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Database: UniProt
Entry: A0A1Q8J476_9BURK
LinkDB: A0A1Q8J476_9BURK
Original site: A0A1Q8J476_9BURK 
ID   A0A1Q8J476_9BURK        Unreviewed;      1096 AA.
AC   A0A1Q8J476;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=BTH42_00235 {ECO:0000313|EMBL:OLL33743.1};
OS   Burkholderia sp. SRS-W-2-2016.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1926878 {ECO:0000313|EMBL:OLL33743.1, ECO:0000313|Proteomes:UP000186182};
RN   [1] {ECO:0000313|Proteomes:UP000186182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRS-W-2-2016 {ECO:0000313|Proteomes:UP000186182};
RA   Chauhan A.;
RL   Submitted (DEC-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:OLL33743.1}.
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DR   EMBL; MSDV01000001; OLL33743.1; -; Genomic_DNA.
DR   RefSeq; WP_075294720.1; NZ_MSDV01000001.1.
DR   AlphaFoldDB; A0A1Q8J476; -.
DR   STRING; 1926878.BTH42_00235; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000186182; 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; 3.90.1570.50; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR   InterPro; IPR040980; SWI2_SNF2.
DR   InterPro; IPR021810; T1RH-like_C.
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   Reference proteome {ECO:0000313|Proteomes:UP000186182};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          278..506
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1096 AA;  123237 MW;  987657A8FC0EDD73 CRC64;
     MGNAEKTGVE IPAIDWLVKL GYIHLPGGQV AVEHRHLAPV LENVLKPRLQ MLNPWLAFAP
     GGVDAALIEL RKRVNDELLP ANKAFWEQAV HRSDIQVKDA EGKPRSVRFF DASKSTNNDF
     HVVDQYVGRN ADDDVFRPDL LLFVNGLPMA IIECKASHHR LDEALAQLDG YRATFSAQFV
     FNQVSVGLNG RQGLYGSIFT PPAFYAHYRL QDAERAEVTA LLADEPSEQD ELLWALFEPA
     RFLELITHYV LFETRDGKTV KKLPRYQQWR AVRKTVQRLT APKPLGGVVW HTQGSGKSLT
     MALLARLLRA ESTGLDNPTV LVLTDRRDLD KQIFDTFHAV GIKAIQAVSV DGLVKMLSND
     YGSVFTSTVQ KFQEKDETDA DAEASAEPSE YEDDTIQATR HRRVRDGKNF FMVEERNVNF
     GQYDADGALL SPKWEEVHRE KVNFRVLSTK PNFYVLVDEA HRSQYDFLAA FMRASLPKAK
     FIAFTGTPLQ NDDKHTLAEF GGGEYIDEYR LHEAVADGAT LPIKYQDAWV ALAPDVGLDQ
     AFKGQFISEP EARQHALKKA LLTRWRQAGD RMEKVAHHLV EHFLNNVQAK GLKGMLVCDG
     REMAVRYKDL LDAIMKDRGE QGLPTFESRV VVSLANITAS RTGASEKEAA AEKGVSADKV
     RTIEERVRGE IKAGKVPVAM PTEQIANFVS KLFPLPYGDE VKGKDGKVHA NNVGLIIVSD
     MLLTGWDAPI VGTMYLDKPL KEHTLLQAIA RVNRTLAGKN AGYIVDYHGV VEHLDHALKI
     YGGDVKPAQV WEGVESELPK LQATLERILK LLPRKHDPVS QREDYKADAE TFLDPAARLD
     KVEDFLELVK QFNRSIDIIL PDVRGVEFKP YFTLFAEIRL MLRDKLPGTA YRERITKLES
     VLLQQLLDEH ISASPAKSLL GKEVSILDAS DMDRLKKLAS PGSRALVMKN QLKHTIETGR
     DKDPVFFDKL AEEMEKLLEE EKAGRITQAK FLEQLDLFGQ RIKEKDNTGF SSPAHSAAFH
     YLESHLSSDM ARGVTTKLFE DEELRHTMAS GHWKAMHDLH PEIKRRISSL LVPLAGWQRA
     VARDHASHLL TILLKN
//
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