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   03-AUG-2022, entry version 134.
DE   RecName: Full=Putative type I restriction enzyme MjaIXP endonuclease subunit {ECO:0000303|PubMed:12654995};
DE            Short=MjaIXP {ECO:0000303|PubMed:12654995};
DE            Short=R protein {ECO:0000305};
DE            EC=3.1.21.3 {ECO:0000250|UniProtKB:P08956};
DE   AltName: Full=Putative type-1 restriction enzyme MjaXP R protein;
GN   OrderedLocusNames=MJECL40;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OG   Plasmid large ECE.
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'-CCAN(5)GTR-3' and cleaves a random distance away.
CC       The R subunit is required for both nuclease and ATPase activities, but
CC       not for modification. After locating a non-methylated recognition site,
CC       the enzyme complex serves as a molecular motor that translocates DNA in
CC       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; L77118; AAC37109.1; -; Genomic_DNA.
DR   PIR; G64514; G64514.
DR   AlphaFoldDB; Q60295; -.
DR   SMR; Q60295; -.
DR   STRING; 243232.MJ_ECL40; -.
DR   REBASE; 191891; Apa1468ORF2715P.
DR   REBASE; 3908; MjaIXP.
DR   EnsemblBacteria; AAC37109; AAC37109; MJ_ECL40.
DR   KEGG; mja:MJ_ECL40; -.
DR   eggNOG; arCOG00878; Archaea.
DR   HOGENOM; CLU_005762_1_0_2; -.
DR   InParanoid; Q60295; -.
DR   OMA; KCARFHQ; -.
DR   PhylomeDB; Q60295; -.
DR   PRO; PR: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:0004386; F:helicase activity; 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   Gene3D; 3.40.50.300; -; 3.
DR   InterPro; IPR014001; Helicase_ATP-bd.
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   InterPro; IPR021810; T1RH-like_C.
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; DNA-binding; Endonuclease; Helicase; Hydrolase; Nuclease;
KW   Nucleotide-binding; Plasmid; Reference proteome; Restriction system.
FT   CHAIN           1..1042
FT                   /note="Putative type I restriction enzyme MjaIXP
FT                   endonuclease subunit"
FT                   /id="PRO_0000077273"
FT   DOMAIN          323..487
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          551..731
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           439..442
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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