(data stored in ACNUC1104 zone)

SWISSPROT: D3VG21_XENNA

ID   D3VG21_XENNA            Unreviewed;      1029 AA.
AC   D3VG21;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   10-APR-2019, entry version 55.
DE   RecName: Full=Type I restriction enzyme R Protein {ECO:0000256|RuleBase:RU364115};
DE            EC=3.1.21.3 {ECO:0000256|RuleBase:RU364115};
GN   Name=hsdR {ECO:0000313|EMBL:CBJ88111.1};
GN   OrderedLocusNames=XNC1_0018 {ECO:0000313|EMBL:CBJ88111.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88111.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88111.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Subunit R is required for both nuclease and ATPase
CC       activities, but not for modification.
CC       {ECO:0000256|RuleBase:RU364115}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of DNA to give random double-
CC         stranded fragments with terminal 5'-phosphates, ATP is
CC         simultaneously hydrolyzed.; EC=3.1.21.3;
CC         Evidence={ECO:0000256|RuleBase:RU364115};
CC   -!- SUBUNIT: The type I restriction/modification system is composed of
CC       three polypeptides R, M and S. {ECO:0000256|RuleBase:RU364115}.
CC   -!- SIMILARITY: Belongs to the HsdR family.
CC       {ECO:0000256|RuleBase:RU364115}.
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DR   EMBL; FN667742; CBJ88111.1; -; Genomic_DNA.
DR   RefSeq; WP_013183038.1; NC_014228.1.
DR   STRING; 406817.XNC1_0018; -.
DR   REBASE; 26663; XnePORF20P.
DR   EnsemblBacteria; CBJ88111; CBJ88111; XNC1_0018.
DR   KEGG; xne:XNC1_0018; -.
DR   eggNOG; ENOG4105DZR; Bacteria.
DR   eggNOG; COG0610; LUCA.
DR   HOGENOM; HOG000063409; -.
DR   KO; K01153; -.
DR   OMA; KCARFHQ; -.
DR   Proteomes; UP000008075; 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   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR   InterPro; IPR004473; Restrct_endonuc_typeI_HsdR.
DR   InterPro; IPR040980; SWI2_SNF2.
DR   Pfam; PF04313; HSDR_N; 1.
DR   Pfam; PF18766; SWI2_SNF2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00348; hsdR; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VG21.
DR   SWISS-2DPAGE; D3VG21.
KW   ATP-binding {ECO:0000256|RuleBase:RU364115};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   DNA-binding {ECO:0000256|RuleBase:RU364115};
KW   Hydrolase {ECO:0000256|RuleBase:RU364115,
KW   ECO:0000313|EMBL:CBJ88111.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364115};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   Restriction system {ECO:0000256|RuleBase:RU364115}.
FT   DOMAIN      262    427       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   COILED      800    820       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1029 AA;  118605 MW;  4048ACDC38FC7132 CRC64;
     MSTVGQRERV TQDRIVKFFQ TELGYRYLGN LQDRDNKNID VDILTAWLKK QGISGTLIGR
     VLRQLINTAA LGDGNKLYYA NKDVYNLLRY GIKEKEDVGE QHQTIWLINW HNPEANDFAI
     AEEVSIKGEN KKRPDIVLYV NGIALGIIEL KRSSVSVSEG IRQNLDNQKK EFIRDFFSTM
     QLVMAGNDTQ GLRYGTIGTP EKYYLEWKEG IDNPYPYRLD FHLSRICSKP RFLQLIHDFI
     VFDAGVKKAC RHNQFFGVEA AKKRIFQREG GIIWHTQGSG KSLTMVWLAK WIRENVPNSR
     VLIVTDRTEL DAQIEKVFTG VEENIYRTKS GADLIFNLNR PNPWLICSLV HKFGHRSEAE
     DDAATDEYIK ELKKSLPSDF RAKGDLFVFV DECHRTQSGK LHDAMKSILP EAVFIGFTGT
     PLMKKDKKKS IEVFGSFIHT YKFDEAVSDG VILDLRYEAR DIDQYLTSQK RIDEWFEANT
     QGLSRLGKTQ LKQKWGTMQK VLSSKSRLEM IVMDIRLDMM KRPRLMDGRG NAMLVCSSIH
     QACTVYDLFS QTDLAGKVAI ITSYKPDSAS IKGEETGEGL TEQLAKYKTY RKMLADYFEQ
     PEDKVANRVE EFETKVKQQF IDEPGQMRLL IVVDKLLTGF DAPSATYLYI DKHMSDHNLF
     QAICRVNRLD GDDKEYGYII DYKDLFRSLN KAISDYTKEV FDGYDKKDID GLLKNRLEQA
     RLNLDAALEM VRALCEPVKA PRNTVDYIHY FCCESGADPE LLSEKEALRL ALYQCVAKLL
     RAFANIANEM TIAGYSPAQM EKIRAEVAHY EKVRDEIKLA SKDKVEMKRY EPAMRSLIDM
     YIRADDSEVL MDFEEIGLLE LIIQKGAAAG EDLPEGIRKD PEAMAETIEN NVRKTIVDEN
     PVNPRYYEHM SVLLDELIAL RRQNALNYQE YLEKIRDLAK KVVRPNQNTA AYPPDIDTPP
     KRAFYDNFDQ NTDLAICIDK TIRDTKKADW VNDRFKEREI ANALRDETAE YKVDIDKIME
     LAKTQRDYR
//

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