ID A0A2H9U6U3_9GAMM Unreviewed; 1049 AA.
AC A0A2H9U6U3;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ORFNames=CUC53_05990 {ECO:0000313|EMBL:PJG59708.1};
OS Aeromonas cavernicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1006623 {ECO:0000313|EMBL:PJG59708.1, ECO:0000313|Proteomes:UP000235861};
RN [1] {ECO:0000313|EMBL:PJG59708.1, ECO:0000313|Proteomes:UP000235861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDC 2508 {ECO:0000313|EMBL:PJG59708.1,
RC ECO:0000313|Proteomes:UP000235861};
RA Colston S.M., Navarro A., Martinez-Murcia A.J., Graf J.;
RT "Draft genome sequence of environmental isolate Aeromonas cavernicola sp.
RT nov. MDC 2508.";
RL Submitted (NOV-2017) 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:PJG59708.1}.
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DR EMBL; PGGC01000050; PJG59708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9U6U3; -.
DR REBASE; 260718; Aca2508ORF6015P.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000235861; 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:0004386; F:helicase activity; 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; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Helicase {ECO:0000313|EMBL:PJG59708.1};
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 Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 303..486
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 510..541
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1049 AA; 117199 MW; B80BEF05A6D317F6 CRC64;
MLNEQQLEEL CIGWFQEAGW RFAHGPDIAP DSSAPERTDY RQVVLRERLL TTLARINPHM
PPSALDQAVH ALLSVSEPQM VVRNRSVHRL LLSGVMVEFA QGDEKKSDLV HFIDFAQPSN
NDFLVVNQFT ITGTKQPRRP DVIAFVNGLP LAVVELKNPA NEQTDVWDAF NQLQTYKDEI
GDLFNSNAAL VVSDGWTARV GSLTANAERM LPWRTIANED DRPRLQMELE TVVRGFFKPE
LFLDYVRHFV LFEQDGDAII KKIAGYHQFH AVREAVRATV IATQEADKGL PAVDEERATY
GKVVKPGSRK AGVVWHTQGS GKSITMACYA GKLLQQPEMK NPTLVVVTDR NDLDGQLFAT
FSAASDLLKT IPVQAGDRDE LREMLASREA GGIIFTTVQK FALLEDEETH PLLSGRTNIV
VISDEAHRSQ YGTKGRLDTK TGKYVFGYAK HLRDALTNAT FIGFTGTPIA LEDKDTRAVF
GDYVSIYDIQ DAVDDGATVP IFYESRLAKL DVNQAEIDTL NEQVEEVVED EEDIANREKT
KSEWAALEKL VGSEPRLQQV ARDLIQHFEA RVSVVDGKAM IVSMSRDICA QLYNAIVALR
PEWHSSDPDK GAIKIVMTGS AADKPLLQPH LYSKQVKKRL EARFKDVSDP LRLVIVRDMW
LTGFDAPCCH TMYIDKPMKG HNLMQAIARV NRVFKNKPGG LVVDYIGIAN ELKAALKTYT
DAKGKGDPTH NAAEALAVLL EKMDILRGMM HGFDYGAFET QAIPLLVPAA NHILGLKDGK
TRFLDTMVAV AKAFSLCGTL DEAGALRKEI AFFSAIKAAI AKFTTVDKKR SDAEKNSALK
QILDNAIISD GVADVFALAG LDKPNIGLLS DEFLEDVRQM DSRNLAVELL EKLLRDEIKA
RTRNNVVQEK KYGDRLLETL RKYHNRAIET AQVIEELIQM AKEFQATLAR EVALGLGHDE
IAFYDALANN ESAVRELGDE VLKKIATEIT EKLRASTTVD WQVRESVRAK LRILVRRCLQ
KWRYPPDQQP DAIEMVLKQA EVLSNAWSQ
//
