ID E6KXZ7_9PAST Unreviewed; 1031 AA.
AC E6KXZ7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
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:EFU67710.1};
GN ORFNames=HMPREF9064_1029 {ECO:0000313|EMBL:EFU67710.1};
OS Aggregatibacter segnis ATCC 33393.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=888057 {ECO:0000313|EMBL:EFU67710.1, ECO:0000313|Proteomes:UP000032871};
RN [1] {ECO:0000313|EMBL:EFU67710.1, ECO:0000313|Proteomes:UP000032871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33393 {ECO:0000313|EMBL:EFU67710.1,
RC ECO:0000313|Proteomes:UP000032871};
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 (DEC-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:EFU67710.1}.
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DR EMBL; AEPS01000005; EFU67710.1; -; Genomic_DNA.
DR RefSeq; WP_006718409.1; NZ_LS483443.1.
DR AlphaFoldDB; E6KXZ7; -.
DR REBASE; 30901; Ase33393ORF1024P.
DR GeneID; 60800420; -.
DR HOGENOM; CLU_004848_1_1_6; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000032871; 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; -; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000032871};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 295..457
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1031 AA; 119524 MW; 57DD14841CAF2018 CRC64;
MTQYKTIAES NHFIVLDQYN KLVEEPNAGY QTEGSLEREF IRDLQAQGYE YLQGLNNHDA
LVKNLRTQLQ RLNNVIFSDA EWRRFLEEYL DKPSDSLIEK TRKIHDDYIY DFVFDNGRIQ
NIYLLDKKNL ANNTLQVINQ FEQTGSYDNR YDVTILVNGL PLVHVELKKR GVAIREAFNQ
IHRYSKESFN KENSLFKYIQ IFVISNGTDT RYFANTTKRD KNSYEFTMNW ATAKNTLIKD
LKDFTATFLQ KHTLLNVLVN YCVFDVSDTL LIMRPYQIAA TERILWKIKS SYLAKNWSNK
ESGGYIWHTT GSGKTLTSFK AARLATELDF IEKVFFVVDR KDLDYQTMKE YQRFSPDSVN
GSENTAGLKR NIDKDDNKII VTTIQKLNNL MKSEDKLPIY DKQVVFIFDE CHRSQFGEAQ
KNLTRKFKKY YQFGFTGTPI FPSNALGAET TASVFGIELH SYIITDAIRD EKVLKFKVDY
NDVRPQFKSI ETEKSLEKLT ALEKKQAFLQ PKRIEQIAQY VLDNFKQKTH RFNAGNHGFN
AMFAVSSVDA AKIYYETFKR LQSAVKNPLK IATIFSFAAN EEQDAIGDIA DESFEVEAMN
STAKEFLKSA IDDYNSYFAT NYDVDGKSFQ NYYRDLAKRV KNKEVDLLIV VGMFLTGFDA
PTLNTLFVDK NLRYHGLIQA YSRTNRIYNS TKSFGNIVTF RDLEQDTIDA ITLFGKSNTR
NVVLEKSYQQ YMEGFTDAGV ACRGYVDIVT ELKEKFPDPS EIQTEKDKKD FVKLFGEYLR
VENILQNYDE FAALQAFQSL DTTDEKAVEA FKEKYYLTDD AFAEMRPIDI PSERNIQNYR
STYNDIRDWL RRQKEGEEKA KSTIDWDDVV FEVDLLKSQE INLDYILELI FEHNKKTKNK
SELIDEIRSI IRASLGNRAK ESLIVDFINQ TDLDNIADKA GIIESFFQFA QKEQQQEADE
LMSSEGLNID AAKRYINVSL KRGYASEQGT DLNDALPKMS PLNPQYLTIK QRIFQKIAAF
VEKFKGIGGN L
//
