ID   T1R2_METJA              Reviewed;        1018 AA.
AC   Q58611;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Putative type I restriction enzyme MjaVIIIP endonuclease subunit {ECO:0000303|PubMed:12654995};
DE            Short=MjaVIIIP {ECO:0000303|PubMed:12654995};
DE            Short=R protein {ECO:0000305};
DE            EC=3.1.21.3 {ECO:0000250|UniProtKB:P08956};
GN   OrderedLocusNames=MJ1214;
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   SEQUENCE REVISION.
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.;
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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'-GAYN(5)GTAA-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; AAB99215.1; -; Genomic_DNA.
DR   PIR; E64451; E64451.
DR   AlphaFoldDB; Q58611; -.
DR   SMR; Q58611; -.
DR   STRING; 243232.MJ_1214; -.
DR   REBASE; 3903; MjaVIIIP.
DR   EnsemblBacteria; AAB99215; AAB99215; MJ_1214.
DR   KEGG; mja:MJ_1214; -.
DR   eggNOG; arCOG00878; Archaea.
DR   HOGENOM; CLU_005762_0_0_2; -.
DR   InParanoid; Q58611; -.
DR   OMA; KQYEAGM; -.
DR   PhylomeDB; Q58611; -.
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; -; 2.
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..1018
FT                   /note="Putative type I restriction enzyme MjaVIIIP
FT                   endonuclease subunit"
FT                   /id="PRO_0000107217"
SQ   SEQUENCE   1018 AA;  120993 MW;  97D383541BE128E2 CRC64;
     MNKMPIPEIY VHNDIEENLN KLGWKELEGY EGEAFSNYII KPILEEQLKI INDHIGEYKD
     EFIEKAINKL INEPKPEEIL DYIKNGILIT LDKGRKGQVS NRVKLIDYKN IEKNIFNYAH
     ELKFKGNDNI IPDFTLFING IPIIIIEAKR EFSEKETYEE AINQINRYER EAPKLFNYVQ
     FAIVYGDEKL YIPTYPNEEK EDRFKKPYKW KNEKKEEDIW DLLKRERVLD TIKNFIFFSK
     DRAGRKTKII PRYMQYWAVK KAYERITNYL NNKDYKNRGL VWHWQGSGKT FEILYLAELF
     YNEFKNKDPI VFIMVDRREL ETQFNDDIIA LQNANFKDCF KKINSVEELK GVLEDIKESE
     NNPNISEKGV YLVMMHKFDK NKLKDFIESF GSIDKKEILI LRDEAHRTES GKFATLRNKI
     LKNAIAIGFT GTPVHKKDMS TFKEYAYPQE GEFYLDRFFI EESIKEGFTL PLIWRVVKPE
     DIKDISEEEI KNIIEKLFVD EEDADKIVVS KKEIAEKIKL SDLLKSESSI KEASKYIAEH
     ILEDTENFKF KAMVVAQDRK SCILFKKYLD EYLKEKIKNY NENWTQVVIT YIHNDDVEIE
     NYKKEIEKKY GKNVDELNKK WTEDFINKEN PKILIVNKKL LTGFDAPILK TIYIHQFLKD
     YLLLQASARA NRPAKNKKYG LIVDLTGILI ENYKKAIENY NLYRDEAINK DILNNLFVET
     SKIWESFLTK LNEFKELFKL IVGIEFDDFI VNLKKQKNSK EFKKIISKII LSDKFDYFYA
     KLRELIQLFE AVGAYGEKLN YYETYEWLKI ISAGINKQMR PKSYKIPYNQ IKKEVIKYLE
     FDTYADIAST SINPQLLENL KNKDEINVIV ADMIYYALDT LQNKKEPIYR MIYDRINELK
     NAYISKTKKN EYVINELINC LNALKTYEEE EKTLSKSEKA IKNMLFYLKN VENCNIKKLP
     LTEKTLKNLE DKKLIKPSDF DKIKKFLFVD LKNAIKETEK RRKVSNKIVE EIIKPIFI