ID   T1R1_METJA              Reviewed;        1075 AA.
AC   Q57588;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Putative type I restriction enzyme MjaVIIP endonuclease subunit {ECO:0000303|PubMed:12654995};
DE            Short=MjaVIIP {ECO:0000303|PubMed:12654995};
DE            Short=R protein {ECO:0000305};
DE            EC=3.1.21.3 {ECO:0000250|UniProtKB:P08956};
GN   OrderedLocusNames=MJ0124;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   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., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   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).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=12654995; DOI=10.1093/nar/gkg274;
RA   Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA   Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA   Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA   Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA   Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA   Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA   Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA   Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA   Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT   "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT   endonucleases and their genes.";
RL   Nucleic Acids Res. 31:1805-1812(2003).
CC   -!- FUNCTION: The restriction (R) subunit of a type I restriction enzyme
CC       that recognizes 5'-CAAN(7)TGG-3' and cleaves a random distance away.
CC       The R subunit is required for both endonuclease and ATPase activities
CC       but not for modification. After locating a non-methylated recognition
CC       site, the enzyme complex serves as a molecular motor that translocates
CC       DNA in an ATP-dependent manner until a collision occurs that triggers
CC       cleavage. {ECO:0000250|UniProtKB:P08956, ECO:0000303|PubMed:12654995}.
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:0000250|UniProtKB:P08956};
CC   -!- SUBUNIT: The type I restriction/modification system is composed of
CC       three polypeptides R, M and S. {ECO:0000250|UniProtKB:P08956}.
CC   -!- MISCELLANEOUS: Type I restriction and modification enzymes are complex,
CC       multifunctional systems which require ATP, S-adenosyl methionine and
CC       magnesium as cofactors and, in addition to their endonucleolytic and
CC       methylase activities, are potent DNA-dependent ATPases.
CC       {ECO:0000250|UniProtKB:P08956}.
CC   -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000305}.
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DR   EMBL; L77117; AAB98104.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q57588; -.
DR   STRING; 243232.MJ_0124; -.
DR   REBASE; 154995; VscVS12ORF1031P.
DR   REBASE; 191862; Apa1447ORF2453P.
DR   REBASE; 191879; Apa1468ORF2954P.
DR   REBASE; 191891; Apa1468ORF2715P.
DR   REBASE; 203827; Bli141ORF4598P.
DR   REBASE; 203830; Bli27ORF807P.
DR   REBASE; 3900; MjaVIIP.
DR   PRIDE; Q57588; -.
DR   EnsemblBacteria; AAB98104; AAB98104; MJ_0124.
DR   KEGG; mja:MJ_0124; -.
DR   eggNOG; arCOG00878; Archaea.
DR   HOGENOM; CLU_005762_0_0_2; -.
DR   InParanoid; Q57588; -.
DR   OMA; FFIANYF; -.
DR   PhylomeDB; Q57588; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009035; F:type I site-specific deoxyribonuclease activity; IEA:InterPro.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 3.
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.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Endonuclease; Helicase; Hydrolase; Nuclease;
KW   Nucleotide-binding; Reference proteome; Restriction system.
FT   CHAIN           1..1075
FT                   /note="Putative type I restriction enzyme MjaVIIP
FT                   endonuclease subunit"
FT                   /id="PRO_0000106704"
SQ   SEQUENCE   1075 AA;  127797 MW;  4F765E19E0B52889 CRC64;
     MDYLKYGIEV VVKKSEKRKF KLIDYKNIDK NTFFYLCEAE FKGNPKNSRP DITLFINGIP
     VVIIEAKATL KIDSHLEGIS QIRRYEKFSP DLFRFVQFAI SYGEEQLYTP TMPNWYKENI
     HLPAYYWRIR QKINGKKVVK DDIFYILNPS ILLEIIRYFI FYRKDEYSKT KTLSKIIARY
     NQYFATKKAM KRIDEYLSGD SKNKGLIWHW QGSGKTYTMF FIANYFLDKY FSENPVIFFV
     VDRVDLERQS KEFYEAIQEK KFKTILKRID SINKLYEVIK SIKMSELSNK VIVRGIYTTT
     IQKFQYERSK KEKDNNKEKD KDDEDLDLSK PIEEIIKKIE DKLKKEEKEG KIKGLKDLLI
     ILAFIYLKHL KEKNPEEYKK HIENLKKLKD KDKKEEYLIN LGNIKRKHIL ILIDEAHRTQ
     YGILGGMRKI TFPNAITFGF TGTPVFKNEK NTFTEFSYPE KGEFYLDVYF IGDSIKDKFT
     LPLTYQIVKE GDIKSEGIQI TLDEEDIKEF IDEWIKRGED INLFDRKKLP KYINKSKTIL
     LNPKRIDKVA KYIVDRIEED TENFKFKAMV VAVNRLGCVR FKKALDKYLK EKFGDEAEKW
     AEVVMTYHHN EEEKEIIEYM KKLKKERNSN DFNEINQIIR EEFLNSENPK ILIVTDMLLT
     GFDAPRLKVM YLDKPLYGHR LLQAIARTNR PYPDKEFGLI VDSVGLFKVL TETMALYNML
     AEEEIREDFK NNLISSIDEI FQEFKLKLEM VKESLKNLKI NDEDLSIDVN TLKTLTKNKD
     FNNNELKEKL DLIAFYAEDG KNARILKLID DLKAVIKLYK ALGSYPQKIF YIEDIELLSF
     IYAYLIKKLK PKKKSNRKFW EELISFIHNK MLVDDLTVIE EINLNPDDLD KILKENIGKR
     EIKRAVANYY FILKNSILDK QHDPIYKEIL ERLERLRRDW IMKRIDDKIY LNAIKNLMEL
     KNNYDKKIKG KSSIERIKES ISTYIGENIL KDQDIKLNLE NTEKLITKMQ NLNKLSKLQR
     KKFKKELSCA LLEDLLKELK GKIKDEDAKK VAELSDNLVS EFILKEIWGE NYENQ