ID E0N9T6_NEIME Unreviewed; 910 AA.
AC E0N9T6;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Type I restriction enzyme endonuclease subunit {ECO:0000256|RuleBase:RU364115};
DE Short=R protein {ECO:0000256|RuleBase:RU364115};
DE EC=3.1.21.3 {ECO:0000256|RuleBase:RU364115};
GN Name=hsdR {ECO:0000313|EMBL:EFM04258.1};
GN ORFNames=HMPREF0602_1266 {ECO:0000313|EMBL:EFM04258.1};
OS Neisseria meningitidis ATCC 13091.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=862513 {ECO:0000313|EMBL:EFM04258.1, ECO:0000313|Proteomes:UP000005526};
RN [1] {ECO:0000313|EMBL:EFM04258.1, ECO:0000313|Proteomes:UP000005526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13091 {ECO:0000313|EMBL:EFM04258.1,
RC ECO:0000313|Proteomes:UP000005526};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit R is required for both nuclease and ATPase
CC activities, but not for modification. {ECO:0000256|RuleBase:RU364115}.
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:0000256|ARBA:ARBA00000851,
CC 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. {ECO:0000256|ARBA:ARBA00008598,
CC ECO:0000256|RuleBase:RU364115}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFM04258.1}.
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DR EMBL; AEEF01000065; EFM04258.1; -; Genomic_DNA.
DR AlphaFoldDB; E0N9T6; -.
DR REBASE; 42977; Nme13091ORF1271P.
DR HOGENOM; CLU_004848_1_0_4; -.
DR Proteomes; UP000005526; Unassembled WGS sequence.
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 CDD; cd18030; DEXHc_RE_I_HsdR; 1.
DR CDD; cd22332; HsdR_N; 1.
DR CDD; cd18800; SF2_C_EcoR124I-like; 1.
DR Gene3D; 1.10.10.2110; -; 1.
DR Gene3D; 1.20.58.2040; -; 1.
DR Gene3D; 3.90.1570.50; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 InterPro; IPR022625; TypeI_RM_Rsu_C.
DR NCBIfam; TIGR00348; hsdR; 1.
DR PANTHER; PTHR30195:SF16; TYPE I RESTRICTION ENZYME ENDONUCLEASE SUBUNIT; 1.
DR PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR Pfam; PF12008; EcoR124_C; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF18766; SWI2_SNF2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364115};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364115};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364115};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 161..323
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 910 AA; 104369 MW; 491D37AE62F29A50 CRC64;
MQLINQFEQT GTHANRYDVT VLVNGLPLVQ IELKKRGVAV REAFNQVHRY SKESFNSENS
LFKFLQIFVI SNGTDTRYFA NTTKRDKNSF DFTMNWARSD NHPIKDLKDF TATFLQKSVL
LSVLLHYSVF DANDTLLIMR PYQIAAAERI LWKINSSAQV KNWSKPESGG YIWHTTGSGK
TLTSFKAARL ATESAFIDKV FFVVDRKDLD YQTMKEYQRF SPDSVNGSES TAGLKRNLEK
DDNKIIVTTI QKLNNLMKSE DNLPVYHQQV VFIFDECHRS QFGEAQKNLK KKFKKFCQFG
FTGTPIFHDH IVDGKLIMKG NALGSESTES VFGRQLHSYV ITDAIRDEKV LKFKVDYNDV
RPQFKAVEAE QDEKKLSAAE NRQALLHPER IREITQYILN QFRQKTHRLN AGGKGFNAMF
AVSSVDAAKC YYEAFKTQQA GSLHPLKVAT IFSFAANEEQ NAVGEIVDET FEPEAMDSSA
KEFLQAAIND YNACFKTNFG TDSKSFQNYY RDLAKRVKNQ EVDLLIVVGM FLTGFDAPTL
NTLFVDKNLR YHGLMQAFSR TNRIYDATKT FGNIVCFRDL EQATIDAITL FGDKNTKNVV
LEKSYEEYMN GYTDSQTGEA RRGYLDVAKE LRQRFPDPDK IETEKDKKDF AKLFGEYLRA
ENVLQNYDEF AALRELQSVD AADEDAMKAF QEKYYLSDED VQEMRQVPMP SERAVQDYRS
AYNDIRDWLR RQKAGEQKEQ SKIDWDDVVF EVDLLKSQEI NLDYILQLVF EHHKKIKGKA
ELVEEIRRII RASIGHRAKE GLIVDFINDT DLDKVPDVPA ILETFYTYGQ EVMRHEAAGL
IVAEGLNETA AKRYLTGSLK RGYASENGTE LTETLPKMSP INPQYLTKKQ SVFQKIAAFV
EKFAGIGTDI
//
