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Database: UniProt
Entry: A0A1H9CPP7_9GAMM
LinkDB: A0A1H9CPP7_9GAMM
Original site: A0A1H9CPP7_9GAMM 
ID   A0A1H9CPP7_9GAMM        Unreviewed;      1121 AA.
AC   A0A1H9CPP7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=SAMN05421693_11472 {ECO:0000313|EMBL:SEQ03192.1};
OS   Ectothiorhodospira magna.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Ectothiorhodospira.
OX   NCBI_TaxID=867345 {ECO:0000313|EMBL:SEQ03192.1, ECO:0000313|Proteomes:UP000199496};
RN   [1] {ECO:0000313|EMBL:SEQ03192.1, ECO:0000313|Proteomes:UP000199496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B7-7 {ECO:0000313|EMBL:SEQ03192.1,
RC   ECO:0000313|Proteomes:UP000199496};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOFO01000014; SEQ03192.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9CPP7; -.
DR   STRING; 867345.SAMN05421693_11472; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000199496; 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; cd18030; DEXHc_RE_I_HsdR; 1.
DR   CDD; cd22332; HsdR_N; 1.
DR   CDD; cd18800; SF2_C_EcoR124I-like; 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; PTHR30195:SF15; TYPE I RESTRICTION ENZYME HINDVIIP R PROTEIN-RELATED; 1.
DR   PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199496};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          317..503
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1121 AA;  125058 MW;  0BD4A1596DC38BA4 CRC64;
     MAGPEYTDVE KPFTDQLVGQ GWAFLAGSVD DPAVTHRDSF AQVVMEPLLR EQLRAINLRD
     GEPWLDEGRL DQAVAAITRL PASKVLEANQ QATDLLLNGL SVEGLEGWDG GRGQTLRYID
     WDEPANNVFT VVNQFKVKCP PGHDGAKGHV IPDLVLFVNG IPLVVVECKS RSVPEGISQA
     VDQLRRYHDQ RWLDGEVGEH EGAPALFATT QCLVASNFDD ARVGTVGARF AHYLSWKTVA
     PRREAEVVLD LGVADLSAQQ RLIAGMLTRA NLLDIVRHYT LFMNLGGQTI KLVCRYQQFR
     GVTRAVERLK QGKTRRQDGE ADRRGGIVWH TQGSGKSLSM VFLVRKLRTD PALRRFKVVV
     ITDRKDLQTQ LADTARLTGE SVEKAGNTAE LKTLLARDGP GLVFGTIQKY RDPDAEGEGD
     AYEIPEGRGL DWAHRDVAEP DLLSGNRTPK KPALSAPFEV LNTSEDILIL VDEAHRTQAG
     DLHANMMRAL PNAARIGFTG TPIIMGDKKR THDIFGEYID RYTIQEAEQD GATVPILYEG
     RTAKGAIKDG ASLDGLFEDL FRDHSPEELE AIKKKYATKG QIFEAPQLIR EKAQDILRHY
     VTHILPNGYK AQLVAYSRRA ALRYVEALET ARAELLEEAL ALSPEDKALD DTQLLTRPPR
     VKAAIQSWRH RQVLRQLAFA VVFSSGNNDD PAWARWSDRA AVERHIQRFK KPLPPLDGTP
     PTDASRYDPL AFLIVKSMLL TGFDAPIEGV MYLDRSLREA ELLQAIARVN RTGHGKTHGI
     VVDYFGVANH LKEALAAYSE EDIEGALRSL KDEIPLLRDR HLRVIDVLRG QGVDDLDDTE
     EAVQALADER VRAEFVVKLK AFSRGLDDVL PRPEGLAFVN DAKRLAYIHA LARNRYKDTP
     ELGQDIGNKV RRLIDDYVIS LGIDPRIPPV QLTDAEFDAH LGRQVGDRAK ASEMAHAVRA
     HVRKHMDEDP VKYGRLSERL EALLQQLDGQ WAEQVAALEG LIHQLREGAV IDGEAIPDMP
     THAEPFWREL VASSGLTPES LDAAQANRLL EATEELVARI QQDITIPDFW KPSHIPDQEA
     LRQHLFTTLM IRRLVPFDRA SEVSQRLLDL ARSNHDRLVS A
//
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