ID Q8EJT2_SHEON Unreviewed; 1033 AA.
AC Q8EJT2;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 127.
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:AAN53463.1};
GN OrderedLocusNames=SO_0380 {ECO:0000313|EMBL:AAN53463.1};
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN53463.1, ECO:0000313|Proteomes:UP000008186};
RN [1] {ECO:0000313|EMBL:AAN53463.1, ECO:0000313|Proteomes:UP000008186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1 {ECO:0000313|EMBL:AAN53463.1,
RC ECO:0000313|Proteomes:UP000008186};
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J.,
RA Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J.,
RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C.,
RA Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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}.
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DR EMBL; AE014299; AAN53463.1; -; Genomic_DNA.
DR RefSeq; NP_716018.1; NC_004347.2.
DR RefSeq; WP_011070740.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EJT2; -.
DR STRING; 211586.SO_0380; -.
DR REBASE; 6514; SonIIP.
DR PaxDb; 211586-SO_0380; -.
DR KEGG; son:SO_0380; -.
DR PATRIC; fig|211586.12.peg.371; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_005762_0_0_6; -.
DR OrthoDB; 9758243at2; -.
DR PhylomeDB; Q8EJT2; -.
DR BioCyc; SONE211586:G1GMP-364-MONOMER; -.
DR Proteomes; UP000008186; Chromosome.
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; 3.90.1570.50; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 InterPro; IPR021810; T1RH-like_C.
DR NCBIfam; TIGR00348; hsdR; 1.
DR PANTHER; PTHR30195:SF15; TYPE I RESTRICTION ENYME HINDI ENDONUCLEASE SUBUNIT; 1.
DR PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF18766; SWI2_SNF2; 1.
DR Pfam; PF11867; T1RH-like_C; 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, ECO:0000313|EMBL:AAN53463.1};
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:UP000008186};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 325..497
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1033 AA; 116967 MW; 6FA78AB03CC49FED CRC64;
MDQDELHKVE LPAIAQLSLL GWQYVAGAKL TPEYHERPYL RDVVLVGRLE AAIKRINPWI
NDENLRKVCR DITHPNFVGL MEYNQAIYQT LVNYLSVEQD VGKGRKGQTV KLIDFDNLAA
NEFICTSQFK VEGVNQNIIP DIVCFINGLP LAVIECKSPY ISAPISEGIN QLRRYANLRN
SVDDEGAQRL FWYNQLMVST CRDQAKVGTI SSNASHYADW KDAYPFTDTT LSEQNLSQAF
SRNSLDDMQV NDNPALYTAT SSNYDAITAV TAQQRLIAGI FSPASFLDIL QNFIIFEPVE
GKLIKKVARY QQYRAVNKVI ERLKTGQDRK EKSGVVWHTQ GSGKSLTMVM LAVKMRRDPV
LKQYKLVFIT DRTQLDEQLS STFRAAQGET IYNAGSVAEL KALLKKDSSD LVTAMVQKFL
DLEKELSTNN ENEGFINLNP SDKIIVLADE AHRTQFGGLA MTINAALPNA PKIGFTGTPL
LKTQKMDKAF GGYIDEYKIN QAVDDGATVR ILYEGRQVKT EVAGESLDKL FEAYFGSYSK
EEQREIKQKY GVERAVREAP ARIRWVCMDL LEHYRKHIQP DGFKAMIVVG SRHAATIFKK
TLDELGAPPS EVIISGYHND EAYIAVHTDK TKQKKIIQDF TKPLSENPVA FLIVKDMLLT
GFDAPIAQVM YIDRKLQDHT LMQAIARVNR TYAKKECGFI VDYFGLSNHL IEAMEMFSSD
DVEGTYQSLK DEIPKLKATH TLAISFFRHI KNKDVDSYVL ALKEETVRAQ FDMAFKRFAK
QMNIVLPDVA AAPFLADMKL LGKVHNSARN QYRDAGLDMT DIGAKVRKLV DEHILSTGVD
PKIPPIDLLA ANFKESIRPE KSAESKASEI ESAIKHHITV KLEEDPEYYK SLSLRLRDII
EKTAGQWEQQ LELLLAMVDT IEIDRRRAAK DAGLSETEFA FYNILTAEVT QTSDIEVIDE
HQLIEIKTIT QNLVAMFDEA TQIVDFFNKG DEIKRLKKEI KRAVIDASFS NVELISNLQD
RFMELAKHKF NKQ
//
