A426JGW0_9FLAO
LinkDB: A0A426JGW0_9FLAO
Original site: A0A426JGW0_9FLAO 
ID   A0A426JGW0_9FLAO        Unreviewed;       937 AA.
AC   A0A426JGW0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   22-FEB-2023, entry version 11.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=EIG84_12305 {ECO:0000313|EMBL:RRO12361.1};
OS   Flavobacteriaceae bacterium 14752.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=2491711 {ECO:0000313|EMBL:RRO12361.1, ECO:0000313|Proteomes:UP000274596};
RN   [1] {ECO:0000313|EMBL:RRO12361.1, ECO:0000313|Proteomes:UP000274596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=14752 {ECO:0000313|EMBL:RRO12361.1,
RC   ECO:0000313|Proteomes:UP000274596};
RA   Yu Y.;
RT   "Wangjiella luteus gen. nov., sp. nov., a novel bacterium of the family
RT   Flavobacteriaceae isolated from a saline lake.";
RL   Submitted (NOV-2018) 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:RRO12361.1}.
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DR   EMBL; RRZV01000095; RRO12361.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A426JGW0; -.
DR   OrthoDB; 9759819at2; -.
DR   Proteomes; UP000274596; 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:0004386; F:helicase activity; 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; 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; PF04313; HSDR_N; 1.
DR   Pfam; PF04851; ResIII; 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   Helicase {ECO:0000313|EMBL:RRO12361.1};
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          175..370
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   937 AA;  108564 MW;  DD4B3D59B662968E CRC64;
     MPADINQNPE QIARDKIDKM LLEAGWEVQS KSKVDLNAKK GVAVREYQTD VGPADYVLFV
     DKKPVGIIEA KREDEGHRLT VVEDQSTNYA NAKLKYLNND PLPFVYESTG TITRFTDYRD
     PKPRGRTVFW FHKPETIAKW LKKGKSLRER LLSMPDLNEM GLRPAQIVAI NNLEHSFKKN
     RPKALIQMAT GAGKTFTAAT FVYRLLKHAD AKRILFLVDT KNLGEQAEQE FMTFQPNDDN
     RKFTELYNVQ RLTSSYIASD SQVSISTIQR LYSILKGEEL EESAEQDNPN ESSWLKSKMS
     EKKAIPVEYT PRVPIEQFDF IVIDEAHRSI YNLWKQVLDY FDAFLIGLTA TPDKRTFGFF
     NENVVSQYTY EESVTDGVNV PYDVYTIETE ISQKGETVKA GWFVDRRDKL TRKKRWQQED
     EDTEYKRNDL DKKVVNPSQI RNIIREYKRA LKTTIFPNRS DENGDYEVPK TLVFAKTDSH
     ADDIIKIIRE EFDEGNDFCK KVTYKIEEDP KSVLNRFRNS YHPRIAVTVD MIATGTDVKP
     LEVLLFMRDV KSVNYFEQMK GRGTRTINKD SLQLVSRTAN SKTHFVIVDA VGATKSKKTD
     SRPLERKPSV AMKDLLGAIT MGVAEEDLFM SLANRLIRLE KQITDKEKDK ILEFSKGKNL
     KQITKELITA FDKDAINDKA QPEIDKIPIE DRTPALVEET KKKAQEELIN EASKTFNGEF
     NDYLENVRKE HDQIIDSINI DTVIKSEWDT NSVDKAKAIV KDFNEYLEAN KDEIKALSIF
     YNQPYNRREI TFKMIKEVME KMKLEKPLLA PDYVWDAYTQ LEEVKSKQPK DELTALVSLI
     RRACGIDTKL VAFDKTIDEN FKNWIFKQNA GKHNRFDKEQ MQWLRMVKDH IVSSYHLELE
     DLDYTPFDNQ GGRGKMYQLF GNEMDNVIKE LNEVLVA
//
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