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Database: UniProt
Entry: A0A2K8U5L7_9GAMM
LinkDB: A0A2K8U5L7_9GAMM
Original site: A0A2K8U5L7_9GAMM 
ID   A0A2K8U5L7_9GAMM        Unreviewed;       926 AA.
AC   A0A2K8U5L7;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=THSYN_07860 {ECO:0000313|EMBL:AUB80873.1};
OS   Candidatus Thiodictyon syntrophicum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiodictyon.
OX   NCBI_TaxID=1166950 {ECO:0000313|EMBL:AUB80873.1, ECO:0000313|Proteomes:UP000232638};
RN   [1] {ECO:0000313|EMBL:AUB80873.1, ECO:0000313|Proteomes:UP000232638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cad16T {ECO:0000313|EMBL:AUB80873.1,
RC   ECO:0000313|Proteomes:UP000232638};
RA   Luedin S.M., Pothier J.F., Danza F., Storelli N., Wittwer M., Tonolla M.;
RT   "Complete genome sequence of Candidatus 'Thiodictyon syntrophicum' sp. nov.
RT   strain Cad16T, a photolithoautotroph purple sulfur bacterium isolated from
RT   an alpine meromictic lake.";
RL   Submitted (MAR-2017) 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}.
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DR   EMBL; CP020370; AUB80873.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K8U5L7; -.
DR   REBASE; 226608; Tsy16TORF7880P.
DR   KEGG; tsy:THSYN_07860; -.
DR   OrthoDB; 9804086at2; -.
DR   Proteomes; UP000232638; Chromosome.
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; cd18032; DEXHc_RE_I_III_res; 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; IPR001650; Helicase_C.
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; PF00271; Helicase_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; 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:AUB80873.1};
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:UP000232638};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          171..361
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   926 AA;  104408 MW;  3455EBADA269BC89 CRC64;
     MTPEAKARQD IEQRLIEAGW VIQDYQDIDL GAARGVAVRE YPTATGPADY VLFIDRAPVG
     IIEAKRAESG ENITVAEDQT LRYATAPLKW RGLMTPLPFL FESTGAIIRF TDARDPAPRS
     REVFHFFRPE QLAHWLAAPD TLRRRLASTL PALPTARLRE CQVAAVGGLE RSLAHNRPRA
     LAHMATGSGK TFTAITAVYR LLKFARARRI LFLVDTRNLG TQAHQEFMAY TPPDDARKFT
     ELYNVQRLSS STIDPQAQVV ISTIQRLYSV LSGEPLDASA EDISLNELQQ MPQQAKRVRY
     NAAVPIETFD FIIIDECHRS IYNVWKQVLD YFDAFLIGLT ATPDKRTFGF FNENIVAEYT
     YEQSVADGVN VGYDVYEIET EVTKKGAELK AKEWVDHRER QTRKRRWAQT EEDQAYTGKE
     LDRSVVNPSQ IRRVIEAMKT AVETQIFPNR KETPKTLIFA KTDSHADDII QCLREVYAQG
     NAFCKKVTYK AEDDPDSTLA SFRNDHYPRI AVTVDMIATG TDVKPLEILL FMRDVRSRGY
     YEQMKGRGVR SLDCDGLKRV SNSADSAKTR FVLIDAVGVE RSLKTDSRPL ERKPGIPLKD
     LLQGVAIGHR DDDTLLSLAN RLVRLAKQLD DKARARVETV SGGVSVADLG KGLIAALNPD
     RIIEDALATA EARGITRSED TLTAGEIAAA RAARVAAACT PFDRPELREA IESARREHEQ
     LIDHINLDQV TFAGYGEQAE AQARKAIQGF ADYIAQHKDE IAALAFFYQQ PYQRRALTFE
     MIEELHDRLG RPPLMLTTER LWSAYARVKT SQVKGADARR QLTDLIALVR FAIGLDSELR
     PFREQVDKRF QEWIFRHNAQ RATAFTPEQT DWLRLMKEHI AASCSIGRGD FDYAEFADKG
     GLQKVWGVFG PALDGLMDEM NRELVA
//
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