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Database: UniProt
Entry: Q60295
LinkDB: Q60295
Original site: Q60295 
ID   T1RH_METJA              Reviewed;        1042 AA.
AC   Q60295;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   13-NOV-2019, entry version 125.
DE   RecName: Full=Putative type-1 restriction enzyme MjaXP R protein;
DE            EC=3.1.21.3;
DE   AltName: Full=Putative type I restriction enzyme MjaXP R protein;
GN   OrderedLocusNames=MJECL40;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 /
OS   JCM 10045 / NBRC 100440) (Methanococcus jannaschii).
OG   Plasmid large ECE.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci;
OC   Methanococcales; Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D.,
RA   Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D.,
RA   Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I.,
RA   Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A.,
RA   Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D.,
RA   Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C.,
RA   Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M.,
RA   Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Subunit R is required for both nuclease and ATPase
CC       activities, but not for modification. {ECO:0000250}.
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   -!- SUBUNIT: The type I restriction/modification system is composed of
CC       three polypeptides R, M and S. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000305}.
DR   EMBL; L77118; AAC37109.1; -; Genomic_DNA.
DR   PIR; G64514; G64514.
DR   STRING; 243232.MJ_ECL40; -.
DR   REBASE; 191879; Apa1468ORF2954P.
DR   REBASE; 191891; Apa1468ORF2715P.
DR   REBASE; 3908; MjaORFCL42P.
DR   PRIDE; Q60295; -.
DR   EnsemblBacteria; AAC37109; AAC37109; MJ_ECL40.
DR   KEGG; mja:MJ_ECL40; -.
DR   HOGENOM; HOG000240457; -.
DR   InParanoid; Q60295; -.
DR   KO; K01153; -.
DR   OMA; KCARFHQ; -.
DR   PhylomeDB; Q60295; -.
DR   Proteomes; UP000000805; Plasmid large ECE.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR021810; DUF3387.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011254; Prismane-like_sf.
DR   InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR   InterPro; IPR004473; Restrct_endonuc_typeI_HsdR.
DR   InterPro; IPR040980; SWI2_SNF2.
DR   Pfam; PF11867; DUF3387; 1.
DR   Pfam; PF04313; HSDR_N; 1.
DR   Pfam; PF18766; SWI2_SNF2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF56821; SSF56821; 1.
DR   TIGRFAMs; TIGR00348; hsdR; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; DNA-binding; Hydrolase;
KW   Nucleotide-binding; Plasmid; Reference proteome; Restriction system.
FT   CHAIN         1   1042       Putative type-1 restriction enzyme MjaXP
FT                                R protein.
FT                                /FTId=PRO_0000077273.
FT   DOMAIN      323    487       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      551    731       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
SQ   SEQUENCE   1042 AA;  121523 MW;  3C8E5A103E7B59D3 CRC64;
     MPISANKYFL LVGVFIGDKM KKEAAKLNED YVVENAAIQR LKNLGYSYKH GSELTPEYNE
     RESYRDAILK NRFIKAIKNI NPWLTEELAL KVYKTVTNID NPDFNMRGKI FYEMLINGVK
     LEFKENGEKK TRFVKLIDFE NINKNEFLVA NQFEVEYYYE NGRFRRPDLV VFINGIPIAI
     FEFKSPKSNQ TAKDAFNDHK TKMKDIPQLY QYAQILVVSD GLETKYGSPT SDWDRFFVWE
     GVESDDDVEV IEVDNYGNTM YKYKGNPYTS LDILLMGLFK KEHLIEFLED FIIHDKKKII
     ATYYQFYTVK KAVDRTIKSV LYGETPEDRR IGIVWHAQGT GKSITMLFYA KKALKQKELN
     YPLLVFLTDR LELDEQLYNV FSSVFSEAER AESIAELQEL IKKTPGGIIF ATIQKFGRKS
     KDEHYPFLTD RNNIIIIADE AHRSHYGTLA QNLRKAIPNA SFLAFTATPI DYKDRSTFLV
     FGDYISAYPI DKAKRHGVVV PIYYEARLVE LHLTNEFIDL EFDEISERVA NDPETKESIK
     EVFAKLEKIM LTEDYLSKVS KDIIEHFNKR LQDFDGKAMV VTISRKVAVE LYKWITKQPN
     APKIAVVMSG NKSKDPEDFH PHIRTKKELE NLAKEFKDPE SDLKMVIVVD MWLTGFDVPC
     LHTMYFLKPM KNHSLAQAIA RVNRVFKDKP GGLIVDYIGI ADDLSKSLSK YSSEARKDLM
     TDIKVVIEEM KRRYEKVTSY FKNINYKDWK KLSSEDLSLL TVKAYQRVAK DDNTKKEFVR
     NVIALKKLYL LARPHPETIG IKDDLEFFEM IKKMIVKYST KKIREISQDL ENDIQSLISK
     SISAKELVDV FEMLKKEKPE LSVLSDEFLS EIAKIEYKDY VRDVLIKILN DDIRVRMAKN
     PIRFKKFSER LNEVIEKYRI KVITTAEMIE ELVNLAKEIR KAAEEGKELG LTEEELAFYD
     LLLSYPNIPL TDKKRVEKIA KEIARMMSGY IKARDWKKKK NLQSKIRAKL KIILMKEGIK
     DYSLINKISD DLFEYAKNIY AI
//
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