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
//