ID   I3Z190_BELBD            Unreviewed;      1007 AA.
AC   I3Z190;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   OrderedLocusNames=Belba_0345 {ECO:0000313|EMBL:AFL83008.1};
OS   Belliella baltica (strain DSM 15883 / CIP 108006 / LMG 21964 / BA134).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Belliella.
OX   NCBI_TaxID=866536 {ECO:0000313|EMBL:AFL83008.1, ECO:0000313|Proteomes:UP000006050};
RN   [1] {ECO:0000313|Proteomes:UP000006050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15883 / CIP 108006 / LMG 21964 / BA134
RC   {ECO:0000313|Proteomes:UP000006050};
RA   Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA   Mikhailova N., Davenport K., Kyrpides N., Mavromatis K., Pagani I.,
RA   Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Belliella baltica DSM 15883.";
RL   Submitted (JUN-2012) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003281; AFL83008.1; -; Genomic_DNA.
DR   RefSeq; WP_014771023.1; NC_018010.1.
DR   AlphaFoldDB; I3Z190; -.
DR   STRING; 866536.Belba_0345; -.
DR   REBASE; 49040; Bba15883ORF350P.
DR   KEGG; bbd:Belba_0345; -.
DR   PATRIC; fig|866536.3.peg.360; -.
DR   eggNOG; COG0610; Bacteria.
DR   HOGENOM; CLU_010804_0_0_10; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000006050; Chromosome.
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   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; IPR040980; SWI2_SNF2.
DR   PANTHER; PTHR42927; HELICASE SUPERFAMILY 1 AND 2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR42927:SF1; HELICASE SUPERFAMILY 1 AND 2 DOMAIN-CONTAINING PROTEIN; 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   Helicase {ECO:0000313|EMBL:AFL83008.1};
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:UP000006050};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          296..509
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1007 AA;  114926 MW;  B9ED097FFD2F81D0 CRC64;
     MTTDTTEKGL ETHIAQYLVN DNGYLLRENT AYDNVACLDS ALLFEFLEAT QPKSVAKLKT
     YHKDLYEQKI IKRLNDQIQA KGVIEVLRKG ITDGFTDTKL HLFYDKPVSN YNVSASILYQ
     ANSFSVMRQV YFSPQNKKSL DLMLFINGIP IISFELKNEL TKQNVQHAIK QYKTDRDPNE
     ELFRLGRLMV NFAVDTEEVW MCTQLKKEKS YFLPFNKGYN NGAGNPPNGG IKTDYLWKEV
     LTKSSLTDVI QNFCQLITEE KEYLDEKGKV RTRKEKKLIF PRYHQLVAVR NLLADAQEKG
     SGQKYLIQHS AGSGKSNSIS WLAHQLVGLH DKSGQNNIFD TVIVVTDRRV LDAQIRENIK
     QYQQVKGVVE AITEGSKQLK QALEEGKKII ITTIQKFPHI VEDIGDLPGN NFAIIIDEAH
     SSLSGQMARK LNETLSSSVQ TGHALSQHLK EEEEFKTEDG DTLTGEDLIA ELIKSRKLLP
     NASYFAFTAT PKNKTLELFG VPYQDDGKTK FRAFHLYSMK QAIEEGFIMD VLQNYTTYQS
     YYALLKKIED DPEYDKLKAQ KKLKHYVESH EHAIKKKAIL IIEHFMENVI RKKRIGGFAK
     AMLVTSSRAN AVKYKKAFDD YLLKINSPFL SVVAFSGEID GQTEASLNGF SSANIPSEFK
     KNEYRFLLVA NKFQTGFDQP LLHTMYVDKK LGGVNAVQTL SRLNRSHPLK KDTFVLDFAN
     SAEDIENAFK PYFESTILGE ATDPNKLFDL QDALDNFQVY TNDQVYEFSE KILANVPVDQ
     LHAMLDTSTE IFRKDLSEEQ QADFRAKVKT YVRLYIFLSQ IVPFENPYLE RLYIFLNHLQ
     SKLGGDTPID LAQGILDNID MDSYRLQLEA TTSIVMEQGQ DLNPIPTDMR GGSSDAEKDR
     LSNILKTFND RYGTQFEDAD KVRQMAENIA TDVAKNKELI SSIQHSDDQN ARITSDKVVG
     EELLKHITTN FDLYKLYSDN KEFKEDFTAM MFGVVKELIN RGINAQK
//