ID G4E5C8_9GAMM Unreviewed; 1008 AA.
AC G4E5C8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=ThisiDRAFT_1507 {ECO:0000313|EMBL:EGZ46254.1};
OS Thiorhodospira sibirica ATCC 700588.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thiorhodospira.
OX NCBI_TaxID=765914 {ECO:0000313|EMBL:EGZ46254.1};
RN [1] {ECO:0000313|EMBL:EGZ46254.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700588 {ECO:0000313|EMBL:EGZ46254.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J.,
RA Frigaard N.-U., Bryant D., Woyke T.;
RT "The draft genome of Thiorhodospira sibirica ATCC 700588.";
RL Submitted (SEP-2011) 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:EGZ46254.1}.
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DR EMBL; AGFD01000026; EGZ46254.1; -; Genomic_DNA.
DR RefSeq; WP_006787520.1; NZ_MU255056.1.
DR AlphaFoldDB; G4E5C8; -.
DR STRING; 765914.ThisiDRAFT_1507; -.
DR PATRIC; fig|765914.3.peg.1504; -.
DR eggNOG; COG0610; Bacteria.
DR OrthoDB; 9758243at2; -.
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; 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; 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; 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 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 261..442
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1008 AA; 115661 MW; 3FE0CDB74A6B7F16 CRC64;
MTLTESQIEQ TLIAKLQELK YTYRPDIRDK AALEANFRVQ FEALNQVSLT DTEFARLRDK
IICADVFQAA RQLREIGYFQ REDGSALHYM LVKLKDWCKN HFEVIHQLRI NTDSSHHRYD
VILLLNGLPL VQIELKTLEI TPRRAMEQIV DYKNDPGNGY TNSVLCFMQL FIVSNRNNTY
YFANNHSQHF AFNADERFLP IYQWADQNNR KITHLNDFAE AFLAKCALGQ MLSRYMVLVA
SEQKLLIMRP YQIYAVQAIV DCIHQNRGNG YIWHTTGSGK TLTSFKASTL LKDNPDIEKC
LFVVDRKDLD RQTRLEFNKF QEGCVEENTN TETLVRRLLS EDYADKVIVT TIQKLGLALD
ESSKKALQHK EKGKQTYKER LAPLRDKRLV IIFDECHRSQ FGENHQAIKA FFPKAQLFGF
TGTPIFEENA SHTQIDGTQG TFKTTEDIFQ QQLHAYTITH AIDDRNVLRF HIEYYKPEVR
TEGESAATPK PNQALTQRAI AEAILTKHDA ATNQRRFNAL FATGSINEAI AYYDLFKQLQ
AERKTQTPDY HPLNIACVFS PPAEGNRDVK QLQEDLPQEK ADNQQEPEHK KAALQAIIND
YNAQYGTNHS LSEFDLYYQD VQTRIKDQQY SKKDVPHRLK IDITLVVDML LTGFDSKYLN
TLYVDKNLKH HGLIQAFSRT NRVLNDTKPH GQILDFRAQE QAVDAAIALF SGENTHRSRD
IWLADSAPTV IQKFEAAVQK LEQFMAAHNQ PFTPAAVNNL KGDIARAEFI ECFKAVQRIK
TDLNQYTDLS DAQREQIEQC LPTEIDRGFK GIYIEIAQRL RKKQGKTGND GALPPEIDQL
DFEFVLFSSA LIDYDYIMGL IAQYRQEAPG KETMTREQIV NLLCAHSNLM DEREDIIAYI
DTLNVGKGHG GIEEIKGEYQ VFKTNKSREE LTAIAERHGL DADALHSFFE EIIERGRFDS
EQLSELFAPQ DLGWKARGKA ETALMVELVP VLKKQAGARE ISGLAAYE
//
