ID   A0A0F5AQ79_9GAMM        Unreviewed;      1082 AA.
AC   A0A0F5AQ79;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=WN56_11665 {ECO:0000313|EMBL:KKA44348.1};
OS   Salinivibrio sp. KP-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Salinivibrio.
OX   NCBI_TaxID=1406902 {ECO:0000313|EMBL:KKA44348.1, ECO:0000313|Proteomes:UP000033449};
RN   [1] {ECO:0000313|EMBL:KKA44348.1, ECO:0000313|Proteomes:UP000033449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KP-1 {ECO:0000313|EMBL:KKA44348.1,
RC   ECO:0000313|Proteomes:UP000033449};
RA   Kaur G., Kumar A., Mathan Kumar R., Kumar N., Singh N.K., Arora A.,
RA   Kaur N., Bala M., Mayilraj S.;
RT   "Taxonomic description and genome sequence of Salinivibrio halophilus sp.
RT   nov., a novel halotolerant gammaproteobacterium isolated from marine
RT   sediment and emended description of the genus Salinivibrio.";
RL   Submitted (MAR-2015) 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:KKA44348.1}.
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; LAQR01000041; KKA44348.1; -; Genomic_DNA.
DR   RefSeq; WP_046075165.1; NZ_LAQR01000041.1.
DR   AlphaFoldDB; A0A0F5AQ79; -.
DR   PATRIC; fig|1406902.3.peg.2318; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000033449; 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   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.
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:KKA44348.1};
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:UP000033449};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          306..541
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|SMART:SM00487"
SQ   SEQUENCE   1082 AA;  123832 MW;  019D7D6FD9C556DD CRC64;
     MKDTTQERIF QDDIIRQMVA NGWVQGTGEG YNRESALYEA DVLSFIKKTQ PKEWEKFCKV
     FPTDSERHFL DALVTQLKKA DENATDRASR TFGTLGVLRH GLKIRNARFE LCQFKPEHNL
     NPETLARYQQ NICRIVPELV YSPYATQAEF EATGKQAKKW RIDLVLFVNG LPVSTLELKS
     EFKQAVENAI AQYKLTRLPK DPATKKPEPL LSFKRGALVH FAVSQYEVYM ATKLAGTDTF
     FLPFNKGTHD GGKGNDIPED ENRYATDYLW NDVLTPDNLL NIIGRFIHLQ IEEKEDWEGR
     KTKKETLIFP RYHQWDVVTK LVNAAIEEGT GNKYLIQHSA GSGKSNSIAW TAHQLSTLHD
     TKGNKQFDSV IVVTDRTVLD DQLQDTIYQF EHADGVVGRI NRKEGDGSKS EKLASALETS
     QPIIIVTIQT FPHVLKAIEN STSLKARRYA VIADEAHSSQ TGATARQLKE VLMTDEVDDD
     TELSSEDILD ATVAARRGSA NLSYYAFTAT PKQKTLALFG RRPDPEQPAS KRNLPVAYHI
     YSMRQAIEEG FILDVLKNYT NYKVIYQLKQ KLEAEDKEVD AGKAKVKLNN WVRLHDHNIS
     QKVKVIIEHF KKNVMGLLGG QAKAMVVTSS RKEAVRYKLA FDKYVYEHGY AGIRAMVAFS
     GEVEFNASDP DSTAFMDQKF TEHSMNPDLK GREMRKAFNT DDYQVMLVAN KFQTGFDQPK
     LCAMYVDKKL AGVECVQTLS RLNRIYPGKA ECGTFVLDFY NEPQDILDAF QPYYQVAELE
     DVTDPDKIFD LSEKLRASGI FLWSEVEQFI DAFFTKNKSN AAISNICKPA IDRWRKRYTS
     AVDEYIHAKN VFERTKKTGD AVLIANAENA FKESKQEKDR LEIFKKDLGS FVRFYEFMSQ
     IVDYDDKELE KLSLYARHLR PMLREKVIEE DELDLGDVVM SHYRLSKIRQ QDIQLQENTP
     EYKLHPSNDV GTAKPKDKKE EFLSHIIERL NEVFLTDNLT DKDMINYAFT VRDKLTENET
     VMSQIANNTR EQAMLGDFPR AIDDAILNSN EAHQEQMMQL LSDPNKTKQF ARVIFDMLSG
     VK
//