ID   A0A369QPL5_9RHOB        Unreviewed;      1023 AA.
AC   A0A369QPL5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=DLJ49_20035 {ECO:0000313|EMBL:RDC68482.1};
OS   Rhodovulum sp. 12E13.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodovulum.
OX   NCBI_TaxID=2203891 {ECO:0000313|EMBL:RDC68482.1, ECO:0000313|Proteomes:UP000253860};
RN   [1] {ECO:0000313|EMBL:RDC68482.1, ECO:0000313|Proteomes:UP000253860}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12E13 {ECO:0000313|EMBL:RDC68482.1,
RC   ECO:0000313|Proteomes:UP000253860};
RA   Zhang R.;
RT   "Rhodovulum sp. nov.,isolated from saltern sediment.";
RL   Submitted (JUL-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:RDC68482.1}.
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DR   EMBL; QPLK01000050; RDC68482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369QPL5; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000253860; 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   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, ECO:0000313|EMBL:RDC68482.1};
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:UP000253860};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          302..502
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1023 AA;  115537 MW;  3E6729FEA65C5112 CRC64;
     MPGHTERDFE TAIEAGLTGA GGYETRPPSD FDEARALFPA DVTGFLRDSQ PTRWSQLEAL
     LGDKTEATVL DSLGKELDVK GALHVLRYGF KCYGKTFRLA YFRPNTGMNP EAAALYARNR
     LTITRQVAFT SVLKRADGKN RRCIIDVTLS INGMPVVTAE LKNPQTGQRA ADAIRQYSDE
     RDERDLLFTF KKRALVHFAV DPDEVWMTTR LKGRETVFLP FNRGHDHGAG NPPVEGNWKT
     HYLWDEVLQA DSLLDILHRF MHLEVKEKQV RTEKGVRTVR KETMIFPRYH QLDAVRKLVA
     HAGTHGAGRN YLVQHSAGSG KSNSIAWLAH RLASLHDAQD EKVFHSVVVV TDRRVLDQQL
     QATIYQFEHK TGVVEKIDED TRQLARALSQ GTPIVITTIQ KFPFISQALS TLQSKGEGVK
     IDTAGKRFAV IVDEAHSSQS GETATALKGM LNKDGIESAI AAQLSDEEDD DLSDDAKAAM
     LRDSLKRARQ PNLSFFAFTA TPKFKTKMLF DEPGLSGAAP FHEYSMRQAI EEGFIMDVLK
     NYTTYKRFYG LIKQVETDPE VPRKKAAKAL TRYLELHPVN IEQVVSVIVE HFRLYVMHEL
     GGRAKAMVVT GSRLAAVKYK LAFDRYVKQQ GYDGIRSLVA FSGTVEDPDD PGSSYTEVSM
     NDGLAESELP EAFERDDYRV LLVADKYQTG FDQPLLQTMY VVKRLAGVQA VQTLSRLNRV
     APGKTRTFVL DFANEEDDIY KAFKPYYETT PVGKNADPHR LSELQHKLLQ WAIFTPDDVN
     AFAEVWYRGK RDHSASDHRA MNAVLDAVVE RFLDKDETEQ EEFRGQLAAY RSLYAFLSQI
     IPYQDSDLEK LYAFVRNLIS KLPPPGDGQG FALDDEIALR YFRLQQMTEG SIDLSDGEAD
     PLKGPTDVGT ARVPDEEVAL SNLIEKLNER FGTDFTEADQ LFFDQIRASA EQDDKIVEAA
     RANNLANFSS FLERMLDELF IDRMEGNEEI FSRVMTDKEF RAAAHEHLAR EIFRRAKQQD
     VVE
//